|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-526 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 1130.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQYS 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VVDAVIMGDVELWKVKQERDRIYSLPEMSEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 161 KLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKF 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 241 LEAAGLQREQLLAENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDEVKASSRMSPSLSFDEGKKMYRQAL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 321 EVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKDFDNDLT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 LFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNA 480
Cdd:PRK15064 401 LFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1180383029 481 LKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGTFDEYLAS 526
Cdd:PRK15064 481 LEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRS 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-525 |
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: 705.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQYSVVDAV 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 IMGDVELWKVKQERDRIYSLPEMSEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVL 165
Cdd:COG0488 83 LDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 166 LAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKFLEAAG 245
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 246 LQREQLLAENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDEVKASSRmSPSLSFDEGKKMYRQALEVNKL 325
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELEGL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 326 GHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDStKDFDNDLTLFDWM 405
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 406 SQWRTAKhNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFA 485
Cdd:COG0488 401 RDGAPGG-TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1180383029 486 GTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGTFDEYLA 525
Cdd:COG0488 480 GTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-531 |
4.03e-85 |
|
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: 273.73 E-value: 4.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQYSVVDAVIMGDVELWK 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 95 VKQERDRIYSLpeMSEEDgmkvADLESVFAEM----------DGYTAESRAEeILLEAgidkefhygLM-----ANVAP- 158
Cdd:TIGR03719 99 ALDRFNEISAK--YAEPD----ADFDKLAAEQaelqeiidaaDAWDLDSQLE-IAMDA---------LRcppwdADVTKl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 --GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGN 236
Cdd:TIGR03719 163 sgGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 237 YEKFLEaaglQREQLLAENAKKSAE----IDELQDFVNRfganASKAKQASSRAKkmdkIKLDEVKASSRMSPSLSFDE- 311
Cdd:TIGR03719 243 YSSWLE----QKQKRLEQEEKEESArqktLKRELEWVRQ----SPKGRQAKSKAR----LARYEELLSQEFQKRNETAEi 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 312 ----GKKMYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYC 387
Cdd:TIGR03719 311 yippGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQdSTKDFDNDLTLFDWMSQwrtakHNDLMV--------RGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:TIGR03719 391 DQ-SRDALDPNKTVWEEISG-----GLDIIKlgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 460 LVMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIK-DKQVIDFQGTFDEYlasIEEKK 531
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY---EEDKK 534
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-523 |
3.40e-82 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 268.58 E-value: 3.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQyS 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VVDAVIMGDVELWKVKQErdriysLPEMSEE-DGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEK 239
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 240 F--LEAAGLQREQLLAENakKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLdeVKASSRMSP-SLSFDEGKKMY 316
Cdd:PRK10636 234 FevQRATRLAQQQAMYES--QQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPfHFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 317 RQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKDFD 396
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 397 NDLTLFDWMSqwRTA-KHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIE 475
Cdd:PRK10636 390 ADESPLQHLA--RLApQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1180383029 476 ALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGTFDEY 523
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-503 |
4.41e-78 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 257.57 E-value: 4.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQYS 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VVDAVIMGDVELWKVKQERDRIYSLPEMSEEDGM--KVADLESVFAEMDGYTAESRAEEILLEAGIDKEfhyGLMANVAP 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYE 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 239 KFLEAaglqREQLLAENAKKSAEIDE--LQDFV-NRFGANASKAK-QASSRAKK---MDKIKLDEVKASSRMSPSLSFDE 311
Cdd:PRK11147 240 QYLLE----KEEALRVEELQNAEFDRklAQEEVwIRQGIKARRTRnEGRVRALKalrRERSERREVMGTAKMQVEEASRS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 312 GKKMYrqalEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQdS 391
Cdd:PRK11147 316 GKIVF----EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQ-H 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 392 TKDFDNDLTLFDWMSQWRtakhNDLMVRG----MLGRL---LFtaddSNKKARN----CSGGEKNRLLFGKLMMQDVNVL 460
Cdd:PRK11147 391 RAELDPEKTVMDNLAEGK----QEVMVNGrprhVLGYLqdfLF----HPKRAMTpvkaLSGGERNRLLLARLFLKPSNLL 462
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1180383029 461 VMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLAT 503
Cdd:PRK11147 463 ILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVT 505
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-532 |
1.14e-76 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 251.58 E-value: 1.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQYSVVDAVIMGDVELWK 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 95 VKQERDRIYSlpEMSEEDgmkvADLESVFAEM----------DGYTAESRAEeILLEAgidkefhygLM-----ANVAP- 158
Cdd:PRK11819 101 ALDRFNEIYA--AYAEPD----ADFDALAAEQgelqeiidaaDAWDLDSQLE-IAMDA---------LRcppwdAKVTKl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 --GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGN 236
Cdd:PRK11819 165 sgGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 237 YEKFLEaaglQREQLLAENAKKSAE----IDELQDFVNrfgANAsKAKQASSRAKkmdkIKLDEVKASSRMSPSLSFDE- 311
Cdd:PRK11819 245 YSSWLE----QKAKRLAQEEKQEAArqkaLKRELEWVR---QSP-KARQAKSKAR----LARYEELLSEEYQKRNETNEi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 312 ----GKKMYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYC 387
Cdd:PRK11819 313 fippGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQdSTKDFDNDLTLFDWMSQwrtakHNDLMV--------RGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:PRK11819 393 DQ-SRDALDPNKTVWEEISG-----GLDIIKvgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 460 LVMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIK-DKQVIDFQGTFDEYlasiEEKKI 532
Cdd:PRK11819 467 LLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEY----EEDKK 536
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-523 |
1.19e-64 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 223.58 E-value: 1.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILsgALVPSAGnvsITPGLKVGNLSQDQFAfEQYSV 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDG---IPKNCQILHVEQEVVG-DDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 VDAVIMGDVELWKVKQERDRIYSLPEMSEEDGMKVAD----------------LESVFAEM---DGYTAESRAEEILLEA 142
Cdd:PLN03073 252 LQCVLNTDIERTQLLEEEAQLVAQQRELEFETETGKGkgankdgvdkdavsqrLEEIYKRLeliDAYTAEARAASILAGL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 143 GIDKEFHYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHM 222
Cdd:PLN03073 332 SFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 223 ADIDYGELRIYPGNYEKFLEAaglQREQLlaENAKKSAEIDE-----LQDFVNRFGANASKAKQASSRAKKMDKIK-LDE 296
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERT---REEQL--KNQQKAFESNErsrshMQAFIDKFRYNAKRASLVQSRIKALDRLGhVDA 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 297 V-----------KASSRMSPSL-SFDEGKKMYRqalevnklghgfDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRC 364
Cdd:PLN03073 487 VvndpdykfefpTPDDRPGPPIiSFSDASFGYP------------GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 365 LVNELKSNEGEIKWSENATFGYCPQDSTKDFDNDLTLFDWMSQ-WRTAKHNDLmvRGMLGRLLFTADDSNKKARNCSGGE 443
Cdd:PLN03073 555 ISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRcFPGVPEQKL--RAHLGSFGVTGNLALQPMYTLSGGQ 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 444 KNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGTFDEY 523
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-512 |
2.05e-50 |
|
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: 169.55 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQdstkdfdndl 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 400 tlfdwmsqwrtakhndlmvrgmlgrlLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNN 479
Cdd:cd03221 71 --------------------------L-------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 1180383029 480 ALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQ 512
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-529 |
2.80e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 174.87 E-value: 2.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 322 VNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDStkDFDNDLTL 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP--PLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 402 FDW-----------MSQWRTAKHN------DLM--------------------VRGMLGRLLFTADDSNKKARNCSGGEK 444
Cdd:COG0488 79 LDTvldgdaelralEAELEELEAKlaepdeDLErlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 445 NRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGTFDEYL 524
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
....*
gi 1180383029 525 ASIEE 529
Cdd:COG0488 239 EQRAE 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-229 |
8.78e-44 |
|
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: 151.83 E-value: 8.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGnlsqdqfAFEQYSvvdav 85
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------YFEQLS----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 imgdvelwkvkqerdriyslpemseedgmkvadlesvfaemdgytaesraeeilleagidkefhyglmanvaPGWKLRVL 165
Cdd:cd03221 73 ------------------------------------------------------------------------GGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 166 LAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
1.01e-30 |
|
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: 117.50 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnLSQDqfafeqysv 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--------LGKD--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgdveLWKVKQE-RDRIYSLPEmseedgmkvadLESVFAEMdgytaesRAEEILleagidkefHYGLmanvapGW 160
Cdd:cd03230 64 ----------IKKEPEEvKRRIGYLPE-----------EPSLYENL-------TVRENL---------KLSG------GM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 161 KLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-248 |
2.25e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.11 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpgLKVGNLSQDQFAFEQYS 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI---DGEDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VVDavimGDVELWkvkqerdriyslpemseeDGMKVADLESVFAE---MDGYTAESRAEEILLEAGIDKEFHYGLMaNVA 157
Cdd:COG4555 78 VLP----DERGLY------------------DRLTVRENIRYFAElygLFDEELKKRIEELIELLGLEEFLDRRVG-ELS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELrIYP 234
Cdd:COG4555 135 TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQ 213
|
250
....*....|....
gi 1180383029 235 GNYEKFLEAAGLQR 248
Cdd:COG4555 214 GSLDELREEIGEEN 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-526 |
5.90e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW------SENATFGYCPQDST 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 393 kdFDND--LTLFDWMSQWRTAKhndlmvRGMLGRLlfTADDsNKKARNC-----------------SGGEKNRLLFGKLM 453
Cdd:COG1121 86 --VDWDfpITVRDVVLMGRYGR------RGLFRRP--SRAD-REAVDEAlervgledladrpigelSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 454 MQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVidFQGTFDEYLAS 526
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTP 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
1.50e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.57 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpgLKVGNLSQDQFAFEQys 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRDAREDYRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvDAVIMGDvelwkvkqeRDRIYslPEMSeedgmkVADLESVFAEMDGY-TAESRAEEIL----LEAGIDKEFHYgLMAn 155
Cdd:COG4133 76 --RLAYLGH---------ADGLK--PELT------VRENLRFWAALYGLrADREAIDEALeavgLAGLADLPVRQ-LSA- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 156 vapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRKCTMIII-SHDRHFLNSV 218
Cdd:COG4133 135 ---GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAahLARGGAVLLtTHQPLELAAA 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-506 |
2.04e-28 |
|
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: 118.47 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQF--GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVSITPGLKVGNLSQdqfafeq 78
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLDGRDLLE------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 79 ysVVDAVIMGDVELwkVKQErdriyslPeMSEEDGMKVADlESVFA----EMDGYTAESRAEEILLEAGIDKEFHYGLmA 154
Cdd:COG1123 76 --LSEALRGRRIGM--VFQD-------P-MTQLNPVTVGD-QIAEAlenlGLSRAEARARVLELLEAVGLERRLDRYP-H 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 231 RiypgnyEKFLEAAGLQREQLLAEnakksaeidelqdfVNRFGANASKAKQASSRAKKMdkIKLDEVkassrmspSLSFD 310
Cdd:COG1123 222 V------EDGPPEEILAAPQALAA--------------VPRLGAARGRAAPAAAAAEPL--LEVRNL--------SKRYP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 311 EGKKMYRQALEvnklghgfdgetlfsGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSENA 382
Cdd:COG1123 272 VRGKGGVRAVD---------------DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltKLSRRS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 383 T------FGYCPQDSTKDFDNDLTLFDWMSQ------WRTAKHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFG 450
Cdd:COG1123 337 LrelrrrVQMVFQDPYSSLNPRMTVGDIIAEplrlhgLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIA 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 451 KLMMQDVNVLVMDEPTNHMD-------MEAIEALNnalKDFAGTLIFVSHDREFVSSLATRII 506
Cdd:COG1123 417 RALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQ---RELGLTYLFISHDLAVVRYIADRVA 476
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
4.43e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.08 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQdqfafeqysv 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-GEDVARDPA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgdvelwKVKQerdRIYSLPEMSE-EDGMKVADLESVFAE---MDGYTAESRAEEIL----LEAGIDKEF-HYGL 152
Cdd:COG1131 70 ------------EVRR---RIGYVPQEPAlYPDLTVRENLRFFARlygLPRKEARERIDELLelfgLTDAADRKVgTLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 153 manvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:COG1131 135 ------GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEllrELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
.
gi 1180383029 230 L 230
Cdd:COG1131 209 I 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-229 |
7.18e-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: 108.87 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGlkvgnlsqdqfafeqysvvdav 85
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK---------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 imgDVELWKVKQERDRIYSLPEMSeedgmkvadlesvfaemdgytaesraeeilleagidkefhyglmanvaPGWKLRVL 165
Cdd:cd00267 62 ---DIAKLPLEELRRRIGYVPQLS------------------------------------------------GGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 166 LAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASrerLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
3.43e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI------TPGLKVGNLSQdQF 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 75 AFEQY---SVVDAVIMGdveLWKvkqerdRIYSLPEMSEEDGMKVAD-LESVfaEMDGYtaesraeeilleagIDKEFHy 150
Cdd:COG1121 85 EVDWDfpiTVRDVVLMG---RYG------RRGLFRRPSRADREAVDEaLERV--GLEDL--------------ADRPIG- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 151 glmanvapgwKL------RVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTH 221
Cdd:COG1121 139 ----------ELsggqqqRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDR 208
|
250 260
....*....|....*....|....*..
gi 1180383029 222 MADIDYGelRIYPGNYEKFLEAAGLQR 248
Cdd:COG1121 209 VLLLNRG--LVAHGPPEEVLTPENLSR 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-221 |
2.92e-26 |
|
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: 106.46 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITP------GLKVGNLSQdQFAFEQY 79
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQ-RRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 ---SVVDAVIMGdveLWKvkqerdRIYSLPEMSEEDgmkvadlesvfaemdgytaESRAEEILLEAGIdKEFHYGLMANV 156
Cdd:cd03235 83 fpiSVRDVVLMG---LYG------HKGLFRRLSKAD-------------------KAKVDEALERVGL-SELADRQIGEL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 157 APGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDrhfLNSVCTH 221
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHD---LGLVLEY 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-223 |
6.72e-26 |
|
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: 106.28 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TP--GL-------KVGNL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgRDlaSLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 70 SQDQFAFEQYSVVDAVIMGdvelwkvkqeRdriysLPEMSEEDGMKVADLEsvfaemdgytaesRAEEILLEAGI----D 145
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG----------R-----YPHLGLFGRPSAEDRE-------------AVEEALERTGLehlaD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 146 KEFHyglmanvapgwKL------RVLLAQALFANPDILLLDEPTNNLDI-HTITWLA--NELNK-RKCTMIIISHDrhfL 215
Cdd:COG1120 133 RPVD-----------ELsggerqRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLEllRRLAReRGRTVVMVLHD---L 198
|
250
....*....|.
gi 1180383029 216 N---SVCTHMA 223
Cdd:COG1120 199 NlaaRYADRLV 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-532 |
1.34e-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: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWsenatFGYCPQDSTKDFDNDL 399
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-----DGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 400 T-------LFDWMsqwrTAKHNDLMV---RGMLGRLLFTA-----------DDSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:COG4555 77 GvlpdergLYDRL----TVRENIRYFaelYGLFDEELKKRieeliellgleEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 459 VLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDEYLASIEEKKI 532
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDELREEIGEENL 228
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
1.55e-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: 99.96 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 223 ADIDYGELRIYPGNYEKFLEAAGLQREQLLAENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDkiKLDEVKASSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALE--KMERIEKPER 78
|
....*..
gi 1180383029 303 MSPSLSF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-529 |
3.57e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 109.65 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKDFDNdlTLFDWMSQW---------- 408
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEG--TVYDFVAEGieeqaeylkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 409 ------------------RTAK------HNDL-----MVRGMLGRLLFTADdsnKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:PRK11147 101 yhdishlvetdpseknlnELAKlqeqldHHNLwqlenRINEVLAQLGLDPD---AALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 460 LVMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGTFDEYLASIEE 529
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEE 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-249 |
3.75e-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: 103.57 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----TPGLKVGNLSQD-----QFAFEQysvv 82
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRRKvglvfQNPDDQ---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 83 daVIMGDVelwkvkqerdriyslpemsEEDgmkVAdlesvFA----EMDGYTAESRAEEILLEAGIDKefhyglMANVAP 158
Cdd:COG1122 88 --LFAPTV-------------------EED---VA-----FGpenlGLPREEIRERVEEALELVGLEH------LADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 -----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLA---NELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:COG1122 133 helsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLellKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
250
....*....|....*....
gi 1180383029 231 rIYPGNYEKFLEAAGLQRE 249
Cdd:COG1122 213 -VADGTPREVFSDYELLEE 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-510 |
9.50e-25 |
|
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: 100.40 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 321 EVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKDFdndlt 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 lfdwmsqwrtakhndlmvrGMLGRLlftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNA 480
Cdd:cd00267 76 -------------------GYVPQL--------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|...
gi 1180383029 481 LKDFAG---TLIFVSHDREFVSSLATRIIDIKD 510
Cdd:cd00267 123 LRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-519 |
3.02e-24 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 101.66 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSENA---TFGYC 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQDSTKDFDndLTLFD--------WMSQWRTAKHNDL-MVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:COG1120 81 PQEPPAPFG--LTVRElvalgrypHLGLFGRPSAEDReAVEEAL-ERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 459 VLVMDEPTNHMD-------MEAIEALNNALKdfaGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGT 519
Cdd:COG1120 158 LLLLDEPTSHLDlahqlevLELLRRLARERG---RTVVMVLHDLNLAARYADRLVLLKDGRIV-AQGP 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-513 |
6.89e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 98.24 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW-----SENAT-----FGYCPQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdiKKEPEevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 DSTkdfdndltLFDWMSqwrtakhndlmVRGMLgrllftaddsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHM 469
Cdd:cd03230 81 EPS--------LYENLT-----------VRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1180383029 470 DMEAIEALNNALKDFA---GTLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:cd03230 127 DPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
1.14e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.08 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsQDQfafeqysvvdavimgDVE 91
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----------DGK---------------DLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 92 LWKVKQERDRIYSL---PemseeDGMKVADleSVFAE---------MDGYTAESRAEEILLEAGIDKefhyglMANVAP- 158
Cdd:cd03225 67 KLSLKELRRKVGLVfqnP-----DDQFFGP--TVEEEvafglenlgLPEEEIEERVEEALELVGLEG------LRDRSPf 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 159 ----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:cd03225 134 tlsgGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-506 |
1.15e-23 |
|
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: 99.14 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 321 EVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK------WSENATFGYCPQDSTKD 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 FDNDLTLFD----------WMSQWRTAKHNDLmVRGMLGRL-LFtaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMD 463
Cdd:cd03235 81 RDFPISVRDvvlmglyghkGLFRRLSKADKAK-VDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 464 EPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRII 506
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-232 |
2.05e-23 |
|
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: 98.06 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSqdqfafEQYSV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD-GKSYQKNI------EALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 VDAVImgdvelwkvkqERDRIYslPEMSEEDGMKVADLESVFaemdgytAESRAEEILLEAGIDKEFH-----YGLmanv 156
Cdd:cd03268 74 IGALI-----------EAPGFY--PNLTARENLRLLARLLGI-------RKKRIDEVLDVVGLKDSAKkkvkgFSL---- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 157 apGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRI 232
Cdd:cd03268 130 --GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-522 |
7.59e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.06 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK------WSENAT----FGYCPQ 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 DSTkdFDNDLTLFDWMSQWRTAKHNDL-----MVRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMD 463
Cdd:COG1131 81 EPA--LYPDLTVRENLRFFARLYGLPRkeareRIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 464 EPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDE 522
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRIV-ADGTPDE 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-247 |
3.10e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 99.97 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFA-FEQysvvDA 84
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdFEN----DL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 85 VIMGDVELWKvkQERDRIYSLPEM------SEEDGMKvadleSVfaemdgytaesraeeilleagidkefhyglmANVAP 158
Cdd:PRK15064 400 TLFDWMSQWR--QEGDDEQAVRGTlgrllfSQDDIKK-----SV-------------------------------KVLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYE 238
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYE 521
|
....*....
gi 1180383029 239 KFLEAAGLQ 247
Cdd:PRK15064 522 EYLRSQGIE 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-515 |
3.89e-22 |
|
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: 99.88 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG--ALVPSAG----NVSITPglKVGNLSQDQFA 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyHVALCE--KCGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 76 FEQYSVVDAVI-MGDVELWKV-----KQERDRIYSLPE----MSEEDGMKVADLESVfaEMDGYTAES---RAEEILLEA 142
Cdd:TIGR03269 79 GEPCPVCGGTLePEEVDFWNLsdklrRRIRKRIAIMLQrtfaLYGDDTVLDNVLEAL--EEIGYEGKEavgRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 143 GIDKEFHYgLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHDRHFLNSV 218
Cdd:TIGR03269 157 QLSHRITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 219 CTHMADIDYGELriypgnyekfleaaglqreqllaenaKKSAEIDELqdfVNRFGANASKAKQASSRAKKMDKIKLDEVK 298
Cdd:TIGR03269 236 SDKAIWLENGEI--------------------------KEEGTPDEV---VAVFMEGVSEVEKECEVEVGEPIIKVRNVS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 299 ASsrmspSLSFDEG--KKMYRQALEVnklghgFDGETlfsggdflleagakLAVIGENGVGKTTFLRCLVNELKSNEGEI 376
Cdd:TIGR03269 287 KR-----YISVDRGvvKAVDNVSLEV------KEGEI--------------FGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 377 ------KWSENATFGYCPQDSTKDFDNDL----------TLFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSNKKARNC- 439
Cdd:TIGR03269 342 nvrvgdEWVDMTKPGPDGRGRAKRYIGILhqeydlyphrTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEIl 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 -------SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDI 508
Cdd:TIGR03269 422 dkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
....*..
gi 1180383029 509 KDKQVID 515
Cdd:TIGR03269 502 RDGKIVK 508
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
5.04e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 95.26 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGA----EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS-----ITPGLKVGNLSQ 71
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 72 DQFAFEQ-YSVVDAVimgdvelWKVkqerDRIYSLPemseedgmkvadlesvFAEMDGYTAESRAEEILLEAGIDKEFHY 150
Cdd:COG1124 81 VQMVFQDpYASLHPR-------HTV----DRILAEP----------------LRIHGLPDREERIAELLEQVGLPPSFLD 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 151 GLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK----RKCTMIIISHDRhflnSVCTHMAD 224
Cdd:COG1124 134 RYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDlreeRGLTYLFVSHDL----AVVAHLCD 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
3.25e-21 |
|
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: 92.50 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 76 -------FEQYSVVDAVIMGdVELwkvkQERDRIYSLPEMSEEDgmkvadlesvfaemdgyTAESRAEEILLEAGIDKEF 148
Cdd:cd03219 80 tfqiprlFPELTVLENVMVA-AQA----RTGSGLLLARARREER-----------------EARERAEELLERVGLADLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 149 HYgLMANVAPGWKLRVLLAQALFANPDILLLDEPT---NNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADI 225
Cdd:cd03219 138 DR-PAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
....*
gi 1180383029 226 DYGEL 230
Cdd:cd03219 217 DQGRV 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-230 |
3.72e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.80 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvGNLSQDQFafeqysv 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL------DGKPLSAM------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgDVELWkvkqeRDRIYSLPEMSEEDGMKVAD-LESVFAEMDGYTAESRAEEILLEAGIDKEFhygLMANVAP-- 158
Cdd:COG4619 68 -------PPPEW-----RRQVAYVPQEPALWGGTVRDnLPFPFQLRERKFDRERALELLERLGLPPDI---LDKPVERls 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 159 -GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:COG4619 133 gGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-514 |
4.24e-21 |
|
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: 90.57 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 321 EVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWsenatfgycpqdstkdfdNDLT 400
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------------DGKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 LFDWMSQWRtAKHndlmvRGMLGRLLFTADDSNKKARNC---SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD------- 470
Cdd:cd03214 63 LASLSPKEL-ARK-----IAYVPQALELLGLAHLADRPFnelSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqiel 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1180383029 471 MEAIEALNnalKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03214 137 LELLRRLA---RERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-242 |
4.78e-21 |
|
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: 96.54 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysv 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimGD-VELWKVKQERDRIyslpemseeDGMKvadleSVFAEMDG---------YTAESRAeeiLLEA----GIDKE 147
Cdd:TIGR03719 382 ------GEtVKLAYVDQSRDAL---------DPNK-----TVWEEISGgldiiklgkREIPSRA---YVGRfnfkGSDQQ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 148 FHYGLMANvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTH-MADID 226
Cdd:TIGR03719 439 KKVGQLSG---GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHiLAFEG 515
|
250
....*....|....*.
gi 1180383029 227 YGELRIYPGNYEKFLE 242
Cdd:TIGR03719 516 DSHVEWFEGNFSEYEE 531
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-251 |
6.13e-21 |
|
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: 96.83 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqDQFAFEQYSVVD-----AVI 86
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-----------DGIDLRQIDPASlrrqiGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 87 MGDVELWK--VkqeRDRI-YSLPEMSEEDGM---KVADLESVFAEM-DGYtaesraEEILLEAGidkefhyglmANVAPG 159
Cdd:COG2274 555 LQDVFLFSgtI---RENItLGDPDATDEEIIeaaRLAGLHDFIEALpMGY------DTVVGEGG----------SNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRHFLNsvcthMAD----IDYGELrIY 233
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIR-----LADriivLDKGRI-VE 689
|
250 260
....*....|....*....|..
gi 1180383029 234 PGNYEKFLEAAG----LQREQL 251
Cdd:COG2274 690 DGTHEELLARKGlyaeLVQQQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-216 |
8.39e-21 |
|
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: 95.98 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYSVV--DAVIM-G 88
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPASWR-RQIAWVpqNPYLFaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 89 DVelwkvkqeRD--RIYSlPEMSEEDGMKV---ADLESVFAEM-DGYtaesraEEILLEAGidkefhyglmANVAPGWKL 162
Cdd:COG4988 426 TI--------REnlRLGR-PDASDEELEAAleaAGLDEFVAALpDGL------DTPLGEGG----------RGLSGGQAQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 163 RVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRHFLN 216
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLALLA 536
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
1.87e-20 |
|
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: 90.33 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFG----AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ--- 73
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLLSGKElrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 ------FAFEQYSVVDA-VIMGDV----ELWKV-KQERdriyslpemseedgmkvadlesvfaemdgytaESRAEEILLE 141
Cdd:cd03258 80 arrrigMIFQHFNLLSSrTVFENValplEIAGVpKAEI--------------------------------EERVLELLEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 142 AGI-DKEFHYglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLN 216
Cdd:cd03258 128 VGLeDKADAY--PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRElGLTIVLITHEMEVVK 205
|
250
....*....|....
gi 1180383029 217 SVCTHMADIDYGEL 230
Cdd:cd03258 206 RICDRVAVMEKGEV 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
1.91e-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: 88.43 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFG--AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeqy 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 sVVDAVimgDVELWKVKQERDRIYSLPEmseedgmkvaDLEsVFaemDGytaeSRAEEILleAGidkefhyglmanvapG 159
Cdd:cd03246 60 -RLDGA---DISQWDPNELGDHVGYLPQ----------DDE-LF---SG----SIAENIL--SG---------------G 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSV 218
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAHRPETLASA 162
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
2.20e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 11 FGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQ-----DQFAFeqySVVDAV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPL---TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 IMGdveLWKvkqerdRIYSLPEMSEEDGMKVAD-LESVfaemdgytaesraeeilleaGIDkEFHYGLMANVAPGWKLRV 164
Cdd:NF040873 79 AMG---RWA------RRGLWRRLTRDDRAAVDDaLERV--------------------GLA-DLAGRQLGELSGGQRQRA 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 165 LLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRH 213
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESrerIIALLAEEHARGATVVVVTHDLE 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-514 |
3.30e-20 |
|
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: 88.85 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSEN--------ATFGYCPQDSTKDFDNDlTLFDWMSQWRT 410
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDVDYQLFTD-SVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 411 AKHNDLM-VRGMLGRL-LFTADDsnKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFA--G 486
Cdd:cd03226 99 ELDAGNEqAETVLKDLdLYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaqG 176
|
170 180
....*....|....*....|....*....
gi 1180383029 487 TLIFV-SHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03226 177 KAVIViTHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-506 |
4.22e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 93.72 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITPG----LKV--GNLSQDQFAfeqysvvdavimgdvelwKVKQERDRIYS 104
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevLKRfrGTELQNYFK------------------KLYNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 105 LPEMSE----------EDGMKVADLESVFAEMdgytaesrAEEILLEAGIDKEFhyglmaNVAPGWKL-RVLLAQALFAN 173
Cdd:PRK13409 165 KPQYVDlipkvfkgkvRELLKKVDERGKLDEV--------VERLGLENILDRDI------SELSGGELqRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 174 PDILLLDEPTNNLDIH---TITWLANELNKRKcTMIIISHDRHFLNsvctHMAD---IDYGElriyPGNYEKFLEAAGLQ 247
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRqrlNVARLIRELAEGK-YVLVVEHDLAVLD----YLADnvhIAYGE----PGAYGVVSKPKGVR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 248 -------REQLLAENAkksaeidelqdfvnRFGANASKAKQASSRAKKMDKIKLdevkassrmspslSFDEGKKMYrqal 320
Cdd:PRK13409 302 vgineylKGYLPEENM--------------RIRPEPIEFEERPPRDESERETLV-------------EYPDLTKKL---- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 321 evnklghgfdgetlfsgGDFLLEA-------GAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSEnaTFGYCPQDSTK 393
Cdd:PRK13409 351 -----------------GDFSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--KISYKPQYIKP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 394 DFdnDLTLFDWMSQWRTAKH-----NDLMVRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNH 468
Cdd:PRK13409 412 DY--DGTVEDLLRSITDDLGssyykSEIIKPLQLERLL------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1180383029 469 MDMEAIEALNNALKDFA----GTLIFVSHDREFVSSLATRII 506
Cdd:PRK13409 484 LDVEQRLAVAKAIRRIAeereATALVVDHDIYMIDYISDRLM 525
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-506 |
6.67e-20 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 92.93 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITPG----LKV--GNLSQDQFAfeqysvvdAVIMGDVelwKVKQERDRIYS 104
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevLKRfrGTELQDYFK--------KLANGEI---KVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 105 LPEMSeeDGmKVADLesvfaeMDGYTAESRAEEIL----LEAGIDKEfhyglMANVAPGWKLRVLLAQALFANPDILLLD 180
Cdd:COG1245 172 IPKVF--KG-TVREL------LEKVDERGKLDELAeklgLENILDRD-----ISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 181 EPTNNLDIH---TITWLANELNKRKCTMIIISHDRHFLNsvctHMAD---IDYGElriyPGNY-------------EKFL 241
Cdd:COG1245 238 EPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILD----YLADyvhILYGE----PGVYgvvskpksvrvgiNQYL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 242 EAaglqreQLLAENAkksaeidelqdfvnRFganaskakqassrakKMDKIKLdEVKASSRMSPS---LSFDEGKKMYrq 318
Cdd:COG1245 310 DG------YLPEENV--------------RI---------------RDEPIEF-EVHAPRREKEEetlVEYPDLTKSY-- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 alevnklghgfdgetlfsgGDFLLEA-------GAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkwSENATFGYCPQDS 391
Cdd:COG1245 352 -------------------GGFSLEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 392 TKDFdnDLTLFDWMSQWRTAK------HNDLMVRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEP 465
Cdd:COG1245 411 SPDY--DGTVEEFLRSANTDDfgssyyKTEIIKPLGLEKLL------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1180383029 466 TNHMDMEAIEALNNALKDFA----GTLIFVSHDREFVSSLATRII 506
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAenrgKTAMVVDHDIYLIDYISDRLM 527
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
9.04e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 9.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 328 GFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKDFDNDLTLFDWMSQ 407
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 408 WRTAKhndlmvRGMLGRLlfTADD----------------SNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:NF040873 81 GRWAR------RGLWRRL--TRDDraavddalervgladlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1180383029 472 EAIEALNNALKDFAG---TLIFVSHDREFVSSlATRII 506
Cdd:NF040873 153 ESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCV 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-211 |
9.33e-20 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 86.72 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysvvdav 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 iMG-DVELWKVKQERDRIYSLPEMSEEdgMKVADL-ESVFAEMDGytaesraeeilleagidkefhyglmanvapGWKLR 163
Cdd:cd03214 59 -DGkDLASLSPKELARKIAYVPQALEL--LGLAHLaDRPFNELSG------------------------------GERQR 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLDIH----TITWLANELNKRKCTMIIISHD 211
Cdd:cd03214 106 VLLARALAQEPPILLLDEPTSHLDIAhqieLLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-224 |
1.65e-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: 86.93 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEP-LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpgLKVGNLSQDqfafEQYSVVDA 84
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL----LNGKPIKAK----ERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 85 ViMGDVElwkvkqerDRIYSlpemseedgmkvadlESVFAE-----MDGYTAESRAEEILLEAGID--KEFHyglmanva 157
Cdd:cd03226 76 V-MQDVD--------YQLFT---------------DSVREElllglKELDAGNEQAETVLKDLDLYalKERH-------- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 158 P-----GWKLRVLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRKCTMIIISHDRHFLNSVCT---HMAD 224
Cdd:cd03226 124 PlslsgGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmeRVGELIRELAAQGKAVIVITHDYEFLAKVCDrvlLLAN 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
3.34e-19 |
|
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: 87.40 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA----- 75
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 76 --------FEQYSVVDAVIMGdvelwkvKQERDRIYSLPEMseedgmkvADLESVFAEMDGytAESRAEEILLEAGIDKE 147
Cdd:COG0411 83 rtfqnprlFPELTVLENVLVA-------AHARLGRGLLAAL--------LRLPRARREERE--ARERAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 148 FHYgLMANVAPGWKLRVLLAQALFANPDILLLDEPT---NNLDIHTITWLANELNK-RKCTMIIISHDRHFLNSVCTHMA 223
Cdd:COG0411 146 ADE-PAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIV 224
|
....*..
gi 1180383029 224 DIDYGEL 230
Cdd:COG0411 225 VLDFGRV 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
9.28e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 84.88 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysvvdav 85
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 imGDVELWKVKQERDRI------YSL-PEMSEED----GMKVadlesvfAEMDGYTAESRAEEILLEAGID---KEFHYG 151
Cdd:cd03259 60 --DGRDVTGVPPERRNIgmvfqdYALfPHLTVAEniafGLKL-------RGVPKAEIRARVRELLELVGLEgllNRYPHE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 152 LMAnvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHDR 212
Cdd:cd03259 131 LSG----GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELkelqRELGITTIYVTHDQ 191
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
1.34e-18 |
|
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: 84.46 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAE----PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ---- 73
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 ------FAFEQYSVvdavimgdvelwkvkqerdriysLPEMSEEDGMKVADLesvFAEMDGYTAESRAEEILLEAGIDKE 147
Cdd:cd03255 80 rrrhigFVFQSFNL-----------------------LPDLTALENVELPLL---LAGVPKKERRERAEELLERVGLGDR 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 148 FHY------GlmanvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDR 212
Cdd:cd03255 134 LNHypselsG-------GQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNKeAGTTIVVVTHDP 201
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
2.94e-18 |
|
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: 81.54 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 17 FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-----------TPGLKVGNLSQDQFAFEQYSVVDAV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 IMGdVELWKVKQERDriyslpemseedgmkvadlesvfaemdgytaESRAEEILLEAGI---DKEFHYGLMANVAPGWKL 162
Cdd:pfam00005 81 RLG-LLLKGLSKREK-------------------------------DARAEEALEKLGLgdlADRPVGERPGTLSGGQRQ 128
|
170 180
....*....|....*....|..
gi 1180383029 163 RVLLAQALFANPDILLLDEPTN 184
Cdd:pfam00005 129 RVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
3.42e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 83.55 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFG----AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ--- 73
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERElar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 -------FAFEQYsvvdavimgdvELwkvkqerdriysLPEMSeedgmkVAD---LESVFAEMDGYTAESRAEEILLEAG 143
Cdd:COG1136 83 lrrrhigFVFQFF-----------NL------------LPELT------ALEnvaLPLLLAGVSRKERRERARELLERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 144 I-DKEFHYglmanvaPGwKL------RVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRK-CTMIIISHDR 212
Cdd:COG1136 134 LgDRLDHR-------PS-QLsggqqqRVAIARALVNRPKLILADEPTGNLDSKTgeeVLELLRELNRELgTTIVMVTHDP 205
|
.
gi 1180383029 213 H 213
Cdd:COG1136 206 E 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-289 |
4.09e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 87.70 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGnlsqdqfAFEQY------ 79
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVA-------YFDQHraeldp 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 --SVVDAVIMGdvelwkvKQErdriyslpemseedgmkvadlesvfAEMDGytaesRAEEILleaGIDKEFHYGLMANVA 157
Cdd:PRK11147 397 ekTVMDNLAEG-------KQE-------------------------VMVNG-----RPRHVL---GYLQDFLFHPKRAMT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 158 P------GWKLRVLLAQaLFANP-DILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFL-NSVCTHMADIDYGE 229
Cdd:PRK11147 437 PvkalsgGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGK 515
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 230 LRIYPGNYEKfleaAGLQREQLLAENAKKSAEIDElqdfvnrfgANASKAKQASSRAKKM 289
Cdd:PRK11147 516 IGRYVGGYHD----ARQQQAQYLALKQPAVKKKEE---------AAAPKAETVKRSSKKL 562
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
4.47e-18 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 83.07 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPL-FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAFEQY 79
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAaLHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIA-GEDVNRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 SVvdAVIMGDVELwkvkqerdriysLPEMSEEDGMKVAdLESVFAEMDGYtaESRAEEILLEAGI-DKEFHYGLmaNVAP 158
Cdd:TIGR02673 80 RI--GVVFQDFRL------------LPDRTVYENVALP-LEVRGKKEREI--QRRVGAALRQVGLeHKADAFPE--QLSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRH 213
Cdd:TIGR02673 141 GEQQRVAIARAIVNSPPLLLADEPTGNLDPDLserILDLLKRLNKRGTTVIVATHDLS 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-512 |
5.34e-18 |
|
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: 82.51 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 321 EVNKLGHGFDG--ETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKD---- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 FDN-D-----LTLFD----WMSQWRTAKHNDLM-VRGMLGRLlftaDDSNKKARNC---SGGEKNRLLFGKLMMQDVNVL 460
Cdd:cd03225 81 FQNpDdqffgPTVEEevafGLENLGLPEEEIEErVEEALELV----GLEGLRDRSPftlSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 461 VMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQ 512
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
339-467 |
1.16e-17 |
|
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: 80.00 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW-----------SENATFGYCPQDSTkdFDNDLT------- 400
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQ--LFPRLTvrenlrl 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 ---LFDWMSQWRTAKHNDLMVRgmLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTN 467
Cdd:pfam00005 83 gllLKGLSKREKDARAEEALEK--LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
1.61e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.78 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ-------- 73
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAElyrlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 -FAFEQYSVVDAVIMGD-VELWkvkqerdriysLPEMSEEDgmkvadlESVFAEmdgytaesRAEEILLEAGIdKEFHYG 151
Cdd:cd03261 80 gMLFQSGALFDSLTVFEnVAFP-----------LREHTRLS-------EEEIRE--------IVLEKLEAVGL-RGAEDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 152 LMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-IHT--ITWLANELNKRKC-TMIIISHDRHFLNSVCTHMADIDY 227
Cdd:cd03261 133 YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpIASgvIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYD 212
|
...
gi 1180383029 228 GEL 230
Cdd:cd03261 213 GKI 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
2.28e-17 |
|
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: 81.67 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNvsitpglkvgnlsqdqfafeqys 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvDAVIMG----DVELWKVKQerdRI-YSLPEMSEE--DGMKVAD-----LESVFAEMDGYTAE--SRAEEILLEAGI-- 144
Cdd:COG1119 60 --DVRLFGerrgGEDVWELRK---RIgLVSPALQLRfpRDETVLDvvlsgFFDSIGLYREPTDEqrERARELLELLGLah 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 145 --DKEFHyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH-------TITWLANElnkRKCTMIIISH 210
Cdd:COG1119 135 laDRPFG-----TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGarelllaLLDKLAAE---GAPTLVLVTH 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
2.59e-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: 81.07 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG-----ALVPSAGNVSITpGLKVGNLSQD---- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLD-GKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 73 ----QFAFEQYSVVDAVIMGDVEL-WKVKQERDRiyslpemseedgmkvadlesvfAEMDGytaesRAEEILLEAGIDKE 147
Cdd:cd03260 80 rrrvGMVFQKPNPFPGSIYDNVAYgLRLHGIKLK----------------------EELDE-----RVEEALRKAALWDE 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 148 FHYGLMA-NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISHD 211
Cdd:cd03260 133 VKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIStakIEELIAELKKEY-TIVIVTHN 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-506 |
2.86e-17 |
|
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: 81.30 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 337 GGDFLLEA-------GAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWsENATFGYCPQDSTKDFdnDLTLFDWM---- 405
Cdd:cd03237 10 LGEFTLEVeggsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADY--EGTVRDLLssit 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 406 ------SQWRTAKHNDLMVRGMLGRLLftaddsnkkaRNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNN 479
Cdd:cd03237 87 kdfythPYFKTEIAKPLQIEQILDREV----------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|.
gi 1180383029 480 ALKDFA----GTLIFVSHDREFVSSLATRII 506
Cdd:cd03237 157 VIRRFAenneKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
332-513 |
4.17e-17 |
|
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: 79.18 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 332 ETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSENA---TFGYCPQDstkdfdndLT 400
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGYLPQD--------DE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 LFDwmsqwRTAKHNDLmvrgmlgrllftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNA 480
Cdd:cd03246 87 LFS-----GSIAENIL-----------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 1180383029 481 LKD---FAGTLIFVSHDREFVSSlATRIIDIKDKQV 513
Cdd:cd03246 139 IAAlkaAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
4.20e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.21 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAE----PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI------TPGLKVGNLSQ 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 72 DQFAFEQYSVVDAVIMGdvelwkvkqerdriyslPEMSeedGMKVADlesvfaemdgytAESRAEEILLEAGIDK-EFHY 150
Cdd:cd03293 81 QDALLPWLTVLDNVALG-----------------LELQ---GVPKAE------------ARERAEELLELVGLSGfENAY 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 151 glmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIISHD 211
Cdd:cd03293 129 -------PhqlsgGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-235 |
4.21e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.84 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkVGNLSQDQFafEQYSVVDAVIMGdvelwkvkQE 98
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-----AGLVPWKRR--KKFLRRIGVVFG--------QK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYSLPemseedgmkVADLESVFAEM---DGYTAESRAEEI--LLEAGidkEFHYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:cd03267 104 TQLWWDLP---------VIDSFYLLAAIydlPPARFKKRLDELseLLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 174 PDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDRHFLNSVCTHMADIDYGELrIYPG 235
Cdd:cd03267 172 PEILFLDEPTIGLDVVAqenIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
8.87e-17 |
|
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: 79.17 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqDQFAFEQYSVVDavIMGDVELwkVKQ 97
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-----------DGTDIRQLDPAD--LRRNIGY--VPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 98 E--------RDRI-YSLPEMSEEDGMKVADLesvfaemdgytaesraeeilleAGIDkEF---H---YGLM-----ANVA 157
Cdd:cd03245 86 DvtlfygtlRDNItLGAPLADDERILRAAEL----------------------AGVT-DFvnkHpngLDLQigergRGLS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKC--TMIIISHDRHFLNSV 218
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-230 |
1.00e-16 |
|
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: 83.03 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYSVVdAVIMGDVE-----L 92
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-GKDLTKLSRRSLR-ELRRRV-QMVFQDPYsslnpR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 93 WKVKQErdriyslpeMSEedGMKVadlesvFAEMDGYTAESRAEEILLEAGIDKEFhyglmANVAP-----GWKLRVLLA 167
Cdd:COG1123 359 MTVGDI---------IAE--PLRL------HGLLSRAERRERVAELLERVGLPPDL-----ADRYPhelsgGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 168 QALFANPDILLLDEPTNNLDIHTITWLAN---ELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNllrDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
1.06e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 78.00 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDqfafeqysvvdav 85
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDE------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 imgdvelwkVKQERDRIyslpemseedGMkvadlesVFAEMDGYTAESRAEEILleagidkefhYGLmanvAPGWKLRVL 165
Cdd:cd03229 71 ---------LPPLRRRI----------GM-------VFQDFALFPHLTVLENIA----------LGL----SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 166 LAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITrreVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
1.07e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.33 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAE-PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAFeqy 79
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPY--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svvdavimgdveLwkvkqeRDRI------YSL-PEMSeedgmkVAD-----LEsvFAEMDGYTAESRAEEILLEAGI-DK 146
Cdd:COG2884 77 ------------L------RRRIgvvfqdFRLlPDRT------VYEnvalpLR--VTGKSRKEIRRRVREVLDLVGLsDK 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 147 EFHYglmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNS 217
Cdd:COG2884 131 AKAL-------PhelsgGEQQRVAIARALVNRPELLLADEPTGNLDPETsweIMELLEEINRRGTTVLIATHDLELVDR 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
1.15e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 79.75 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAE----PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT------PGLKVGnls 70
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 71 qdqFAFEQYSVvdavimgdvelwkvkqerdriysLPEMSEED----GMKVADLESvfAEmdgytAESRAEEILLEAGI-D 145
Cdd:COG1116 84 ---VVFQEPAL-----------------------LPWLTVLDnvalGLELRGVPK--AE-----RRERARELLELVGLaG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 146 KEFHYglmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTI----TWLANELNKRKCTMIIISHD 211
Cdd:COG1116 131 FEDAY-------PhqlsgGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-510 |
1.17e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 78.00 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWS-ENATFGycpQDSTKDFDN- 397
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDL---EDELPPLRRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 ------DLTLFDWMSqwrtakhndlmVRGMLGRLLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:cd03229 78 igmvfqDFALFPHLT-----------VLENIALGL-------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 472 EA---IEALNNALKDFAG-TLIFVSHDREFVSSLATRIIDIKD 510
Cdd:cd03229 134 ITrreVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-522 |
1.81e-16 |
|
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: 78.63 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSENA--------T 383
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPPHEiarlgigrT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 384 FgycpQDsTKDFDNdLTLFDWMsqwRTAKHNDLMVRGMLGRLLFTADDSNKKARNC-----------------SGGEKNR 446
Cdd:cd03219 81 F----QI-PRLFPE-LTVLENV---MVAAQARTGSGLLLARARREEREARERAEELlervgladladrpagelSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 447 LLFGKLMMQDVNVLVMDEPT---NHMDMEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIdikdkqVIDF-----QG 518
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT------VLDQgrviaEG 225
|
....
gi 1180383029 519 TFDE 522
Cdd:cd03219 226 TPDE 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
1.87e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 78.00 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGnRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TPGLK--------VGNLSQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLKqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 72 DQFAFEQYSVVDAV----IMGDVELWKVKQERDRIYSLPEMSEEDGMKVADLesvfaemdgytaesraeeilleAGidke 147
Cdd:cd03264 80 EFGVYPNFTVREFLdyiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSL----------------------SG---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 148 fhyglmanvapGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCtmIIIS-HDRHFLNSVCTHMA 223
Cdd:cd03264 134 -----------GMRRRVGIAQALVGDPSILIVDEPTAGLDPeerIRFRNLLSELGEDRI--VILStHIVEDVESLCNQVA 200
|
....*...
gi 1180383029 224 DIDYGELR 231
Cdd:cd03264 201 VLNKGKLV 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
2.17e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFafeqys 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vVDAVIMGDVELWkvkqerdriyslpeMSEEDGMKVAD----LESVFAEMdgytaesraeeiLLEAGIDKefhyglmanV 156
Cdd:PRK09544 78 -LDTTLPLTVNRF--------------LRLRPGTKKEDilpaLKRVQAGH------------LIDAPMQK---------L 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 157 APGWKLRVLLAQALFANPDILLLDEPTNNLDIH-------TITWLANELNkrkCTMIIISHDRHFLnsvcthMADID 226
Cdd:PRK09544 122 SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvalydLIDQLRRELD---CAVLMVSHDLHLV------MAKTD 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-514 |
2.48e-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: 78.02 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 340 FLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW-------------SENatFGYCPQDSTKDF----DNdLTLF 402
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlRRN--IGYVPQDVTLFYgtlrDN-ITLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 403 DwmsqwRTAKHNDLMVRGMLGRLL-FTADDSN-------KKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAI 474
Cdd:cd03245 102 A-----PLADDERILRAAELAGVTdFVNKHPNgldlqigERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1180383029 475 EALNNALKDFAG--TLIFVSHdREFVSSLATRIIDIKDKQVI 514
Cdd:cd03245 177 ERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRIV 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
319-525 |
2.75e-16 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 82.19 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGET--LFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK-------------WSENat 383
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpasLRRQ-- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 384 FGYCPQDstkDF-------DNdLTLFD-WMSQ---WRTAK----HNDLMVR--------GMLGRLLftaddsnkkarncS 440
Cdd:COG2274 551 IGVVLQD---VFlfsgtirEN-ITLGDpDATDeeiIEAARlaglHDFIEALpmgydtvvGEGGSNL-------------S 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 441 GGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG--TLIFVSHDREFVsSLATRIIDIKDKQVIDfQG 518
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DG 691
|
....*..
gi 1180383029 519 TFDEYLA 525
Cdd:COG2274 692 THEELLA 698
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-525 |
3.85e-16 |
|
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: 81.35 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGET--LFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK--------WSENA---TFG 385
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 386 YCPQD----STKDFDNdLTLFDwmsqwRTAKHNDLM-----VRgmLGRLLFTADDS-----NKKARNCSGGEKNRLLFGK 451
Cdd:COG4987 413 VVPQRphlfDTTLREN-LRLAR-----PDATDEELWaalerVG--LGDWLAALPDGldtwlGEGGRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 452 LMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG--TLIFVSHDREFVsSLATRIIDIKDKQVIDfQGTFDEYLA 525
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGL-ERMDRILVLEDGRIVE-QGTHEELLA 558
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-242 |
4.73e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysvvdav 85
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 imGD-VELWKVKQERDRIyslpemseeDGMKvadleSVFAEMDG---------YTAESRAeeiLLEA----GIDKEFHYG 151
Cdd:PRK11819 384 --GEtVKLAYVDQSRDAL---------DPNK-----TVWEEISGgldiikvgnREIPSRA---YVGRfnfkGGDQQKKVG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 152 LMANvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL-NKRKCTMiIISHDRHFLNSVCTHMadIDY--- 227
Cdd:PRK11819 445 VLSG---GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALlEFPGCAV-VISHDRWFLDRIATHI--LAFegd 518
|
250
....*....|....*
gi 1180383029 228 GELRIYPGNYEKFLE 242
Cdd:PRK11819 519 SQVEWFEGNFQEYEE 533
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
339-512 |
6.94e-16 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 75.50 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSEN-----------ATFGYCPQDStkdfdndlTLFDwmsq 407
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrKNIAYVPQDP--------FLFS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 408 wRTAKHNdlmvrgmlgrLLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG- 486
Cdd:cd03228 90 -GTIREN----------IL-------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKg 145
|
170 180
....*....|....*....|....*..
gi 1180383029 487 -TLIFVSHDREFVsSLATRIIDIKDKQ 512
Cdd:cd03228 146 kTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
348-514 |
7.36e-16 |
|
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: 76.77 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 348 LAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENAT----------FGYCPQDSTkdFDNDLTLFD---WMSQWR--TAK 412
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrkaarqsLGYCPQFDA--LFDELTVREhlrFYARLKglPKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 413 HNDLMVRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG--TLIF 490
Cdd:cd03263 109 EIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIIL 187
|
170 180
....*....|....*....|....
gi 1180383029 491 VSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03263 188 TTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.11e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.77 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysv 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgdvelwkvkqerdriyslpemseeDGMKVAdlesvFAEmdgyTAESRAeeilleAGIdkEFHYGLmanvAPGWK 161
Cdd:cd03216 60 ------------------------------DGKEVS-----FAS----PRDARR------AGI--AMVYQL----SVGER 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLfkvIRRLRAQGVAVIFISH 140
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-230 |
1.59e-15 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 75.64 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQD--------Q 73
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLTDDKKNinelrqkvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 FAFEQY------SVVDAVIMGDVELWKvkqerdriyslpeMSEEDgmkvadlesvfaemdgytAESRAEEILLEAGI-DK 146
Cdd:cd03262 80 MVFQQFnlfphlTVLENITLAPIKVKG-------------MSKAE------------------AEERALELLEKVGLaDK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 147 EFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMA 223
Cdd:cd03262 129 ADAYP--AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
....*..
gi 1180383029 224 DIDYGEL 230
Cdd:cd03262 207 FMDDGRI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
330-526 |
1.60e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 79.42 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 330 DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK-------------WSENatFGYCPQDSTkdfd 396
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdldpasWRRQ--IAWVPQNPY---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 397 ndltLF-----------------DWMSQW-RTAKHNDLmVRGMLGRLLFTADDSnkkARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:COG4988 422 ----LFagtirenlrlgrpdasdEELEAAlEAAGLDEF-VAALPDGLDTPLGEG---GRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 459 VLVMDEPTNHMDMEAIEALNNALKDFAG--TLIFVSHDREFVsSLATRIIDIKDKQVIDfQGTFDEYLAS 526
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAK 561
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-249 |
2.94e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI---TPglkvgnlSQDQFAF-EQYSVVdaviMGD-VEL 92
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyVP-------FKRRKEFaRRIGVV----FGQrSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 93 W---------KVKQErdrIYSLPEmseedgmkvADLESVFAEMDgytaesraeEIL-LEAGIDKefhyglmanvaP---- 158
Cdd:COG4586 108 WwdlpaidsfRLLKA---IYRIPD---------AEYKKRLDELV---------ELLdLGELLDT-----------Pvrql 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 --GWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNK-RKCTMIIISHDrhflnsvcthMADI------- 225
Cdd:COG4586 156 slGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNReRGTTILLTSHD----------MDDIealcdrv 225
|
250 260
....*....|....*....|....*..
gi 1180383029 226 ---DYGELrIYPGNYEKFLEAAGLQRE 249
Cdd:COG4586 226 iviDHGRI-IYDGSLEELKERFGPYKT 251
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-230 |
3.08e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 76.00 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF-AFEQysvvdavimgDVELw 93
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRrAFRR----------DVQL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 94 kVKQerDRIYSL-PEMSEED--GMKVADLESvfaeMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQAL 170
Cdd:TIGR02769 93 -VFQ--DSPSAVnPRMTVRQiiGEPLRHLTS----LDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 171 FANPDILLLDEPTNNLDIH---TITWLANELNKRKCT-MIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVlqaVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-211 |
3.14e-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: 74.64 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 26 NGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGL---------------KVGNLSQDQFAFEQYSVVDAVIMGdv 90
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 eLWKVKQERDRIyslpemseedgmkvadlesvfaemdgytaesRAEEILLEAGIDK-EFHYglMANVAPGWKLRVLLAQA 169
Cdd:cd03297 100 -LKRKRNREDRI-------------------------------SVDELLDLLGLDHlLNRY--PAQLSGGEKQRVALARA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 170 LFANPDILLLDEPTNNLDIHTITWLANELNKRK----CTMIIISHD 211
Cdd:cd03297 146 LAAQPELLLLDEPFSALDRALRLQLLPELKQIKknlnIPVIFVTHD 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-526 |
3.14e-15 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 75.23 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK-----WSENA---------TFG 385
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSeaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 386 YCPQDSTKdFDnDLTLFD----WMSQWRTAKHND-----LMVRGMLGrllfTADDSNKKARNCSGGEKNRLLFGKLMMQD 456
Cdd:cd03261 81 MLFQSGAL-FD-SLTVFEnvafPLREHTRLSEEEireivLEKLEAVG----LRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 457 VNVLVMDEPTNHMD---MEAIEALNNALKD-FAGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDEYLAS 526
Cdd:cd03261 155 PELLLYDEPTAGLDpiaSGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRAS 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-243 |
4.83e-15 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 74.63 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDqfafEQYS 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEK----ELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VvdavimgdvelwkvkqeRDRI---------YslpemseeDGMKVAD------LEsvFAEMDGYTAESRAEEILLEAGID 145
Cdd:COG1127 80 L-----------------RRRIgmlfqggalF--------DSLTVFEnvafplRE--HTDLSEAEIRELVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 146 KefHYGLManvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLN 216
Cdd:COG1127 133 G--AADKM----PselsgGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELRDElGLTSVVVTHDLDSAF 206
|
250 260
....*....|....*....|....*..
gi 1180383029 217 SVCTHMADIDYGELrIYPGNYEKFLEA 243
Cdd:COG1127 207 AIADRVAVLADGKI-IAEGTPEELLAS 232
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
5.59e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 77.39 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-----------TPGLKVGNLSQDqfafeqys 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdreTFGKHIGYLPQD-------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvdavimgdVELWK--VKQERDRIYSLPEmSEE--DGMKVADLESVFAEM-DGYtaesraEEILLEAGidkefhyglmAN 155
Cdd:TIGR01842 401 ---------VELFPgtVAENIARFGENAD-PEKiiEAAKLAGVHELILRLpDGY------DTVIGPGG----------AT 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSV 218
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANaikALKARGITVVVITHRPSLLGCV 520
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
6.85e-15 |
|
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: 72.42 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysvvdavimGDVE 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI---------------------------DGVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 92 LWKVKQE--RDRIYSLPEmseedgmkvadlESVFaeMDGytaeSRAEEILleAGidkefhyglmanvapGWKLRVLLAQA 169
Cdd:cd03228 66 LRDLDLEslRKNIAYVPQ------------DPFL--FSG----TIRENIL--SG---------------GQRQRIAIARA 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 170 LFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRH 213
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAHRLS 156
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-533 |
8.62e-15 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 74.14 E-value: 8.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGF-DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENatfgycpqDSTKDFDND 398
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--------DINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 399 LTlfdwmsQWR----------------TAKHNDLMvrGMLGRL--------LFT----------------ADDSNKKARN 438
Cdd:cd03256 73 LR------QLRrqigmifqqfnlierlSVLENVLS--GRLGRRstwrslfgLFPkeekqralaalervglLDKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 439 CSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG----TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
250
....*....|....*....
gi 1180383029 515 dfqgtFDEYLASIEEKKIA 533
Cdd:cd03256 225 -----FDGPPAELTDEVLD 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
1.08e-14 |
|
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: 73.31 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 17 FENISAKFGNGNRY-----------------GLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeqy 79
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSI--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svvdavIMGDVELWKVKQERDRIY-------------SL-PemseedGMKVADLesvFAE-------MDGYTAESRAEEI 138
Cdd:cd03257 63 ------IFDGKDLLKLSRRLRKIRrkeiqmvfqdpmsSLnP------RMTIGEQ---IAEplrihgkLSKKEARKEAVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 139 LLEA-GIDKEFhyglmANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIII 208
Cdd:cd03257 128 LLVGvGLPEEV-----LNRYPhelsgGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFI 202
|
250 260
....*....|....*....|..
gi 1180383029 209 SHDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03257 203 THDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-506 |
1.42e-14 |
|
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: 72.55 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkWSENATF----------GYCPQ 389
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDVtgvpperrniGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 dstkdfdnDLTLFDWMSQW-------RTAKHNDLMVRGMLGRLLFTADDS---NKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:cd03259 80 --------DYALFPHLTVAeniafglKLRGVPKAEIRARVRELLELVGLEgllNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 460 LVMDEPTNHMDMEAIEALNNALKDF---AG-TLIFVSHDREFVSSLATRII 506
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELqreLGiTTIYVTHDQEEALALADRIA 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
1.42e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysvvdavimgdvelwkvkqe 98
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-------------------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYSL--------PEMSEED---------GMKVADLESVFaemdgytaesraEEILLEAGIDKEFHyglmanvAP--- 158
Cdd:COG1134 86 NGRVSALlelgagfhPELTGREniylngrllGLSRKEIDEKF------------DEIVEFAELGDFID-------QPvkt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 ---GWKLRVLLAQALFANPDILLLDEptnnldihtitWLA--------------NELNKRKCTMIIISHDRHFLNSVCTH 221
Cdd:COG1134 147 yssGMRARLAFAVATAVDPDILLVDE-----------VLAvgdaafqkkclariRELRESGRTVIFVSHSMGAVRRLCDR 215
|
250
....*....|..
gi 1180383029 222 MADIDYGELRIY 233
Cdd:COG1134 216 AIWLEKGRLVMD 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-531 |
1.42e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.63 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLvNELKSNE-GEIKwsenatFGYCPQDSTKDFDN 397
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEaGTIR------VGDITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 DLTLFDWMSQW-------------RTAKHN----DLMVRGM-------LGRLLFT----ADDSNKKARNCSGGEKNRLLF 449
Cdd:PRK11264 76 QKGLIRQLRQHvgfvfqnfnlfphRTVLENiiegPVIVKGEpkeeataRARELLAkvglAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 450 GKLMMQDVNVLVMDEPTNHMDMEAI-EALNN--ALKDFAGTLIFVSHDREFVSSLATRIIDIkDKQVIDFQGTFDEYLAS 526
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFM-DQGRIVEQGPAKALFAD 234
|
....*
gi 1180383029 527 IEEKK 531
Cdd:PRK11264 235 PQQPR 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
1.47e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 76.25 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAF------EQYSVVDAV 85
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRrvsvcaQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 IMGDVELWKvkqerdriyslPEMSEEDGMKVadLESVfaemdgytaesRAEEIL--LEAGIDKEFHYGlMANVAPGWKLR 163
Cdd:TIGR02868 425 VRENLRLAR-----------PDATDEELWAA--LERV-----------GLADWLraLPDGLDTVLGEG-GARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHD 211
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAalSGRTVVLITHH 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
2.43e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ------- 73
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN-GRPLADWSPAElarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 --------FAFeqySVVDAVIMGDVELWKVKQERDRIYslpemseEDGMKVADLESvFAEMDgYTAESRAEeilleagid 145
Cdd:PRK13548 81 lpqhsslsFPF---TVEEVVAMGRAPHGLSRAEDDALV-------AAALAQVDLAH-LAGRD-YPQLSGGE--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 146 kefhyglmanvapgwKLRVLLAQAL--FANPD----ILLLDEPTNNLDI---HTITWLANEL-NKRKCTMIIISHDrhfL 215
Cdd:PRK13548 140 ---------------QQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqHHVLRLARQLaHERGLAVIVVLHD---L 201
|
.
gi 1180383029 216 N 216
Cdd:PRK13548 202 N 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
2.56e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPGLK----VGN 68
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInninynklDHKLAaqlgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 69 LSQDQFAFEQYSVVDAVIMGDVELWKVKqerdriyslpemseedGMKVADlesvFAEMdgytaESRAEEILLEAGIDKEF 148
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVC----------------GVNIID----WREM-----RVRAAMMLLRVGLKVDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 149 HYgLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISHDRHFLNSVC---THM 222
Cdd:PRK09700 140 DE-KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICdryTVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 223 ADidygelriypGNYekfleaaglqreqlLAENAKKSAEIDEL------QDFVNRFGANASKAKQASSRAkkmdkikLDE 296
Cdd:PRK09700 219 KD----------GSS--------------VCSGMVSDVSNDDIvrlmvgRELQNRFNAMKENVSNLAHET-------VFE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 297 VKASSRmspslsFDEGKkmyrqaleVNKLghgfdgetlfsggDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI 376
Cdd:PRK09700 268 VRNVTS------RDRKK--------VRDI-------------SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 377 KWSENATFGYCPQDSTKD-------------FDNDLTLFDWMSQWRTAKHNDLmvRGMLGrlLFTADDSNKKARN----- 438
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKgmayitesrrdngFFPNFSIAQNMAISRSLKDGGY--KGAMG--LFHEVDEQRTAENqrell 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 439 ---C----------SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEALNNALKDFAGTLIFVSHDREFVSSLA 502
Cdd:PRK09700 397 alkChsvnqnitelSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVC 476
|
....
gi 1180383029 503 TRII 506
Cdd:PRK09700 477 DRIA 480
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
3.78e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 75.02 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQF-GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----TPGLK-------VGNL 69
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADadswrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 70 SQDQFAFEQySVVDAVIMGDvelwkvkqerdriyslPEMSEEDGMKVADLesvfAEMDGYTAEsraeeilLEAGIDKEFH 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR----------------PDASDAEIREALER----AGLDEFVAA-------LPQGLDTPIG 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 150 YGlMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISHDRH 213
Cdd:TIGR02857 454 EG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeaeVLEALRALAQGR-TVLLVTHRLA 518
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
421-530 |
3.94e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 75.28 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 421 MLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAGTLIFVSHDREFVSS 500
Cdd:PLN03073 327 ILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNT 406
|
90 100 110
....*....|....*....|....*....|
gi 1180383029 501 LATRIIDIKDKQVIDFQGTFDEYLASIEEK 530
Cdd:PLN03073 407 VVTDILHLHGQKLVTYKGDYDTFERTREEQ 436
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-233 |
4.26e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 71.16 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeQYSV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-----------------DGKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 VDAVImgdvelwkvkqeRDRIYSLPemsEEDG----MKVADLESVFAEMDGYT---AESRAEEILleagidKEFHYGLMA 154
Cdd:cd03269 64 LDIAA------------RNRIGYLP---EERGlypkMKVIDQLVYLAQLKGLKkeeARRRIDEWL------ERLELSEYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 155 NV-----APGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADID 226
Cdd:cd03269 123 NKrveelSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLN 202
|
....*..
gi 1180383029 227 YGELRIY 233
Cdd:cd03269 203 KGRAVLY 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-189 |
5.22e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-----------TPGLKVGNL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 70 SQD-QFAFEqYSVVDAVIMGDVelwkvkqerdriyslPEMSEEDGMKVADLESVFAEMDgytaesRAEeilLEAGIDKEF 148
Cdd:PRK09536 83 PQDtSLSFE-FDVRQVVEMGRT---------------PHRSRFDTWTETDRAAVERAME------RTG---VAQFADRPV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1180383029 149 hyglmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH 189
Cdd:PRK09536 138 -----TSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-226 |
5.42e-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: 71.31 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlsqdqfafEQYSVVDAVIMGDVELWK 94
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR---------------HDGGWVDLAQASPREILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 95 VKqeRDRI-Y------SLPEMSEEDgmkvadlesVFAE------MDGYTAESRAEEILLEAGIDKEFHyglmaNVAP--- 158
Cdd:COG4778 90 LR--RRTIgYvsqflrVIPRVSALD---------VVAEpllergVDREEARARARELLARLNLPERLW-----DLPPatf 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 159 --GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADID 226
Cdd:COG4778 154 sgGEQQRVNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-518 |
5.67e-14 |
|
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: 70.03 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGE--TLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkwsenaTFGYCPQDSTKDfdn 397
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI------TLDGVPVSDLEK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 dlTLFDWMSQWRTAKHndlmvrgmlgrlLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEA 473
Cdd:cd03247 72 --ALSSLISVLNQRPY------------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1180383029 474 IEALNNALKDfaGTLIFVSHDREFVSSlATRIIDIKDKQVIdFQG 518
Cdd:cd03247 138 LSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKII-MQG 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-245 |
6.03e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 74.42 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYSVV--DAVIM-- 87
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDLR-RRIAVVpqRPHLFdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 88 -------------GDVELWKVkqerdriyslpemseedgMKVADLESVFAEM-DGYtaesraEEILLEAGidkefhyglm 153
Cdd:COG4987 424 tlrenlrlarpdaTDEELWAA------------------LERVGLGDWLAALpDGL------DTWLGEGG---------- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL-----NKrkcTMIIISHDRHFLNSVcTHMADIDYG 228
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLlealaGR---TVLLITHRLAGLERM-DRILVLEDG 545
|
250
....*....|....*..
gi 1180383029 229 ELrIYPGNYEKFLEAAG 245
Cdd:COG4987 546 RI-VEQGTHEELLAQNG 561
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-518 |
1.03e-13 |
|
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: 70.30 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAkLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSE----------NATFGYCPQ 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 DstkdfdndltlFDWMSQWRT--------------AKHNDLMVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQ 455
Cdd:cd03264 80 E-----------FGVYPNFTVrefldyiawlkgipSKEVKARVDEVL-ELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 456 DVNVLVMDEPTNHMDMEAIEALNNALKDFAGTLIFV--SHDREFVSSLATRIIDIKDKQVIdFQG 518
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-513 |
1.15e-13 |
|
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: 70.21 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSE-------NATFGYCPQDstkdFD--NDLTL 401
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEkelaafrRRHIGFVFQS----FNllPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 402 FD-----WMSQWRTAKHNDLMVRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----- 470
Cdd:cd03255 100 LEnvelpLLLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDsetgk 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1180383029 471 --MEAIEALNnalKDFAGTLIFVSHDREFVsSLATRIIDIKDKQV 513
Cdd:cd03255 178 evMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-231 |
2.03e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 69.32 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPL----FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVgnlSQDQFAF 76
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDV---VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 77 EQYsvvdaviMGdvelwkVKQERDRIYslpemseeDGMKVADLESVFAE---MDGYTAESRAEEILLEAGIdKEFHYGLM 153
Cdd:cd03266 77 RRR-------LG------FVSDSTGLY--------DRLTARENLEYFAGlygLKGDELTARLEELADRLGM-EELLDRRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03266 135 GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
.
gi 1180383029 231 R 231
Cdd:cd03266 215 V 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
2.43e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglKVGNLSQDQFAFEQYSVVDAVIMGDV---ELWK 94
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW----IFKDEKNKKKTKEKEKVLEKLVIQKTrfkKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 95 VKQERDRI--------YSLPEMS-EEDGMkvadLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVL 165
Cdd:PRK13651 100 IKEIRRRVgvvfqfaeYQLFEQTiEKDII----FGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1180383029 166 LAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRKCTMIIISHD 211
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQgvkEILEIFDNLNKQGKTIILVTHD 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
330-511 |
3.28e-13 |
|
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: 67.56 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 330 DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLvNEL-KSNEGEIkwsenatfgYCPQDSTkdfdndlTLFdwMSQw 408
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLwPWGSGRI---------GMPEGED-------LLF--LPQ- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 409 RTakhndLMVRGML-GRLLFTADDsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAGT 487
Cdd:cd03223 72 RP-----YLPLGTLrEQLIYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGIT 140
|
170 180
....*....|....*....|....
gi 1180383029 488 LIFVSHdREFVSSLATRIIDIKDK 511
Cdd:cd03223 141 VISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-231 |
3.29e-13 |
|
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: 69.07 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafEQYSVVdavimgdvelwkvkQE 98
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI----------------NGYSIR--------------TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYS----------LPemseeDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYglmANVA-----PGWKLR 163
Cdd:cd03263 70 RKAARQslgycpqfdaLF-----DELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDK---ANKRartlsGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLDIHT--ITW-LANELnKRKCTMIIISHDRHFLNSVCTHMADIDYGELR 231
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASrrAIWdLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-210 |
3.39e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpgLKVGNLSQDQFAFEQYSV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV---LGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 VDAVIMGDVElWKVKQerdriySLPEMSEEDGMKVADLESVFAemdgytaeSRAEEILLEAGIDKEfhyglMANVAPGWK 161
Cdd:PRK13536 119 VPQFDNLDLE-FTVRE------NLLVFGRYFGMSTREIEAVIP--------SLLEFARLESKADAR-----VSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLDIHT--ITW--LANELNKRKcTMIIISH 210
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLARGK-TILLTTH 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-233 |
3.45e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.10 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 17 FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT------PGLKVGnlsqdqfaFE-QYSVVDAVIMgd 89
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsslLGLGGG--------FNpELTGRENIYL-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 90 velwkvkqeRDRIYslpemseedGMKVADLESVFAEMdgytaESRAEeilLEAGIDKEF-HYglmanvAPGWKLRVLLAQ 168
Cdd:cd03220 108 ---------NGRLL---------GLSRKEIDEKIDEI-----IEFSE---LGDFIDLPVkTY------SSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 169 ALFANPDILLLDEptnnldihtitWLA--------------NELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIY 233
Cdd:cd03220 156 ATALEPDILLIDE-----------VLAvgdaafqekcqrrlRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-210 |
4.78e-13 |
|
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: 68.80 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAE-PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYSVV-- 82
Cdd:cd03253 5 NVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLR-RAIGVVpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 83 DAVIMGDVELWKVKqerdriYSLPEMSEED---GMKVADLESVFAEM-DGYtaesraEEILLEAGidkefhygLManVAP 158
Cdd:cd03253 83 DTVLFNDTIGYNIR------YGRPDATDEEvieAAKAAQIHDKIMRFpDGY------DTIVGERG--------LK--LSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-213 |
5.03e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 68.61 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQF--GAEPL--FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAf 76
Cdd:COG4181 8 IIELRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDARA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 77 eqysVVDAVIMGDV----ELwkvkqerdriysLPEMSeedgmkvAdLESVF--AEMDGYT-AESRAEEILLEAGI-DKEF 148
Cdd:COG4181 86 ----RLRARHVGFVfqsfQL------------LPTLT-------A-LENVMlpLELAGRRdARARARALLERVGLgHRLD 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 149 HYglmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDRH 213
Cdd:COG4181 142 HY-------PaqlsgGEQQRVALARAFATEPAILFADEPTGNLDAATgeqIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
331-477 |
5.51e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 331 GETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWS-ENATFGYCPQDST----KDFDND-LTLFDW 404
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEACHylghRNAMKPaLTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 405 MSQWRTAKHN-DLMVRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEAL 477
Cdd:PRK13539 94 LEFWAAFLGGeELDIAAALEAVgL--APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
6.30e-13 |
|
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: 68.17 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGnvsitpglkvgnlsqdqfafeqysv 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vDAVIMGDVELWKVKQERDRIYSLPEM-SEEDGMKVADLESVFAEMDGYTAESRAEEI--LLEAGIDKEFHYGLMANVAP 158
Cdd:cd03265 56 -RATVAGHDVVREPREVRRRIGIVFQDlSVDDELTGWENLYIHARLYGVPGAERRERIdeLLDFVGLLEAADRLVKTYSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIII-SHDRHFLNSVCTHMADIDYGELR 231
Cdd:cd03265 135 GMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahVWEYIEKLKEEFGMTILLtTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-210 |
8.51e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVgnlsqdQFAfeqySVVDA- 84
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-GEPV------RFR----SPRDAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 85 ---VIMgdvelwkVKQERdriySL-PEMSeedgmkVAdlESVF-------------AEMdgytaESRAEEILLEAGIDke 147
Cdd:COG1129 78 aagIAI-------IHQEL----NLvPNLS------VA--ENIFlgreprrgglidwRAM-----RRRARELLARLGLD-- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 148 fhyglmanVAPGWKLR---------VLLAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISH 210
Cdd:COG1129 132 --------IDPDTPVGdlsvaqqqlVEIARALSRDARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISH 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-514 |
9.65e-13 |
|
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: 67.53 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLF----SGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSEN-------------- 381
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 382 ATFGYCPQDSTKDFDNDLTLFD-----WMSQWRTAKHNDLMVRGMLGRLLFTADDS--NKKARNCSGGEKNRLLFGKLMM 454
Cdd:cd03257 82 KEIQMVFQDPMSSLNPRMTIGEqiaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 455 QDVNVLVMDEPTNHMDM----EAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03257 162 LNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-506 |
1.33e-12 |
|
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: 67.92 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK--------WSENAT---FGYCP 388
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARarrVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 389 QDStkDFDNDLTLFDWMSQWRT---------AKHNDLMVRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:TIGR03873 82 QDS--DTAVPLTVRDVVALGRIphrslwagdSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 460 LVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRII 506
Cdd:TIGR03873 159 LLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVV 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
1.41e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.43 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQD-------- 72
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVNDPKVDerlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 73 -----QF-AFEQYSVVDAVIMGDVelwKVKqerdriyslpemseedGMKVADlesvfaemdgytAESRAEEILLEAGI-D 145
Cdd:PRK09493 80 gmvfqQFyLFPHLTALENVMFGPL---RVR----------------GASKEE------------AEKQARELLAKVGLaE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 146 KEFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHM 222
Cdd:PRK09493 129 RAHHYP--SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
....*.
gi 1180383029 223 ADIDYG 228
Cdd:PRK09493 207 IFIDKG 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-514 |
1.51e-12 |
|
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: 66.92 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENA-------TFGYCPQDst 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnRIGYLPEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 393 KDFDNDLTLFD---WMSQWRTAKHNDLM--VRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTN 467
Cdd:cd03269 79 RGLYPKMKVIDqlvYLAQLKGLKKEEARrrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 468 HMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03269 158 GLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-230 |
1.57e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.66 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAE-PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAFEQYS 80
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-GQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VvdAVIMGDVELwkvkqerdriysLPEMSEEDGMKVAdLESVfaEMDGYTAESRAEEILLEAGIdKEFHYGLMANVAPGW 160
Cdd:cd03292 80 I--GVVFQDFRL------------LPDRNVYENVAFA-LEVT--GVPPREIRKRVPAALELVGL-SHKHRALPAELSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 161 KLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-211 |
2.47e-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: 66.72 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF-AFEQYSVVDavimgdvelWKVK 96
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-GKQITEPGPDRMvVFQNYSLLP---------WLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 97 qeRDRIY-----SLPEMSEEDGMKVADlESVfaEMDGYT--AESRAEEIlleagidkefhyglmanvAPGWKLRVLLAQA 169
Cdd:TIGR01184 72 --RENIAlavdrVLPDLSKSERRAIVE-EHI--ALVGLTeaADKRPGQL------------------SGGMKQRVAIARA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 170 LFANPDILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHD 211
Cdd:TIGR01184 129 LSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
2.55e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqys 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvdavimGDVELWKV--KQERDRIYSLPE--MSEEdGMKVADL--------ESVFAEMDGyTAESRAEEILLEAGIDkEF 148
Cdd:PRK11231 62 -------GDKPISMLssRQLARRLALLPQhhLTPE-GITVRELvaygrspwLSLWGRLSA-EDNARVNQAMEQTRIN-HL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 149 HYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI-HTITW--LANELNKRKCTMIIISHDrhfLNSVC 219
Cdd:PRK11231 132 ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInHQVELmrLMRELNTQGKTVVTVLHD---LNQAS 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-526 |
3.22e-12 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 68.78 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFS--GGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSN---EGEIKWSENATF--------- 384
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 385 --GYCPQDSTKDFdNDLTLFDWM----------SQWRTAKHNDLMVRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKL 452
Cdd:COG1123 84 riGMVFQDPMTQL-NPVTVGDQIaealenlglsRAEARARVLELLEAVGLERRL------DRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 453 MMQDVNVLVMDEPTNHMDM----EAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDEYLAS 526
Cdd:COG1123 157 LALDPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV-EDGPPEEILAA 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
3.71e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAE--PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeq 78
Cdd:PRK13632 7 MIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 79 ysvvDAVIMGDVELWKVKQERDRIYSLPEmSEEDGMKVAD-----LESV---FAEMDGYTAESrAEEILLEAGIDKEFHy 150
Cdd:PRK13632 69 ----DGITISKENLKEIRKKIGIIFQNPD-NQFIGATVEDdiafgLENKkvpPKKMKDIIDDL-AKKVGMEDYLDKEPQ- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 151 glmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANEL-NKRKCTMIIISHD 211
Cdd:PRK13632 142 ----NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLrKTRKKTLISITHD 202
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
315-505 |
3.83e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 66.29 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSENA---- 382
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVlfggtdltGLDEHEiarl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 383 ----TFgycpQDSTKdFDNdLTLFD------------W--MSQWRTAKHNDLmVRGMLgRLLFTADDSNKKARNCSGGEK 444
Cdd:COG4674 86 gigrKF----QKPTV-FEE-LTVFEnlelalkgdrgvFasLFARLTAEERDR-IEEVL-ETIGLTDKADRLAGLLSHGQK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 445 NRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG--TLIFVSHDREFVSSLATRI 505
Cdd:COG4674 158 QWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHDMEFVRQIARKV 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
4.11e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYS 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATTPSRELA-KRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VvdavimgdvelwkVKQE---------RDRI------YSLPEMSEEDGMKVA------DLESvFA-----EMDGytaesr 134
Cdd:COG4604 79 I-------------LRQEnhinsrltvRELVafgrfpYSKGRLTAEDREIIDeaiaylDLED-LAdryldELSG------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 135 aeeilleagidkefhyglmanvapGWKLRVLLAQALFANPDILLLDEPTNNLDIH-------TITWLANELNKrkcTMII 207
Cdd:COG4604 139 ------------------------GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKhsvqmmkLLRRLADELGK---TVVI 191
|
....
gi 1180383029 208 ISHD 211
Cdd:COG4604 192 VLHD 195
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-212 |
4.23e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.48 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlsqDQfafeqysv 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN----------GR-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgDVELWKVKQERdRI------YSL-PEMSEED----GMKVADLESvfAEmdgytAESRAEEILLEAGIDKefhy 150
Cdd:COG1118 65 -------DLFTNLPPRER-RVgfvfqhYALfPHMTVAEniafGLRVRPPSK--AE-----IRARVEELLELVQLEG---- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 151 glMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTI----TWLANELNKRKCTMIIISHDR 212
Cdd:COG1118 126 --LADRYPsqlsgGQRQRVALARALAVEPEVLLLDEPFGALDAKVRkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-522 |
4.58e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.19 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYcpqdSTKDFDNDL 399
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML----SSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 400 TLFD---------------------WMSQW-RTAKHNDLMVRGMLGRLlFTADDSNKKARNCSGGEKNRLLFGKLMMQDV 457
Cdd:PRK11231 79 ALLPqhhltpegitvrelvaygrspWLSLWgRLSAEDNARVNQAMEQT-RINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 458 NVLVMDEPTNHMD-------MEAIEALNNALKdfagTLIFVSHDREFVSSLATRIIDIKDKQVIDfQGTFDE 522
Cdd:PRK11231 158 PVVLLDEPTTYLDinhqvelMRLMRELNTQGK----TVVTVLHDLNQASRYCDHLVVLANGHVMA-QGTPEE 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
4.66e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglKVGN--------LSQD 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI------RVGDitidtarsLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 73 Q-----------FAFEQY------SVVDAVIMGDVELWKVKQERdriyslpemseedgmkvadlesvfaemdgytAESRA 135
Cdd:PRK11264 77 KglirqlrqhvgFVFQNFnlfphrTVLENIIEGPVIVKGEPKEE-------------------------------ATARA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 136 EEILLEAGID-KEFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANElnKRkcTMII 207
Cdd:PRK11264 126 RELLAKVGLAgKETSYP--RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQE--KR--TMVI 199
|
250 260
....*....|....*....|.
gi 1180383029 208 ISHDRHFLNSVCTHMADIDYG 228
Cdd:PRK11264 200 VTHEMSFARDVADRAIFMDQG 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-222 |
4.73e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----------TPG-LKVGNLS 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdKDGqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 71 QDQFAFEQYSVVdaviMGDVELWKVKQERDRIYSLPemseedgMKVADLESvfaemdgYTAESRAEEILLEAGIDKEFHY 150
Cdd:PRK10619 86 QLRLLRTRLTMV----FQHFNLWSHMTVLENVMEAP-------IQVLGLSK-------QEARERAVKYLAKVGIDERAQG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 151 GLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHM 222
Cdd:PRK10619 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-190 |
5.56e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT------PGLKVGNLSQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 75 AFEQYSVVDAVIMGdVELWKV-KQERdriyslpemseedgmkvadlesvfaemdgytaESRAEEILLEAGIDkEFHYGLM 153
Cdd:PRK11248 81 LLPWRNVQDNVAFG-LQLAGVeKMQR--------------------------------LEIAHQMLKKVGLE-GAEKRYI 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 1180383029 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT 190
Cdd:PRK11248 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-514 |
5.70e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 63.99 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKdfdndl 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 400 tlfdwmsqwrtakhndlmvrgmLG-RLLFtaddsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALN 478
Cdd:cd03216 75 ----------------------AGiAMVY----------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 1180383029 479 NALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03216 123 KVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
7.40e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.44 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS-QDQ---FAFE 77
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-GEDATDVPvQERnvgFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 78 QY------SVVDAVIMGdvelWKVKQERDRiysLPEmseedgmkvadlesvfAEMDGytaesRAEEILLEAGIDKefhyg 151
Cdd:cd03296 82 HYalfrhmTVFDNVAFG----LRVKPRSER---PPE----------------AEIRA-----KVHELLKLVQLDW----- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 152 lMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIISHD 211
Cdd:cd03296 129 -LADRYPaqlsgGQRQRVALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHD 196
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-218 |
8.25e-12 |
|
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: 67.47 E-value: 8.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfeQYsvvdaviMG--- 88
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-GADLSQWDREELG--RH-------IGylp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 89 -DVELWK--VKQErdrIYSLPEmseedgmkvADLESVFA--------EM-----DGYtaesraEEILLEAGidkefhygl 152
Cdd:COG4618 413 qDVELFDgtIAEN---IARFGD---------ADPEKVVAaaklagvhEMilrlpDGY------DTRIGEGG--------- 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 153 mANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITwlanELNKRKCTMIIISHDRHFLNSV 218
Cdd:COG4618 466 -ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLLAAV 533
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-508 |
1.48e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW------SENAT-----FGYCP 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddveALSARaasrrVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 389 QDSTKDFDND------------LTLFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSnkkarnCSGGEKNRLLFGKLMMQD 456
Cdd:PRK09536 84 QDTSLSFEFDvrqvvemgrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTS------LSGGERQRVLLARALAQA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 457 VNVLVMDEPTNHMDM-EAIEALNNA--LKDFAGTLIFVSHDREfvssLATRIIDI 508
Cdd:PRK09536 158 TPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDLD----LAARYCDE 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-247 |
1.60e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnLSQDQfafeqysvvdav 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI----------LLDAQ------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 imgDVELWKVKQERDRIYSLP-EMSEEDGMKVADLESV-----FAEMDGYTAESRA--EEILLEAGIdKEFHYGLMANVA 157
Cdd:PRK10575 74 ---PLESWSSKAFARKVAYLPqQLPAAEGMTVRELVAIgrypwHGALGRFGAADREkvEEAISLVGL-KPLAHRLVDSLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDI-HTITWLA--NELNK-RKCTMIIISHDRHFLNSVCTHMADIDYGELrIY 233
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEM-IA 228
|
250
....*....|....
gi 1180383029 234 PGNYEKFLEAAGLQ 247
Cdd:PRK10575 229 QGTPAELMRGETLE 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
338-514 |
1.63e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 63.85 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 338 GDFLLEA-----GAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSenatfGYCPQDSTKDFD------------NDLT 400
Cdd:cd03297 11 PDFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-----GTVLFDSRKKINlppqqrkiglvfQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 LFDWMS----------QWRTAKHNDLmVRGMLGRLlftADDSNKKAR--NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNH 468
Cdd:cd03297 86 LFPHLNvrenlafglkRKRNREDRIS-VDELLDLL---GLDHLLNRYpaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 469 MD----MEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03297 162 LDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-187 |
1.72e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAeplF---ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITPG-----LKVGNLSQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGdiatrRRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 73 qfAFEQYSvvdavimgdvELwKVKQERD---RIYSLPEmsEEDGMKVADLESVFAEMDgyTAESRAEEILLeaGIdkefh 149
Cdd:NF033858 347 --AFSLYG----------EL-TVRQNLElhaRLFHLPA--AEIAARVAEMLERFDLAD--VADALPDSLPL--GI----- 402
|
170 180 190
....*....|....*....|....*....|....*...
gi 1180383029 150 yglmanvapgwKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:NF033858 403 -----------RQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-211 |
1.78e-11 |
|
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: 64.13 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNL---------SQDQFAFEQY------SVV 82
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLkgkalrqlrRQIGMIFQQFnlierlSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 83 DAVIMGdvelwkvkqerdriySLPEMSeedgmKVADLESVFAEMDGYtaesRAEEILLEAGIDkEFHYGLMANVAPGWKL 162
Cdd:cd03256 97 ENVLSG---------------RLGRRS-----TWRSLFGLFPKEEKQ----RALAALERVGLL-DKAYQRADQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 163 RVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKrkcTMIIISHD 211
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQ 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-506 |
1.79e-11 |
|
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: 64.12 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCL--VNELKSN---EGEIKWSenatfgycPQDSTKD 394
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGapdEGEVLLD--------GKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 FDNDL-------------TLFD-----------WMSQWRTAKHNDLMVRGMLGR-LLFTADDSNKKARNCSGGEKNRLLF 449
Cdd:cd03260 73 DVDVLelrrrvgmvfqkpNPFPgsiydnvayglRLHGIKLKEELDERVEEALRKaALWDEVKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 450 GKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG--TLIFVSHDREFVSSLATRII 506
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADRTA 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-278 |
3.01e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQFAFEQyS 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLLALRQ-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VVDAVIMGDVELWKVKQERDRIYSLPEMSeedgmkVADLESVFAEMDGYTaesraeeiLLEAgidKEFHYGLMANVAPGW 160
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDSDIAFSLRNLG------VPEAEITRRVDEALT--------LVDA---QHFRHQPIQCLSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 161 KLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKrkctMIIISHDRHFLNSVCTHMADIDYGELRIY 233
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 234 --PGNY---EKFLEAAGLQREQLLAENAKKSAEIDELQ-DFVNRFGANASK 278
Cdd:PRK13638 218 gaPGEVfacTEAMEQAGLTQPWLVKLHTQLGLPLCKTEtEFFHRMQKCAFR 268
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
3.06e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.71 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqys 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvDAVIMGDVELwkvkQERDrI------YSL-PEMSEED----GMKVADLESvfAEMDgytaeSRAEEILLEAGIDkefH 149
Cdd:COG3839 63 --GGRDVTDLPP----KDRN-IamvfqsYALyPHMTVYEniafPLKLRKVPK--AEID-----RRVREAAELLGLE---D 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 150 YglmANVAPGwKL------RVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHD 211
Cdd:COG3839 126 L---LDRKPK-QLsggqrqRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-522 |
3.19e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 63.16 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGE--------IKWSEN--ATFGYCPQ 389
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 DSTkdFDNDLTLFD---WMSQWRTAKHNDLMVR-GMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEP 465
Cdd:cd03265 81 DLS--VDDELTGWEnlyIHARLYGVPGAERRERiDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 466 TNHMDMEA-------IEALNnalKDFAGTLIFVSHDREFVSSLATRIIdIKDKQVIDFQGTFDE 522
Cdd:cd03265 159 TIGLDPQTrahvweyIEKLK---EEFGMTILLTTHYMEEAEQLCDRVA-IIDHGRIIAEGTPEE 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-230 |
4.13e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----------SITPGLKVGNLSQdqf 74
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 75 afeqysvvDAVIMGDVELwkvkQE---RDRIYSLPEMSEedgMKVADLESVFAEMdgytaesRAEEI--LLEAGIDkefh 149
Cdd:PRK10253 89 --------NATTPGDITV----QElvaRGRYPHQPLFTR---WRKEDEEAVTKAM-------QATGIthLADQSVD---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 150 yglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI-HTITWLA--NELNKRK-CTMIIISHDrhfLNSVC---THM 222
Cdd:PRK10253 143 -----TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNREKgYTLAAVLHD---LNQACryaSHL 214
|
....*...
gi 1180383029 223 ADIDYGEL 230
Cdd:PRK10253 215 IALREGKI 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
339-526 |
4.54e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 64.36 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSenatfGYCPQDSTKDFD------------NDLTLFdwms 406
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-----GRTLFDSRKGIFlppekrrigyvfQEARLF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 407 qwrtaKHndLMVRGML--GRLLFTADDSN-----------------KKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTN 467
Cdd:TIGR02142 88 -----PH--LSVRGNLryGMKRARPSERRisferviellgighllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 468 HMDM----EAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFqGTFDEYLAS 526
Cdd:TIGR02142 161 ALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWAS 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-508 |
5.29e-11 |
|
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: 65.00 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGG-DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENatfgycpqdSTKDFDN 397
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPvSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---------PLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 DltlfDWMSQWRTAKHNDLMVRG------MLGRLLFTADDSNKKARNC------------------------SGGEKNRL 447
Cdd:TIGR02857 392 D----SWRDQIAWVPQHPFLFAGtiaeniRLARPDASDAEIREALERAgldefvaalpqgldtpigeggaglSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 448 LFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG--TLIFVSHDREfVSSLATRIIDI 508
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA-LAALADRIVVL 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
339-531 |
5.77e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATF------GycpqdstkdFDNDLTLFDwmsqwrtak 412
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAllelgaG---------FHPELTGRE--------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 413 hNdlmVRgMLGRLL-FTADDSNKKA-----------------RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME-- 472
Cdd:COG1134 108 -N---IY-LNGRLLgLSRKEIDEKFdeivefaelgdfidqpvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfq 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 473 --AIEALNNALKDfAGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDE----YLASIEEKK 531
Cdd:COG1134 183 kkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLV-MDGDPEEviaaYEALLAGRE 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-494 |
6.48e-11 |
|
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: 64.69 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDG-ETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSEN---ATFGYC 387
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQDSTkdfdndltLFDwmsqwrTAKHNDLMV---------------RGMLGRLLFTADDS-----NKKARNCSGGEKNRL 447
Cdd:TIGR02868 415 AQDAH--------LFD------TTVRENLRLarpdatdeelwaaleRVGLADWLRALPDGldtvlGEGGARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 448 LFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALkdFAG----TLIFVSHD 494
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL--LAAlsgrTVVLITHH 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
6.59e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSqdqfafeqySVVDAVIMgdvelwkvKQE 98
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLS---------SAAKAELR--------NQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYS----LPEMSEedgmkvadLESV-----FAEMDGYTAESRAEEILLEAGIDKEFHYgLMANVAPGWKLRVLLAQA 169
Cdd:PRK11629 89 LGFIYQfhhlLPDFTA--------LENVampllIGKKKPAEINSRALEMLAAVGLEHRANH-RPSELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 170 LFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCT-MIIISHD 211
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNadsIFQLLGELNRLQGTaFLVVTHD 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-508 |
6.64e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCP----------- 388
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsiargllylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 389 QDSTKdfdNDLTLFDWMSQWRtAKHNDLMVRGMLGRLLFTADDsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNH 468
Cdd:cd03231 81 APGIK---TTLSVLENLRFWH-ADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 469 MDMEAIEALNNALKDFA---GTLIFVSHDREFVSSLATRIIDI 508
Cdd:cd03231 156 LDKAGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
6.96e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.80 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYSVV--DAVIM-G 88
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-GVDIRDLTLESLR-RQIGVVpqDTFLFsG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 89 DVelwkvkqeRDRI-YSLPEMSEED---GMKVADLESVFAEM-DGYtaesraEEILLEAGidkefhyglmANVAPGWKLR 163
Cdd:COG1132 429 TI--------RENIrYGRPDATDEEveeAAKAAQAHEFIEALpDGY------DTVVGERG----------VNLSGGQRQR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
8.26e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 32 LIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ----------FAFEQYSVVDAV-IMGDVELWKV-KQER 99
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQMDEEAraklrakhvgFVFQSFMLIPTLnALENVELPALlRGES 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 100 DRiyslpemseedgmkvadlesvfaemdgyTAESRAEEILLEAGIDKEFHYgLMANVAPGWKLRVLLAQALFANPDILLL 179
Cdd:PRK10584 120 SR----------------------------QSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1180383029 180 DEPTNNLDIHT---ITWLANELNKR-KCTMIIISHD 211
Cdd:PRK10584 171 DEPTGNLDRQTgdkIADLLFSLNREhGTTLILVTHD 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
339-533 |
9.20e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 61.97 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWS---------ENATFGYCPQDSTkdfdndltLFDWMS--- 406
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQNYA--------LFPHMTvyk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 407 --------QWRTAKHNDLMVR---GMLG--RLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA 473
Cdd:cd03299 91 niayglkkRKVDKKEIERKVLeiaEMLGidHLL------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 474 IEALNNALKD----FAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFqGTFDEYLASIEEKKIA 533
Cdd:cd03299 165 KEKLREELKKirkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEEVFKKPKNEFVA 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
9.64e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 61.97 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQD--QFAFeqysvvdavimgdvelwkV 95
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-GKDITNLPPEkrDISY------------------V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 96 KQErdriYSL-PEMSEED----GMKVADLESVfaemdgyTAESRAEEILLEAGIDKEFHYGlMANVAPGWKLRVLLAQAL 170
Cdd:cd03299 77 PQN----YALfPHMTVYKniayGLKKRKVDKK-------EIERKVLEIAEMLGIDHLLNRK-PETLSGGEQQRVAIARAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1180383029 171 FANPDILLLDEPTNNLDIHTITWLANELNK----RKCTMIIISHD 211
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
1.08e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.40 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF-AFEqysvvdavimGDV 90
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRkAFR----------RDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 ELwkVKQE-------RDRI-YSLPE-MSEEDGMKVADlesvfaemdgytAESRAEEILLEAGIDKEFHYGLMANVAPGWK 161
Cdd:PRK10419 92 QM--VFQDsisavnpRKTVrEIIREpLRHLLSLDKAE------------RLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRKCT-MIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVlqaGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
1.40e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.97 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfeqysvvdavimgdvelwKVKQ 97
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-GQDVATLDADALA------------------QLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 98 ER-----DRIYSLPEMSEEDGMKVAdleSVFAEMDGYTAESRAEEILLEAGIDKEFHYGlMANVAPGWKLRVLLAQALFA 172
Cdd:PRK10535 86 EHfgfifQRYHLLSHLTAAQNVEVP---AVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1180383029 173 NPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHD 211
Cdd:PRK10535 162 GGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
340-498 |
1.70e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 340 FLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKDFDNDLTLFDWMSQWRTAKHNDLM-- 417
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILpa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 418 -VRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEAL----NNALKDFAGTLIFVS 492
Cdd:PRK09544 105 lKRVQAGHLI------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVS 178
|
....*.
gi 1180383029 493 HDREFV 498
Cdd:PRK09544 179 HDLHLV 184
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
2.97e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.04 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqys 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvdavimGDVELWKVKQERDRI------YSL-PEMSEED----GMKVADLESvfAEmdgytAESRAEEIL----LEAgid 145
Cdd:COG3842 65 -------DGRDVTGLPPEKRNVgmvfqdYALfPHLTVAEnvafGLRMRGVPK--AE-----IRARVAELLelvgLEG--- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 146 kefhyglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHDR 212
Cdd:COG3842 128 -------LADRYPhqlsgGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
3.29e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----TPGlkvgnlsqdqfafe 77
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepVPS-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 78 qysvvdavimgdvelwKVKQERDRIYSLPEMSEED-GMKVADLESVFAEMDGYTAESRAEEI--LLEAGIDKEFHYGLMA 154
Cdd:PRK13537 74 ----------------RARHARQRVGVVPQFDNLDpDFTVRENLLVFGRYFGLSAAAARALVppLLEFAKLENKADAKVG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYG 228
Cdd:PRK13537 138 ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPqarHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-529 |
3.43e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCL--VNELKSNEGEIKWSenatFGYCPQ-------- 389
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYH----VALCEKcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 ----------DSTKDFDNDLTLFDWMSQWRTAKHNDLM----------------VRGMLGRLLFTADDSNKKA------- 436
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygddtvldnVLEALEEIGYEGKEAVGRAvdliemv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 437 ----------RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNAL----KDFAGTLIFVSHDREFVSSLA 502
Cdd:TIGR03269 157 qlshrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|....*..
gi 1180383029 503 TRIIDIKDKQVIDfQGTFDEYLASIEE 529
Cdd:TIGR03269 237 DKAIWLENGEIKE-EGTPDEVVAVFME 262
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-506 |
3.98e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQF-GAEPLfENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVgnlsqdQFAfeqySVVDA 84
Cdd:PRK11288 9 GIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-GQEM------RFA----STTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 85 VIMGDVELWkvkQErdrIYSLPEMSEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDkefhyglmanVAPGWKLRV 164
Cdd:PRK11288 77 LAAGVAIIY---QE---LHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVD----------IDPDTPLKY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 165 L---------LAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISH--DRHF-LNSVCTHMADidyge 229
Cdd:PRK11288 141 LsigqrqmveIAKALARNARVIAFDEPTSSLSAREIEQLfrvIRELRAEGRVILYVSHrmEEIFaLCDAITVFKD----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 230 lriypGNY-EKFLEAAGLQREQLLAENAKKsaEIDELQDFvnrfganaskakqaSSRAKKMDKIKLDEVKASSRMSPsLS 308
Cdd:PRK11288 216 -----GRYvATFDDMAQVDRDQLVQAMVGR--EIGDIYGY--------------RPRPLGEVRLRLDGLKGPGLREP-IS 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 309 FDegkkmYRQalevnklghgfdGETLfsgGDFlleagaklaviGENGVGKTTFLRCLVNELKSNEGEI------------ 376
Cdd:PRK11288 274 FS-----VRA------------GEIV---GLF-----------GLVGAGRSELMKLLYGATRRTAGQVyldgkpidirsp 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 377 KWSENATFGYCPQDSTKD--------FDN--------DLTLFDWMSQWRTAKHNDLMVRgmlgRLLFTADDSNKKARNCS 440
Cdd:PRK11288 323 RDAIRAGIMLCPEDRKAEgiipvhsvADNinisarrhHLRAGCLINNRWEAENADRFIR----SLNIKTPSREQLIMNLS 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 441 GGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRII 506
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqgvAVLFVSSDLPEVLGVADRIV 467
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
4.55e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFafeqysvvdavimgdveLWKVKQE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKY-----------------IRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYSLPEMSE-EDGMkvaDLESVFA----EMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:PRK13646 87 IGMVFQFPESQLfEDTV---EREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1180383029 174 PDILLLDEPTNNLD-------IHTITWLANELNKrkcTMIIISHD 211
Cdd:PRK13646 164 PDIIVLDEPTAGLDpqskrqvMRLLKSLQTDENK---TIILVSHD 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
332-511 |
4.78e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 332 ETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSenatfgyCPQDstkDFDNDLTLFDWMSQWRTA 411
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------VPDN---QFGREASLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 412 KhndlMVRGMLGRL-LFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNALKDFAG 486
Cdd:COG2401 113 K----DAVELLNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGI 188
|
170 180
....*....|....*....|....*
gi 1180383029 487 TLIFVSHDREFVSSLATRIIDIKDK 511
Cdd:COG2401 189 TLVVATHHYDVIDDLQPDLLIFVGY 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-526 |
5.02e-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: 59.55 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI-----------KWSENATFGYCPQDST----------KDFDN 397
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVLQDTFlfsgtimeniRLGRP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 DLTLFDWMSQWRTAKHNDLMVRgmLGRLLFTAddSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEAL 477
Cdd:cd03254 103 NATDEEVIEAAKEAGAHDFIMK--LPNGYDTV--LGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 478 NNAL-KDFAG-TLIFVSHdREFVSSLATRIIDIKDKQVIDfQGTFDEYLAS 526
Cdd:cd03254 179 QEALeKLMKGrTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGTHDELLAK 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
329-526 |
5.71e-10 |
|
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: 59.71 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 329 FDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNEL---KSNE----GEIKWSEN-----ATFGYCPQDSTKDFD 396
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptYGNDvrlfGERRGGEDvwelrKRIGLVSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 397 NDLT--------LFDWMSQWRTAKHNDLM-VRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPT 466
Cdd:COG1119 93 RDETvldvvlsgFFDSIGLYREPTDEQRErARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 467 NHMDMEAIEALNNALKDFAG----TLIFVSHDREFVSSLATRIIDIKDKQVIDfQGTFDEYLAS 526
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAegapTLVLVTHHVEEIPPGITHVLLLKDGRVVA-AGPKEEVLTS 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-218 |
5.93e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGalvpsagnvsITPglkvgnlsqdqfafeqYSVVDAV 85
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG----------VYP----------------HGTYEGE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 IMGDVELWKVKQERDriyslpemSEEDG--------MKVADL---ESVF--AE------MDGYTAESRAEEILLEAGID- 145
Cdd:PRK13549 64 IIFEGEELQASNIRD--------TERAGiaiihqelALVKELsvlENIFlgNEitpggiMDYDAMYLRAQKLLAQLKLDi 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 146 ----KEFHYGLmanvapGWKLRVLLAQALFANPDILLLDEPTNNL---DIHTITWLANELNKRKCTMIIISHDrhfLNSV 218
Cdd:PRK13549 136 npatPVGNLGL------GQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISHK---LNEV 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-230 |
6.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 16 LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglKVGNLSQDQFAfeqysvVDAVimgdvelwKV 95
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQ------IDAI--------KL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 96 KQERDRIYS----LPEMSEEDGMKVAdLESvFAEMDGYTAESRAEEILLEAGIDKEFHYGL---MANVAPGWKLRVLLAQ 168
Cdd:PRK14246 89 RKEVGMVFQqpnpFPHLSIYDNIAYP-LKS-HGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 169 ALFANPDILLLDEPTNNLDI---HTITWLANELnKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIvnsQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
339-516 |
7.54e-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: 59.08 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATfgyCPQDSTKDFDNDLTLFDwmsqwrtakhNDLMV 418
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLLGLGGGFNPELTGRE----------NIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 419 RGMLG--------RLLFTADDS------NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD---ME-AIEALNNA 480
Cdd:cd03220 109 GRLLGlsrkeideKIDEIIEFSelgdfiDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafQEkCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1180383029 481 LKDfAGTLIFVSHDREFVSSLATRIIDIKDKQVIDF 516
Cdd:cd03220 189 LKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-210 |
8.06e-10 |
|
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: 59.17 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAE--PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGL------------KVG 67
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-GHdvrdytlaslrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 68 NLSQDQFAFEqysvvDAVimgdvelwkvkqeRDRI-YSLPEMSEEDGM---KVADLESVFAEM-DGYtaesraEEILLEA 142
Cdd:cd03251 80 LVSQDVFLFN-----DTV-------------AENIaYGRPGATREEVEeaaRAANAHEFIMELpEGY------DTVIGER 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 143 GIdkefhyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISH 210
Cdd:cd03251 136 GV----------KLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlVQAALERLMKNR-TTFVIAH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-208 |
8.26e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsQDQF------AFEQysvvdavimgdveLWK-VKQE- 98
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGER------------QSQFshitrlSFEQ-------------LQKlVSDEw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYSLPEMSEEDGMKVAdlesvfAEM--DGYTAESRAEEILLEAGI----DKEFHYglmanVAPGWKLRVLLAQALFA 172
Cdd:PRK10938 84 QRNNTDMLSPGEDDTGRTT------AEIiqDEVKDPARCEQLAQQFGItallDRRFKY-----LSTGETRKTLLCQALMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1180383029 173 NPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIII 208
Cdd:PRK10938 153 EPDLLILDEPFDGLDVASRQQLAEllaSLHQSGITLVLV 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-187 |
9.06e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.50 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlSQDqfafeqysVVDAV 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID--------GED--------VTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 ImgdvelwkvkQERD-----RIYSL-PEMSEED----GMKvadlesvfaeMDGYTAESRAEEI--LLE----AGIDKEFh 149
Cdd:PRK11432 75 I----------QQRDicmvfQSYALfPHMSLGEnvgyGLK----------MLGVPKEERKQRVkeALElvdlAGFEDRY- 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1180383029 150 yglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PRK11432 134 ---VDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-510 |
9.73e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 330 DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLvNEL-KSNEGEIKWSENATFGYCPQ----------------DST 392
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLwPYGSGRIARPAGARVLFLPQrpylplgtlreallypATA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 393 KDFDnDLTLFDWMSQwrtakhndlmVRgmLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME 472
Cdd:COG4178 453 EAFS-DAELREALEA----------VG--LGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1180383029 473 AIEA----LNNALKDfaGTLIFVSHdREFVSSLATRIIDIKD 510
Cdd:COG4178 520 NEAAlyqlLREELPG--TTVISVGH-RSTLAAFHDRVLELTG 558
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-506 |
9.85e-10 |
|
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: 58.70 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLvNEL-KSNEGEIkwsenATFGYCPQDSTKDFDN- 397
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTI-----IIDGLKLTDDKKNINEl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 ---------DLTLFDWMsqwrTAKHNdLM-----VRGM-------LGRLLFT----ADDSNKKARNCSGGEKNRLLFGKL 452
Cdd:cd03262 75 rqkvgmvfqQFNLFPHL----TVLEN-ITlapikVKGMskaeaeeRALELLEkvglADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 453 MMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRII 506
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVI 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
338-526 |
1.20e-09 |
|
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: 60.11 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 338 GDFLLEAGAKL------AVIGENGVGKTTFLRCLVNELKSNEGEIK-----W--SENATF--------GYCPQDStkdfd 396
Cdd:COG4148 12 GGFTLDVDFTLpgrgvtALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLqdSARGIFlpphrrriGYVFQEA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 397 ndlTLFDWMS--------QWRTAKHNDLM----VRGMLG--RLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVM 462
Cdd:COG4148 87 ---RLFPHLSvrgnllygRKRAPRAERRIsfdeVVELLGigHLL------DRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 463 DEPTNHMDMEA-------IEALNnalKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDfQGTFDEYLAS 526
Cdd:COG4148 158 DEPLAALDLARkaeilpyLERLR---DELDIPILYVSHSLDEVARLADHVVLLEQGRVVA-SGPLAEVLSR 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
1.20e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglkvgnlsqdqfafeqys 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvdavimGDVELWKVkqeRDRIYSLpemSEEDGMK----VADLESVFAEMDGyTAESRAEEIL----LEAGIDKEFHYgL 152
Cdd:PRK13539 64 -------GDIDDPDV---AEACHYL---GHRNAMKpaltVAENLEFWAAFLG-GEELDIAAALeavgLAPLAHLPFGY-L 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1180383029 153 MAnvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN 196
Cdd:PRK13539 129 SA----GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-211 |
1.37e-09 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 58.04 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqysvvDAV 85
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI----------------------GGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 86 IMGDVElwkvKQERD-----RIYSL-PEMSEED----GMKVADLESvfAEMDGYTaeSRAEEILleaGIDKEFHYgLMAN 155
Cdd:cd03301 63 DVTDLP----PKDRDiamvfQNYALyPHMTVYDniafGLKLRKVPK--DEIDERV--REVAELL---QIEHLLDR-KPKQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK----RKCTMIIISHD 211
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqqrLGTTTIYVTHD 190
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-211 |
2.02e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglkvgnlsqdqfafeqysvVDAVIMGDVELWKVKQERDRIYsLP 106
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRRKKIAMV-FQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 107 EMSEEDGMKVADLESVFAEMDGYTAESRAE---EILLEAGIDKEFHyGLMANVAPGWKLRVLLAQALFANPDILLLDEPT 183
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREkalDALRQVGLENYAH-SYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190
....*....|....*....|....*....|..
gi 1180383029 184 NNLDIHTITWLANEL----NKRKCTMIIISHD 211
Cdd:PRK10070 193 SALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
2.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 11 FGAEPLFEnISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglKVGNLSQDQFAFEQysvvdavimgdv 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVGDIVVSSTSKQK------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 ELWKVKQERDRIYSLPE--MSEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQ 168
Cdd:PRK13643 78 EIKPVRKKVGVVFQFPEsqLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1180383029 169 ALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISH 210
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-211 |
2.35e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.42 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 32 LIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ---------------FA-FEQYSVVDAVIMGdVELWKV 95
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLID-GQDIAAMSRKElrelrrkkismvfqsFAlLPHRTVLENVAFG-LEVQGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 96 -KQERdriyslpemseedgmkvadlesvfaemdgytaESRAEEILLEAGIdKEFHYGLMANVAPGWKLRVLLAQALFANP 174
Cdd:cd03294 133 pRAER--------------------------------EERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1180383029 175 DILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHD 211
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELlrlqAELQKTIVFITHD 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
2.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 11 FGAEPLFeNISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeqySVVDAVIMGDV 90
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---------------------RVDDTLITSTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 ELWKVKQERDR---IYSLPE--MSEEDGMK-VADLESVFAeMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRV 164
Cdd:PRK13649 76 KNKDIKQIRKKvglVFQFPEsqLFEETVLKdVAFGPQNFG-VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRV 154
|
170 180
....*....|....*....|...
gi 1180383029 165 LLAQALFANPDILLLDEPTNNLD 187
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
336-513 |
3.34e-09 |
|
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: 57.03 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 336 SGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYcPQDST-----------KDFD--NDLTLF 402
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRAIpylrrkigvvfQDFRllPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 403 DWMS---QWRTAKHNDLMVR-GMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALN 478
Cdd:cd03292 97 ENVAfalEVTGVPPREIRKRvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1180383029 479 NALKDF--AGTLIFVS-HDREFVSSLATRIIDIKDKQV 513
Cdd:cd03292 177 NLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-466 |
4.16e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 56.67 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLgHGFDGET--LFsGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW-SENAT-----------FG 385
Cdd:cd03224 1 LEVENL-NAGYGKSqiLF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 386 YCPQDStkdfdndlTLFDWMsqwrTAKHNDLMVRGMLGRLLFTADD-------------SNKKARNCSGGEKNRLLFGKL 452
Cdd:cd03224 79 YVPEGR--------RIFPEL----TVEENLLLGAYARRRAKRKARLervyelfprlkerRKQLAGTLSGGEQQMLAIARA 146
|
170
....*....|....
gi 1180383029 453 MMQDVNVLVMDEPT 466
Cdd:cd03224 147 LMSRPKLLLLDEPS 160
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-513 |
4.18e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkwsenaTFGYCP----QDSTKDF 395
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPlaeaREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 396 DNDLTLFDWMS-----------QWRTAKHNDLMVRGMlgrllftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDE 464
Cdd:PRK11247 87 FQDARLLPWKKvidnvglglkgQWRDAALQALAAVGL-------ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 465 PTNHMD-------MEAIEALnnaLKDFAGTLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:PRK11247 160 PLGALDaltriemQDLIESL---WQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-187 |
4.19e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.31 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQ----FAFEQYSV 81
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHVPPYQrpinMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgdvelwkvkqerdriysLPEMSEED----GMKVADLESvfAEMdgytaESRAEEILLEAGIdKEFHYGLMANVA 157
Cdd:PRK11607 103 -----------------------FPHMTVEQniafGLKQDKLPK--AEI-----ASRVNEMLGLVHM-QEFAKRKPHQLS 151
|
170 180 190
....*....|....*....|....*....|
gi 1180383029 158 PGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
4.20e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.17 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS----QDQFAFE 77
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-GTDVSRLHardrKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 78 QY------SVVDAVIMGdvelWKVKQERDRiyslPEMSEEDgMKVADLesvfAEMdgytaesraeeILLEagidkefHyg 151
Cdd:PRK10851 82 HYalfrhmTVFDNIAFG----LTVLPRRER----PNAAAIK-AKVTQL----LEM-----------VQLA-------H-- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 152 lMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTIT----WLANELNKRKCTMIIISHDR 212
Cdd:PRK10851 129 -LADRYPaqlsgGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-210 |
4.38e-09 |
|
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: 56.85 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TPGL---------KVGNLSQDQFAFEQySVV 82
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgIDIRdisrkslrsMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 83 DAVIMGD--------VELWKVKQERDRIYSLPemseedgmkvadlesvfaemDGYtaesraEEILLEAGidkefhyglmA 154
Cdd:cd03254 95 ENIRLGRpnatdeevIEAAKEAGAHDFIMKLP--------------------NGY------DTVLGENG----------G 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKcTMIIISH 210
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEaleKLMKGR-TSIIIAH 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-256 |
4.93e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.81 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TPglkvgnLSQDQfafeq 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgEP------LDPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 79 ysvvdavimgdvelwkvkqeRDRI-YsLPemsEEDG----MKVADLESVFAEMDGYT---AESRAEEiLLEAgidkefhY 150
Cdd:COG4152 70 --------------------RRRIgY-LP---EERGlypkMKVGEQLVYLARLKGLSkaeAKRRADE-WLER-------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 151 GLmanvaPGW------KL------RVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRKCTMIIIS-HDrhfL 215
Cdd:COG4152 118 GL-----GDRankkveELskgnqqKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRelAAKGTTVIFSsHQ---M 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1180383029 216 NSV---CTHMADIDYGELRIYpGNYEKFLEAAGLQREQLLAENA 256
Cdd:COG4152 190 ELVeelCDRIVIINKGRKVLS-GSVDEIRRQFGRNTLRLEADGD 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-505 |
5.51e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQfafeqys 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-GNPCARLTPAK------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 vvdAVIMGdveLWKVKQERdriYSLPEMSEEDGMkvadlesVFAEMDGYTAESRAEEILLEAG--IDKEFHYGLMaNVAP 158
Cdd:PRK15439 83 ---AHQLG---IYLVPQEP---LLFPNLSVKENI-------LFGLPKRQASMQKMKQLLAALGcqLDLDSSAGSL-EVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 GWKLRVLlaQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISHdrhflnsvcthmadidygelriypg 235
Cdd:PRK15439 146 RQIVEIL--RGLMRDSRILILDEPTASLTPAETERLfsrIRELLAQGVGIVFISH------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 236 nyekfleaaglqreqllaenakKSAEIDELQDFVN--RFGANAskakqassRAKKMDKIKLDEV-KASSRMSPSLSFDEG 312
Cdd:PRK15439 199 ----------------------KLPEIRQLADRISvmRDGTIA--------LSGKTADLSTDDIiQAITPAAREKSLSAS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 313 KKMY--------RQA-----LEVNKL-GHGfdgetlFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkW 378
Cdd:PRK15439 249 QKLWlelpgnrrQQAagapvLTVEDLtGEG------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-M 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 379 SENATFG-------------YCPQD---STKDFDNDLT------LFDWMSQW-RTAKHNDLMVR--GMLGrLLFTadDSN 433
Cdd:PRK15439 322 LNGKEINalstaqrlarglvYLPEDrqsSGLYLDAPLAwnvcalTHNRRGFWiKPARENAVLERyrRALN-IKFN--HAE 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 434 KKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRI 505
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRV 473
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
315-473 |
5.83e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.51 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTK- 393
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 394 ----DFDN---DLTLFDWMSQW-RTAKHNDLMVRGMLGRLLFTADDSNK---KARNCSGGEKNRLLFGKLMMQDVNVLVM 462
Cdd:PRK13537 83 gvvpQFDNldpDFTVRENLLVFgRYFGLSAAAARALVPPLLEFAKLENKadaKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170
....*....|.
gi 1180383029 463 DEPTNHMDMEA 473
Cdd:PRK13537 163 DEPTTGLDPQA 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
6.09e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAeplF---ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPG----LK 65
Cdd:COG3845 5 ALELRGITKRFGG---VvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvrirSPRdaiaLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 66 VGNLSQDqFA-FEQYSVVDAVIMGDVELWKV----KQERDRIyslPEMSEEDGM------KVADLeSVfaemdgytaesr 134
Cdd:COG3845 82 IGMVHQH-FMlVPNLTVAENIVLGLEPTKGGrldrKAARARI---RELSERYGLdvdpdaKVEDL-SV------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 135 aeeilleagidkefhyglmanvapGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANElnkrKCTMII 207
Cdd:COG3845 145 ------------------------GEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRLAAE----GKSIIF 196
|
...
gi 1180383029 208 ISH 210
Cdd:COG3845 197 ITH 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
324-492 |
6.84e-09 |
|
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: 55.73 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 324 KLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSN---EGEIKWS--ENATFG--------YCPQD 390
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNgiPYKEFAekypgeiiYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 391 STKdfDNDLTLFDWMSQWRTAKHNDlMVRGMlgrllftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:cd03233 92 DVH--FPTLTVRETLDFALRCKGNE-FVRGI------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|....*.
gi 1180383029 471 -MEAIEALnNALKDFA---GTLIFVS 492
Cdd:cd03233 151 sSTALEIL-KCIRTMAdvlKTTTFVS 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
320-514 |
7.85e-09 |
|
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: 57.91 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLR--CLVNELKSNEGEIKWSENATFGYCPQDSTKD--- 394
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKASNIRDTERAgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 -FDNDLTLFDWMSQWRTA------------KHNDLMVR---GMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:TIGR02633 82 iIHQELTLVPELSVAENIflgneitlpggrMAYNAMYLrakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 459 VLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-211 |
8.97e-09 |
|
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: 56.15 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGA-EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-------TPGL----KVGNL 69
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedireQDPVelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 70 SQDQFAFEQYSVVDAV-IMGDVELWKVKQERDRIYSLpemseedgMKVADLESV-FAemDGYTAEsraeeilleagidke 147
Cdd:cd03295 81 IQQIGLFPHMTVEENIaLVPKLLKWPKEKIRERADEL--------LALVGLDPAeFA--DRYPHE--------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 148 fhyglmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT-------ITWLANELNKrkcTMIIISHD 211
Cdd:cd03295 136 --------LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITrdqlqeeFKRLQQELGK---TIVFVTHD 195
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-232 |
1.36e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.81 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSgALVPSAGNVSITPGLKVGNlsqdQFAFEQysv 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFN----QNIYER--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgDVELWKVKQERDRIYSLPE---MSEED----GMKVADLESVFaEMDGyTAESRAEEILLEAGIDKEFHYGLMa 154
Cdd:PRK14258 80 -------RVNLNRLRRQVSMVHPKPNlfpMSVYDnvayGVKIVGWRPKL-EIDD-IVESALKDADLWDEIKHKIHKSAL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN 229
|
..
gi 1180383029 231 RI 232
Cdd:PRK14258 230 RI 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
320-481 |
1.44e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI-------KWSENATF----GYCP 388
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRFmaylGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 389 QdstkdFDNDLTLFDWMS-----QWRTAKH---NDLMVRGMlgrllftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVL 460
Cdd:PRK13543 92 G-----LKADLSTLENLHflcglHGRRAKQmpgSALAIVGL-------AGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170 180
....*....|....*....|.
gi 1180383029 461 VMDEPTNHMDMEAIEALNNAL 481
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMI 180
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-188 |
1.72e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlSQDQFAFEQYSvvdavimgdvelwkVKQ 97
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---------DDHPLHFGDYS--------------YRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 98 ERDR-IYSLPEMSEEDGMKVADLESV----FAEMDGYTAESRAEEILLEAGI--DKEFHYGLManVAPGWKLRVLLAQAL 170
Cdd:PRK15112 87 QRIRmIFQDPSTSLNPRQRISQILDFplrlNTDLEPEQREKQIIETLRQVGLlpDHASYYPHM--LAPGQKQRLGLARAL 164
|
170
....*....|....*...
gi 1180383029 171 FANPDILLLDEPTNNLDI 188
Cdd:PRK15112 165 ILRPKVIIADEALASLDM 182
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
1.75e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.80 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVP---SAGNV-----SITPG----LKVGN 68
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVllngrRLTALpaeqRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 69 LSQDQFAFEQYSVVDAVIMGDVELWKVKQERDRIyslpemseedgmkvadlesvfaemdgytaesraEEILLEAGIDKef 148
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIGRAQRRARV---------------------------------EQALEEAGLAG-- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 149 hyglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHD 211
Cdd:COG4136 126 ----FADRDPatlsgGQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
315-526 |
2.83e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.98 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATfgycpqDSTKD 394
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI------NLVRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 FDNDLTLFD--------------------W--MSQWRTAKHNDLMVRGM------------LGRLLFTADDSNKKARNCS 440
Cdd:PRK10619 75 KDGQLKVADknqlrllrtrltmvfqhfnlWshMTVLENVMEAPIQVLGLskqeareravkyLAKVGIDERAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 441 GGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAI-EALN--NALKDFAGTLIFVSHDREFVSSLATRIIDIKdKQVIDFQ 517
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIEEE 233
|
....*....
gi 1180383029 518 GTFDEYLAS 526
Cdd:PRK10619 234 GAPEQLFGN 242
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
2.95e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 55.47 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 17 FENISAKFGNGNR-----------------YGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDqfafeqy 79
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD-GVDLTALSER------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svvdavimgdvELWKVKQerdRIyslpemseedGM-----------KVAD-----LEsvFAEMDGYTAESRAEEIL---- 139
Cdd:COG1135 76 -----------ELRAARR---KI----------GMifqhfnllssrTVAEnvalpLE--IAGVPKAEIRKRVAELLelvg 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 140 LEagiDKEFHYglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFL 215
Cdd:COG1135 130 LS---DKADAY--PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsILDLLKDINRElGLTIVLITHEMDVV 204
|
250
....*....|....*
gi 1180383029 216 NSVCTHMADIDYGEL 230
Cdd:COG1135 205 RRICDRVAVLENGRI 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
317-526 |
3.19e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 56.33 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 317 RQALEVNKLGHGFDGET-LFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW-----------SENATF 384
Cdd:COG1132 337 RGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltleSLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 385 GYCPQDSTkdfdndltLFDwmsqwRTAKHNdlmVRgmLGRLlfTADDSN-----KKAR---------------------N 438
Cdd:COG1132 417 GVVPQDTF--------LFS-----GTIREN---IR--YGRP--DATDEEveeaaKAAQahefiealpdgydtvvgergvN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 439 CSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME---AI-EALNNALKDfaGTLIFVSHdRefVSSL--ATRIIDIKDKQ 512
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTEteaLIqEALERLMKG--RTTIVIAH-R--LSTIrnADRILVLDDGR 551
|
250
....*....|....
gi 1180383029 513 VIDfQGTFDEYLAS 526
Cdd:COG1132 552 IVE-QGTHEELLAR 564
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
3.57e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQF-GAEPLFE---NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQFAf 76
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDGQDLTALSEKELR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 77 eqysvvdavimgdvelwkvkQERDRIyslpemseedGM-----------KVADLESVFAEMDGYTA---ESRAEEILLEA 142
Cdd:PRK11153 79 --------------------KARRQI----------GMifqhfnllssrTVFDNVALPLELAGTPKaeiKARVTELLELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 143 GI-DKEFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLNS 217
Cdd:PRK11153 129 GLsDKADRYP--AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsILELLKDINRElGLTIVLITHEMDVVKR 206
|
250
....*....|...
gi 1180383029 218 VCTHMADIDYGEL 230
Cdd:PRK11153 207 ICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
3.70e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.64 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQF--GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpglkvgnlsqdqfafeqy 79
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT-------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svVDAVIMGDVELWKVKQERDRIYSLPEmSEEDGMKVADlESVFA-EMDGYTAES---RAEEILLEAGIdKEFHYGLMAN 155
Cdd:PRK13635 66 --VGGMVLSEETVWDVRRQVGMVFQNPD-NQFVGATVQD-DVAFGlENIGVPREEmveRVDQALRQVGM-EDFLNREPHR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNkrkCTMIIISHD 211
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKG---ITVLSITHD 200
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
4.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQF--GAEPLfENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPGL-----K 65
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikydKKSLlevrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 66 VGNLSQ---DQ-FAfeqYSVVDAVIMGDVELwkvkqerdriySLPEmsEEDGMKVAD-LESVfaEMDGYTaesraeeill 140
Cdd:PRK13639 80 VGIVFQnpdDQlFA---PTVEEDVAFGPLNL-----------GLSK--EEVEKRVKEaLKAV--GMEGFE---------- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 141 eagiDKEFHYglmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHD 211
Cdd:PRK13639 132 ----NKPPHH-----LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
4.34e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.46 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKI------------------LSGALVPSAGNVSITPG 63
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 64 LKVGNLSQDQFAFEQYSVVDAVIMGdVELWKVKQERDRiysLPEMSEEDGMKVADLESVFAEMDGYTAesraeeilleag 143
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKE---LDERVEWALKKAALWDEVKDRLNDYPS------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 144 idkefhyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELnKRKCTMIIISHDRHFLNSVCT 220
Cdd:PRK14267 149 -----------NLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSD 216
|
250 260
....*....|....*....|..
gi 1180383029 221 HMADIDYGELrIYPGNYEKFLE 242
Cdd:PRK14267 217 YVAFLYLGKL-IEVGPTRKVFE 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
5.16e-08 |
|
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: 53.78 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeqysV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI----------------------L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 VDAVIMGDVELWK-----VKQErdriYSL-PEMSEED----GMKVAdlesvfaEMDGYTAESRAEEILLEAGIDkEFHYG 151
Cdd:cd03300 59 LDGKDITNLPPHKrpvntVFQN----YALfPHLTVFEniafGLRLK-------KLPKAEIKERVAEALDLVQLE-GYANR 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 152 LMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELnKR-----KCTMIIISHD 211
Cdd:cd03300 127 KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL-KRlqkelGITFVFVTHD 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-241 |
5.93e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.61 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLfeNISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPGL-KVGNLSQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalPPAErPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 72 DQFAFEQYSVVDAVIMGdvelwkvkqerdriyslpeMSeeDGMKvadlesvfaemdgYTAESRA--EEILLEAGIdkefh 149
Cdd:COG3840 79 ENNLFPHLTVAQNIGLG-------------------LR--PGLK-------------LTAEQRAqvEQALERVGL----- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 150 YGLM----ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNK-RKCTMIIISHD----RHFlns 217
Cdd:COG3840 120 AGLLdrlpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrQEMLDLVDELCReRGLTVLMVTHDpedaARI--- 196
|
250 260
....*....|....*....|....
gi 1180383029 218 vCTHMADIDYGELrIYPGNYEKFL 241
Cdd:COG3840 197 -ADRVLLVADGRI-AADGPTAALL 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
6.49e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 20 ISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQfafeqysvvdavIMGDVELwkVKQE- 98
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVNAENEKW------------VRSKVGL--VFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYSlpEMSEEDgmkVAdLESVFAEMDGYTAESRAEEILLEAGIdKEFHYGLMANVAPGWKLRVLLAQALFANPDILL 178
Cdd:PRK13647 89 DDQVFS--STVWDD---VA-FGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1180383029 179 LDEPTNNLD---IHTITWLANELNKRKCTMIIISHD 211
Cdd:PRK13647 162 LDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-210 |
7.06e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 53.32 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITP-------GLKVGNL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqDITKlpmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 70 SQDQFAFEQYSVVDAvIMGDVELWKV-KQERdriyslpemseedgmkvadlesvfaemdgytaESRAEEILLEAGIDKef 148
Cdd:cd03218 81 PQEASIFRKLTVEEN-ILAVLEIRGLsKKER--------------------------------EEKLEELLEEFHITH-- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 149 hygLMANVAP----GWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISH 210
Cdd:cd03218 126 ---LRKSKASslsgGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDH 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-502 |
7.47e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.89 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLvNELKSNEGEIKWSENATF-------------- 384
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFfnqniyerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 385 ------------GYCPQDSTKDFDNDLTLFDWmsqwrtakHNDLMVRGMLGRLLFTAD-------DSNKKARNCSGGEKN 445
Cdd:PRK14258 86 lrrqvsmvhpkpNLFPMSVYDNVAYGVKIVGW--------RPKLEIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 446 RLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEALNNALKDFAG-TLIFVSHDREFVSSLA 502
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSElTMVIVSHNLHQVSRLS 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-237 |
7.51e-08 |
|
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: 53.52 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITPG----LKVGNLSQDQFAFE-------------QYsvVD---AVIMGDV 90
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdeiLDEFRGSELQNYFTkllegdvkvivkpQY--VDlipKAVKGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 -ELWKVKQERDRIyslpemseEDGMKVADLESVfaemdgytaesraeeilLEAGIDkefhyglmaNVAPGWKLRVLLAQA 169
Cdd:cd03236 108 gELLKKKDERGKL--------DELVDQLELRHV-----------------LDRNID---------QLSGGELQRVAIAAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 170 LFANPDILLLDEPTNNLDIH---TITWLANELNKRKCTMIIISHDRhflnSVCTHMAD---IDYGElriyPGNY 237
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDL----AVLDYLSDyihCLYGE----PGAY 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-210 |
8.66e-08 |
|
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: 52.88 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 7 ITMQFGAEPLfeNISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT--------PGLK-VGNLSQDQFAFE 77
Cdd:cd03298 6 IRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaapPADRpVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 78 QYSVVDAVIMGdvelwkvkqerdRIYSLpEMSEEDGMKVadlesvfaemdgytaesraEEILLEAGIDkEFHYGLMANVA 157
Cdd:cd03298 84 HLTVEQNVGLG------------LSPGL-KLTAEDRQAI-------------------EVALARVGLA-GLEKRLPGELS 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNK-RKCTMIIISH 210
Cdd:cd03298 131 GGERQRVALARVLVRDKPVLLLDEPFAALDPalrAEMLDLVLDLHAeTKMTVLMVTH 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
329-513 |
9.28e-08 |
|
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: 52.64 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 329 FDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDstKD----FDNdLTLFDW 404
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDiamvFQN-YALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 405 MSQWRTAKHNdLMVRGM-----------LGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD--- 470
Cdd:cd03301 87 MTVYDNIAFG-LKLRKVpkdeidervreVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDakl 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1180383029 471 -MEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:cd03301 166 rVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
319-514 |
9.34e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGF-DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFL------------RCLVNELKSNEGEIKWSENATfG 385
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgRVKVMGREVNAENEKWVRSKV-G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 386 YCPQD------STKDFDnDLTlFDWMSQWRTAKHNDLMVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:PRK13647 83 LVFQDpddqvfSSTVWD-DVA-FGPVNMGLDKDEVERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 460 LVMDEPTNHMD-------MEAIEALNNALKdfagTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK13647 160 IVLDEPMAYLDprgqetlMEILDRLHNQGK----TVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-187 |
9.85e-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: 52.50 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 4 TANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGlkvgnlsqdqfafeqysvvd 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 84 avimgdvelwKVKQERDRIY-SLPEMSEEDGMK--VADLESV-FAEMDGytAESRAEEILLEAGIdKEFHYGLMANVAPG 159
Cdd:cd03231 63 ----------PLDFQRDSIArGLLYLGHAPGIKttLSVLENLrFWHADH--SDEQVEEALARVGL-NGFEDRPVAQLSAG 129
|
170 180
....*....|....*....|....*...
gi 1180383029 160 WKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-506 |
1.09e-07 |
|
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: 52.47 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGE----TLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI------KWSENATFGYCPQ 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 DSTkdfdndltLFdwmsQWRTAKHN---DLMVRGMLGRllftadDSNKKARNC-----------------SGGEKNRLLF 449
Cdd:cd03293 81 QDA--------LL----PWLTVLDNvalGLELQGVPKA------EARERAEELlelvglsgfenayphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 450 GKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG----TLIFVSHDREFVSSLATRII 506
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetgkTVLLVTHDIDEAVFLADRVV 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-210 |
1.16e-07 |
|
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: 52.93 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS----QDQFAFeqysvvdavimgdv 90
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLNlrwlRSQIGL-------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 elwkVKQE--------RDRI-YSLPEMSEEDgmkvadlesvfaemdgytaesrAEEILLEAGIDK---EFHYGLMANVAP 158
Cdd:cd03249 82 ----VSQEpvlfdgtiAENIrYGKPDATDEE----------------------VEEAAKKANIHDfimSLPDGYDTLVGE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 159 -------GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKC--TMIIISH 210
Cdd:cd03249 136 rgsqlsgGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
320-522 |
1.22e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGET-LFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK------WSEN-----ATFGYC 387
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepiTKENirevrKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQDS-------TKDFDNDLTLFDWMSQWRTAKHNDLMVRGMLGrllfTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVL 460
Cdd:PRK13652 84 FQNPddqifspTVEQDIAFGPINLGLDEETVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 461 VMDEPTNHMD----MEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIdIKDKQVIDFQGTFDE 522
Cdd:PRK13652 160 VLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIY-VMDKGRIVAYGTVEE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
343-470 |
1.23e-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: 52.66 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 343 EAGAKLAVIGENGVGKTTFLR---CLVNELKSNEGEI----------KWSENatFGYCPQDSTkdFDNDLTLFD---WMS 406
Cdd:cd03234 31 ESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQIlfngqprkpdQFQKC--VAYVRQDDI--LLPGLTVREtltYTA 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 407 QWRTAKHNDLMVRGML---GRLLFTADDS--NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:cd03234 107 ILRLPRKSSDAIRKKRvedVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-211 |
1.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.27 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVP-SAGNVSITpglkvgnlsqdqfafeqysvVDAVIMGDVEL 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPdDNPNSKIT--------------------VDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 93 WKVKQERDRIYSLPEmSEEDGMKVAD-----LES---VFAEMDGYTAESRAEEILLEAgIDKEfhyglMANVAPGWKLRV 164
Cdd:PRK13640 80 WDIREKVGIVFQNPD-NQFVGATVGDdvafgLENravPRPEMIKIVRDVLADVGMLDY-IDSE-----PANLSGGQKQRV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 165 LLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRK-CTMIIISHD 211
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPagkEQILKLIRKLKKKNnLTVISITHD 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-230 |
1.27e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-------SITP-----GLKVGNLSQDQ 73
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddediSLLPlharaRRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 FAFEQYSVVDavimgdvELWKVKQERDriyslpEMSEEDgmkvadlesvfaemdgytAESRAEEILleagidKEFHYGLM 153
Cdd:PRK10895 88 SIFRRLSVYD-------NLMAVLQIRD------DLSAEQ------------------REDRANELM------EEFHIEHL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 154 AN-----VAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADI 225
Cdd:PRK10895 131 RDsmgqsLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIV 210
|
....*
gi 1180383029 226 DYGEL 230
Cdd:PRK10895 211 SQGHL 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
339-510 |
1.43e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 52.09 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWseNATFGYCPQ------DSTKD-------FDN-------- 397
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQepwiqnGTIREnilfgkpFDEeryekvik 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 398 ------DLTLFDwmsqwrtakHNDLMV---RGMlgrllftaddsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEP--- 465
Cdd:cd03250 103 acalepDLEILP---------DGDLTEigeKGI----------------NLSGGQKQRISLARAVYSDADIYLLDDPlsa 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1180383029 466 ----TNHMDMEaiEALNNALKDFAgTLIFVSHDREFVSSlATRIIDIKD 510
Cdd:cd03250 158 vdahVGRHIFE--NCILGLLLNNK-TRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-493 |
1.43e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 51.78 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 348 LAVIGENGVGKTTFLRCLVNELKSN--EGEI--------KWSENATFGYCPQDstkdfdnDLTlfdwmsqwrtakHNDLM 417
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLgvSGEVlingrpldKRSFRKIIGYVPQD-------DIL------------HPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 418 VRGMLgrlLFTAddsnkKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDmeAIEALN--NALKDFAG---TLIFVS 492
Cdd:cd03213 99 VRETL---MFAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD--SSSALQvmSLLRRLADtgrTIICSI 168
|
.
gi 1180383029 493 H 493
Cdd:cd03213 169 H 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
1.58e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 53.98 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFG-AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGL-----------KVGNL 69
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 70 SQDQFAFEQySVVDAVIMGdvelwkvkqerdriySLPEMSEEDGMKVADLesvfaemdgytAESRAEEILLEAGIDKEFH 149
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLG---------------AKENVSQDEIWAACEI-----------AEIKDDIENMPLGYQTELS 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 150 YGlMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDihTIT---WLANELNKRKCTMIIISH 210
Cdd:TIGR01193 607 EE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD--TITekkIVNNLLNLQDKTIIFVAH 667
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-235 |
1.68e-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: 52.27 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 16 LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVS---------ITPGLkvgnlSQDQFAFeqysvvdavi 86
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilfngqpRKPDQ-----FQKCVAY---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 87 mgdvelwkVKQErDRIysLPEMSEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLL 166
Cdd:cd03234 86 --------VRQD-DIL--LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 167 AQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHD-RHFLNSVCTHMADIDYGELrIYPG 235
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTalnLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
349-514 |
1.71e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 349 AVIGENGVGKTTFLRCLVNELKSNEGEIkWSENAT------------FGYCPQDSTKdfDNDLTLFDWMS---------- 406
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHiqhyaskevarrIGLLAQNATT--PGDITVQELVArgryphqplf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 407 -QWRTaKHNDLMVRGMlgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNAL 481
Cdd:PRK10253 114 tRWRK-EDEEAVTKAM--QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELN 190
|
170 180 190
....*....|....*....|....*....|...
gi 1180383029 482 KDFAGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK10253 191 REKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-215 |
1.80e-07 |
|
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: 51.95 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEQYSVvdAVIMGDVELWK 94
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV--AYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 95 VKQERDRIYSLPeMSEEDGMKVADLESVFAEMDGYTAESRAEeiLLEAGIdkefhyglmaNVAPGWKLRVLLAQALFANP 174
Cdd:cd03290 93 ATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTE--IGERGI----------NLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 175 DILLLDEPTNNLDIHTITWLANE-----LNKRKCTMIIISHDRHFL 215
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-513 |
1.83e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGalvpsagnvsITP-GLKVGNLSQDQFAFEQYSVVDA 84
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG----------VYPhGTWDGEIYWSGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 85 VIMGDVelwKVKQErdrIYSLPEMSEedgmkvadLESVF---------AEMDGYTAESRAEEILLEAGIDKEFHYGLMAN 155
Cdd:TIGR02633 76 ERAGIV---IIHQE---LTLVPELSV--------AENIFlgneitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGElri 232
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDiirDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 233 ypgnYEKFLEAAGLQREQLLAENAKKS------AEIDELQDFVNRfGANASKAKQASSRAKKMDKIKldevkassrmsps 306
Cdd:TIGR02633 219 ----HVATKDMSTMSEDDIITMMVGREitslypHEPHEIGDVILE-ARNLTCWDVINPHRKRVDDVS------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 307 lsfdegkkmyrqalevnklghgfdgetlfsggdFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSN-EGEI--------- 376
Cdd:TIGR02633 281 ---------------------------------FSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVfingkpvdi 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 377 ---KWSENATFGYCPQDSTKD-------FDNDLTL-----FDWMSQWRTAKHNDLMVRGMlGRLLFTADDSNKKARNCSG 441
Cdd:TIGR02633 328 rnpAQAIRAGIAMVPEDRKRHgivpilgVGKNITLsvlksFCFKMRIDAAAELQIIGSAI-QRLKVKTASPFLPIGRLSG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 442 GEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-258 |
2.80e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.30 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQF-GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQdqfafeqy 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSK-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svvdavimgdvelwkvkqerdriysLPEMSEEDGMKVADLESVFAemdGYTAES------------------RAEEILLE 141
Cdd:PRK13644 72 -------------------------LQGIRKLVGIVFQNPETQFV---GRTVEEdlafgpenlclppieirkRVDRALAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 142 AGIDKeFHYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT-ITWLAN--ELNKRKCTMIIISHDRHFLnsv 218
Cdd:PRK13644 124 IGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERikKLHEKGKTIVYITHNLEEL--- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 219 ctHMAD----IDYGELRIyPGNYEKFLEAAGLQREQL-------LAENAKK 258
Cdd:PRK13644 200 --HDADriivMDRGKIVL-EGEPENVLSDVSLQTLGLtppslieLAENLKM 247
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-226 |
2.86e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.23 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSA-GNVSITpglkvgnlsqdqfafeqysvvdavimgdvelw 93
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRIGMP-------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 94 kvkqERDRIYSLPEMSeedgmkvadlesvfaemdgYTAESRAEEILLeagidkefhYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:cd03223 62 ----EGEDLLFLPQRP-------------------YLPLGTLREQLI---------YPWDDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 174 PDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHdRHFLNSVCTHMADID 226
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
337-515 |
3.01e-07 |
|
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: 51.21 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 337 GGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGeikwseNATF-GYcpqDSTKD----------FDNDLTLFDWM 405
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVdGF---DVVKEpaearrrlgfVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 406 SQWRT----AKHNDLMVRGMLGRL------LFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIE 475
Cdd:cd03266 94 TARENleyfAGLYGLKGDELTARLeeladrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 476 ALNN---ALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:cd03266 174 ALREfirQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
3.46e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQF-GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvGNLSQDQFAFEQY 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-----GEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 SVVDAVImgdvelwkvKQERDRIYSlPEMSEEDGMKVADLesvfaEMDGYTAESRAEEILLEAGIDkEFHYGLMANVAPG 159
Cdd:PRK13652 78 KFVGLVF---------QNPDDQIFS-PTVEQDIAFGPINL-----GLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 160 WKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGELRIYPG 235
Cdd:PRK13652 142 EKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
250
....*....|....*.
gi 1180383029 236 NYEKFLEAAGLQREQL 251
Cdd:PRK13652 222 VEEIFLQPDLLARVHL 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
132-219 |
3.66e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 132 ESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMII 207
Cdd:PRK15134 402 EQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLF 481
|
90
....*....|..
gi 1180383029 208 ISHDRHFLNSVC 219
Cdd:PRK15134 482 ISHDLHVVRALC 493
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
330-495 |
3.85e-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: 52.99 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 330 DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVnELKSNEGEI-------------KWSEnaTFGYCPQDS---TK 393
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIqidgvswnsvtlqTWRK--AFGVIPQKVfifSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 394 DFDNDLTLFD-WMSQ--WRTAKHNDL--MVRGMLGRLLFTADDSNKKARNcsgGEKNRLLFGKLMMQDVNVLVMDEPTNH 468
Cdd:TIGR01271 1307 TFRKNLDPYEqWSDEeiWKVAEEVGLksVIEQFPDKLDFVLVDGGYVLSN---GHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180
....*....|....*....|....*...
gi 1180383029 469 MDMEAIEALNNALKD-FAGTLIFVSHDR 495
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
4.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.63 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAE------PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqf 74
Cdd:PRK13633 4 MIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 75 afeqysVVDAVIMGDVE-LWKVKQERDRIYSLPE------MSEEDgmkVAdlesvFA-EMDGYTAE---SRAEEILLEAG 143
Cdd:PRK13633 68 ------YVDGLDTSDEEnLWDIRNKAGMVFQNPDnqivatIVEED---VA-----FGpENLGIPPEeirERVDESLKKVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 144 IDKEFHYglmanvAP-----GWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTItwlaNELNKRK-CTMIIISH 210
Cdd:PRK13633 134 MYEYRRH------APhllsgGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTI----KELNKKYgITIILITH 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
320-528 |
4.63e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGF-DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkwsenaTFGYCPQDSTK----- 393
Cdd:PRK13636 6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI------LFDGKPIDYSRkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 394 ----------DFDNDL--------TLFDWMSQWRTAKHNDLMVRGMLGRLlFTADDSNKKARNCSGGEKNRLLFGKLMMQ 455
Cdd:PRK13636 80 lresvgmvfqDPDNQLfsasvyqdVSFGAVNLKLPEDEVRKRVDNALKRT-GIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 456 DVNVLVMDEPTNHMD----MEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDEYLASIE 528
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKE 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-211 |
4.95e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.95 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILsgalvpsAGNVSITPG-LKVGNlsqdqfafeqysvvda 84
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI-------AGLEDITSGdLFIGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 85 VIMGDVELWK-----VKQErdriYSL-PEMSEED----GMKVADLESvfAEMDGYTAEsrAEEIL-LEAGIDKEfhyglM 153
Cdd:PRK11000 65 KRMNDVPPAErgvgmVFQS----YALyPHLSVAEnmsfGLKLAGAKK--EEINQRVNQ--VAEVLqLAHLLDRK-----P 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANE---LNKR-KCTMIIISHD 211
Cdd:PRK11000 132 KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEisrLHKRlGRTMIYVTHD 193
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-233 |
4.95e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 50.49 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAE--PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqy 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svvDAVIMGDVELWKVkqeRDRIYSLPemsEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGidkefhyGLmaNVAPG 159
Cdd:cd03369 68 ---DGIDISTIPLEDL---RSSLTIIP---QDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEG-------GL--NLSQG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDrhfLNSV--CTHMADIDYGELRIY 233
Cdd:cd03369 130 QRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR---LRTIidYDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-211 |
5.03e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.37 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlsqdqfafeQYSVVDAVimGDVELWKVKQ 97
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA----------------GYHITPET--GNKNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 98 ERDRIYSLPEMSEEDGMKVADLEsvFAEMD-GYT---AESRAEEILLEAGIDKEfhyglMANVAP-----GWKLRVLLAQ 168
Cdd:PRK13641 86 KVSLVFQFPEAQLFENTVLKDVE--FGPKNfGFSedeAKEKALKWLKKVGLSED-----LISKSPfelsgGQMRRVAIAG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 169 ALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHD 211
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPegrKEMMQLFKDYQKAGHTVILVTHN 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
315-509 |
5.21e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGF-DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI--------KWSENATFG 385
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 386 YCPQDSTKDFD-----NDLTL---FDWMSQWRTAK-HNDLMVRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQD 456
Cdd:PRK15056 82 YVPQSEEVDWSfpvlvEDVVMmgrYGHMGWLRRAKkRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 457 VNVLVMDEPTNHMDMEA---IEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIK 509
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-376 |
5.36e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.93 E-value: 5.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI 376
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV 59
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-210 |
6.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS-----ITPGLKVGNLSQDQ------FAFEQYSVVDAVIm 87
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervITAGKKNKKLKPLRkkvgivFQFPEHQLFEETV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 88 gdvelwkvkqERDrIYSLPE---MSEEDgmkvadlesvfaemdgytAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRV 164
Cdd:PRK13634 104 ----------EKD-ICFGPMnfgVSEED------------------AKQKAREMIELVGLPEELLARSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 165 LLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRK-CTMIIISH 210
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPkgrKEMMEMFYKLHKEKgLTTVLVTH 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-210 |
7.60e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 50.16 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGlKVGNLSQDQFAFEQYSVV--DAVIMGdvel 92
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDG-KPISQYEHKYLHSKVSLVgqEPVLFA---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 93 wkvKQERDRI-YSLPEMSeedgmkvadLESVFAEMDGYTAESRAEEilLEAGIDKEF-HYGlmANVAPGWKLRVLLAQAL 170
Cdd:cd03248 102 ---RSLQDNIaYGLQSCS---------FECVKEAAQKAHAHSFISE--LASGYDTEVgEKG--SQLSGGQKQRVAIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 171 FANPDILLLDEPTNNLDI---HTITWLANELNKRKcTMIIISH 210
Cdd:cd03248 166 IRNPQVLILDEATSALDAeseQQVQQALYDWPERR-TVLVIAH 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
320-378 |
1.04e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 1.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW 378
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW 60
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-224 |
1.16e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnLSQDQFAfeqysvvdaviMGDVELWKVKQERDRIYSLP 106
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAW--------LGKDLLG-----------MKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 107 EMSEEDGMKVAD-----LESVFAEMDGYTAESRAEEILLEAgidkefhyGLMANV--------APGWKLRVLLAQALFAN 173
Cdd:PRK15079 108 LASLNPRMTIGEiiaepLRTYHPKLSRQEVKDRVKAMMLKV--------GLLPNLinryphefSGGQCQRIGIARALILE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 174 PDILLLDEPTNNLDIHTITWLANELNKRKCTM----IIISHDRhflnSVCTHMAD 224
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMglslIFIAHDL----AVVKHISD 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
315-505 |
1.24e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.99 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQD---- 390
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 391 -STKDFDNdLTLFDWMsqwrTAKHNdLMV-------RGMLGRLLFTA-----------------------DDSNKKARNC 439
Cdd:PRK11300 81 gVVRTFQH-VRLFREM----TVIEN-LLVaqhqqlkTGLFSGLLKTPafrraesealdraatwlervgllEHANRQAGNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPT---NHMDMEAIEALNNALKD-FAGTLIFVSHDREFVSSLATRI 505
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRI 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-224 |
1.34e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 20 ISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVSItpglkvgnlsqDQFAFEQYSVVDavimgdvelwkvkQER 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILL-----------NGRPLSDWSAAE-------------LAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 100 DRIYsLPEMSEedgmkvadleSVFAeMDGYtaesraeEIL---LEAGIDKEFHYGLMANVAPGWKL-------------- 162
Cdd:COG4138 70 HRAY-LSQQQS----------PPFA-MPVF-------QYLalhQPAGASSEAVEQLLAQLAEALGLedklsrpltqlsgg 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 163 ---RVLLAQALF-----ANPD--ILLLDEPTNNLDIH----TITWLaNELNKRKCTMIIISHDrhfLNSVCTHmAD 224
Cdd:COG4138 131 ewqRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAqqaaLDRLL-RELCQQGITVVMSSHD---LNHTLRH-AD 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
1.37e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.91 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG--ALVPSA---GNVSITpglkvgnlSQDQFAf 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLD--------GQDIFK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 77 eqysvvdaviMGDVELWKVKQERDRIYS-LPEMSEED----GMKVADLESVFAEMdgytaESRAEEILLEAGIDKEFHYG 151
Cdd:PRK14247 75 ----------MDVIELRRRVQMVFQIPNpIPNLSIFEnvalGLKLNRLVKSKKEL-----QERVRWALEKAQLWDEVKDR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 152 LMA---NVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELnKRKCTMIIISH 210
Cdd:PRK14247 140 LDApagKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpenTAKIESLFLEL-KKDMTIVLVTH 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-212 |
1.39e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 32 LIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAFEQYSVvdAVIMGDVELWKVKQERDRIySLPemsee 111
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFS-GHDITRLKNREVPFLRRQI--GMIFQDHHLLMDRTVYDNV-AIP----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 112 dgmkvadleSVFAEMDGYTAESRAEEILLEAGI-DKEFHYGLmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD--- 187
Cdd:PRK10908 104 ---------LIIAGASGDDIRRRVSAALDKVGLlDKAKNFPI--QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdal 172
|
170 180
....*....|....*....|....*
gi 1180383029 188 IHTITWLANELNKRKCTMIIISHDR 212
Cdd:PRK10908 173 SEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-275 |
1.50e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.23 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGnlsqDQFAFEQYSVVDAvimgDVELWKVKQ 97
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-DIYIG----DKKNNHELITNPY----SKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 98 ERDRI---YSLPEMS------EEDGMkvadLESVFAEMDGYTAESRAEEILLEAGIDKEF----HYGLmanvAPGWKLRV 164
Cdd:PRK13631 114 LRRRVsmvFQFPEYQlfkdtiEKDIM----FGPVALGVKKSEAKKLAKFYLNKMGLDDSYlersPFGL----SGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 165 LLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKFL 241
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPkgeHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFT 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 242 EAAGLQR------------EQLLAENAK-------KSAEIDELQDFVNRFGAN 275
Cdd:PRK13631 266 DQHIINStsiqvprviqviNDLIKKDPKykklyqkQPRTIEQLADAINEFIKG 318
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-506 |
1.58e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 345 GAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKwsenatfgycpqdstkdfdndltLFDwMSQWRTAKHNDLMVRGMLGR 424
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------YID-GEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 425 LLFTaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD---------MEAIEALNNALKDFAGTLIFVSHDR 495
Cdd:smart00382 58 KASG-----------SGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDE 126
|
170
....*....|.
gi 1180383029 496 EFVSSLATRII 506
Cdd:smart00382 127 KDLGPALLRRR 137
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
338-506 |
1.75e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 338 GDFLLEA-------GAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWsENATFGYCPQdstkdfdndltlfdwmsqwrt 410
Cdd:cd03222 11 GVFFLLVelgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQ--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 411 akHNDLmvrgmlgrllftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFA----G 486
Cdd:cd03222 69 --YIDL-----------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeegkK 123
|
170 180
....*....|....*....|
gi 1180383029 487 TLIFVSHDREFVSSLATRII 506
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-183 |
1.76e-06 |
|
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: 48.97 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA-------------FEQYSVVDAVIMGDVELWK--V 95
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-GRDITGLPPHERAragigyvpegrriFPELTVEENLLLGAYARRRakR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 96 KQERDRIYSL-PEMSEEDGMKVADLesvfaemdgytaeSRAEEILLEagidkefhyglmanvapgwklrvlLAQALFANP 174
Cdd:cd03224 109 KARLERVYELfPRLKERRKQLAGTL-------------SGGEQQMLA------------------------IARALMSRP 151
|
....*....
gi 1180383029 175 DILLLDEPT 183
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
440-528 |
1.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNAL----KDFAGTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
90
....*....|....*...
gi 1180383029 516 FQGTFD-----EYLASIE 528
Cdd:PRK13645 232 IGSPFEifsnqELLTKIE 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-210 |
1.92e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.66 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGN-----VSITPglKVGNLSQDQ------FAFEQYSVVDAVI 86
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgVDITD--KKVKLSDIRkkvglvFQYPEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 87 MGDVELWKVkqerdriySLPEMSEEDGMKV-ADLESVFAEMDGYTAESRAEeilleagidkefhyglmanVAPGWKLRVL 165
Cdd:PRK13637 102 EKDIAFGPI--------NLGLSEEEIENRVkRAMNIVGLDYEDYKDKSPFE-------------------LSGGQKRRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1180383029 166 LAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISH 210
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHKEyNMTIILVSH 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
2.17e-06 |
|
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: 48.08 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFG--AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeqy 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 svvdavimgdvelwkvkqerdriyslpemseeDGMKVADLEsvfaemdgytaESRAEEIlleAGIDKE---FHYGLMANV 156
Cdd:cd03247 62 --------------------------------DGVPVSDLE-----------KALSSLI---SVLNQRpylFDTTLRNNL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 157 ----APGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISH 210
Cdd:cd03247 96 grrfSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqLLSLIFEVLKDK-TLIWITH 155
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
320-506 |
2.28e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.70 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFD---GETLF----------SGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGY 386
Cdd:PRK15079 9 LEVADLKVHFDikdGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 387 CP--------------QDSTKDFDNDLTLFDWMSQWRTAKHNDL-------MVRGMLGRLLFTADDSNKKARNCSGGEKN 445
Cdd:PRK15079 89 KDdewravrsdiqmifQDPLASLNPRMTIGEIIAEPLRTYHPKLsrqevkdRVKAMMLKVGLLPNLINRYPHEFSGGQCQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 446 RLLFGKLMMQDVNVLVMDEPTNHMDMeAIEA-LNNALKDFAG----TLIFVSHDREFVSSLATRII 506
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDV-SIQAqVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVL 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-189 |
2.89e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 11 FGAEP--LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnLSQDQFAF--EQYSVVDAVI 86
Cdd:PTZ00243 668 FELEPkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------WAERSIAYvpQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 87 mgdvelwkvkqeRDRIYSLPEMSEE---DGMKVADLESVFAEMDGytaesRAEEILLEAGIdkefhyglmaNVAPGWKLR 163
Cdd:PTZ00243 738 ------------RGNILFFDEEDAArlaDAVRVSQLEADLAQLGG-----GLETEIGEKGV----------NLSGGQKAR 790
|
170 180
....*....|....*....|....*.
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLDIH 189
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAH 816
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-218 |
3.82e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 47.91 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGalvpsagnvsitpglkvgnlsqdqfaFEQYSVVDAVIM--GDVELWKV 95
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--------------------------HPKYEVTEGEILfkGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 96 KQERDR--IYSLPEMSEE-DGMKVAD-LESVFAEMDGytaesraeeilleagidkefhyglmanvapGWKLRVLLAQALF 171
Cdd:cd03217 71 PEERARlgIFLAFQYPPEiPGVKNADfLRYVNEGFSG------------------------------GEKKRNEILQLLL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 172 ANPDILLLDEPTNNLDIHTITWLANELNK---RKCTMIIISHDRHFLNSV 218
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKlreEGKSVLIITHYQRLLDYI 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
409-514 |
4.25e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.34 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 409 RTAKHNDLMVRGMLGrllftaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM---EAIEALNNALKDFA 485
Cdd:PRK10535 121 RLLRAQELLQRLGLE------DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLRDRG 194
|
90 100
....*....|....*....|....*....
gi 1180383029 486 GTLIFVSHDREfVSSLATRIIDIKDKQVI 514
Cdd:PRK10535 195 HTVIIVTHDPQ-VAAQAERVIEIRDGEIV 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-512 |
4.83e-06 |
|
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: 47.60 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 349 AVIGENGVGKTTFLRCLvnelksnegeikwsENATFGYCPQDSTK-DFDNDLTlfdwMSQWRTAKhNDLMVRGMLGRL-- 425
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL--------------KYALTGELPPNSKGgAHDPKLI----REGEVRAQ-VKLAFENANGKKyt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 426 -----------LFT-ADDSNK----KARNCSGGEKN------RLLFGKLMMQDVNVLVMDEPTNHMDMEAIE-ALNNALK 482
Cdd:cd03240 87 itrslailenvIFChQGESNWplldMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIE 166
|
170 180 190
....*....|....*....|....*....|....
gi 1180383029 483 DFAGTLIF----VSHDREFVSSLATRIIDIKDKQ 512
Cdd:cd03240 167 ERKSQKNFqlivITHDEELVDAADHIYRVEKDGR 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-190 |
5.27e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.14 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNvsitpgLKVGN--LS----------QDQ 73
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAGTapLAearedtrlmfQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 74 FAFEQYSVVDAVIMGDVELWKVKQERDriyslpemseedgmkvadLESVfaemdgyTAESRAEEilleagidkefhygLM 153
Cdd:PRK11247 91 RLLPWKKVIDNVGLGLKGQWRDAALQA------------------LAAV-------GLADRANE--------------WP 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 1180383029 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT 190
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-211 |
6.50e-06 |
|
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: 47.79 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 31 GLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQdQFAFEQYSVVDAVIMGDVelwkvkqerDRIYSLPEMsE 110
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQ-YIKADYEGTVRDLLSSIT---------KDFYTHPYF-K 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 111 EDGMKVADLESVfaemdgytaesraeeilleagIDKEfhyglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH- 189
Cdd:cd03237 97 TEIAKPLQIEQI---------------------LDRE-----VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEq 150
|
170 180
....*....|....*....|....*...
gi 1180383029 190 ------TITWLAneLNKRKcTMIIISHD 211
Cdd:cd03237 151 rlmaskVIRRFA--ENNEK-TAFVVEHD 175
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-506 |
7.15e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 46.66 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVnklgHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW------------SENATFGY 386
Cdd:cd03215 4 VLEV----RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 387 CPQDSTKDfdndlTLFDWMSQWRTAkhndlmvrgMLGRLLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPT 466
Cdd:cd03215 80 VPEDRKRE-----GLVLDLSVAENI---------ALSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 467 NHMDMEAIEALNNALKDFA---GTLIFVSHDREFVSSLATRII 506
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRIL 175
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
440-528 |
7.35e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM----EAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIdIKDKQVID 515
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII-VMNKGKCE 224
|
90
....*....|...
gi 1180383029 516 FQGTFDEYLASIE 528
Cdd:PRK13637 225 LQGTPREVFKEVE 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-473 |
7.40e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK----------WSENATFGYCP 388
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 389 QdstkdfdndltlFDWMSQWRTAKHNdLMVRG----MLGR---------LLFTADDSNKKAR--NCSGGEKNRLLFGKLM 453
Cdd:PRK13536 121 Q------------FDNLDLEFTVREN-LLVFGryfgMSTReieavipslLEFARLESKADARvsDLSGGMKRRLTLARAL 187
|
170 180
....*....|....*....|
gi 1180383029 454 MQDVNVLVMDEPTNHMDMEA 473
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHA 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-267 |
7.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.92 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKfgNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfaFEQYSVVDAVIMGDVELWK---- 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-----------------LFDGKPIDYSRKGLMKLREsvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 95 VKQERDRIYSLPEMSEEDGMKVADLESVFAEMdgytaESRAEEILLEAGI----DKEFHYglmanVAPGWKLRVLLAQAL 170
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIehlkDKPTHC-----LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 171 FANPDILLLDEPTNNLD---IHTITWLANELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKFLEAAGL 246
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
250 260
....*....|....*....|.
gi 1180383029 247 QREQLLAENAKKSAEIDELQD 267
Cdd:PRK13636 237 RKVNLRLPRIGHLMEILKEKD 257
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-310 |
7.90e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGlKVGNLSQDQFAFEQySVVDAVIMGDvelw 93
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG-SVAYVPQVSWIFNA-TVRENILFGS---- 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 94 kvKQERDRIYslpemseedgmKVADLESVFAEMDGYTAESRAEeiLLEAGIdkefhyglmaNVAPGWKLRVLLAQALFAN 173
Cdd:PLN03232 704 --DFESERYW-----------RAIDVTALQHDLDLLPGRDLTE--IGERGV----------NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 174 PDILLLDEPTNNLDIHTITWLANELNK---RKCTMIIISHDRHFLNSVcTHMADIDYGELRiYPGNYEKFLEAAGLQREq 250
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMKdelKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK-EEGTFAELSKSGSLFKK- 835
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 251 lLAENAKK---SAEIDELQDFVNRFG----ANASKAKQASSRAKKMDKIKLdeVKASSRMSPSLSFD 310
Cdd:PLN03232 836 -LMENAGKmdaTQEVNTNDENILKLGptvtIDVSERNLGSTKQGKRGRSVL--VKQEERETGIISWN 899
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
8.02e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 47.34 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG--ALVPSA---GNVSI------TPGL------ 64
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLdgediyDPDVdvvelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 65 -KVGNLSQ--DQFAFeqySVVDAVIMGdveLwKVKQERDRiyslpemseedgmkvadlesvfAEMDGytaesRAEEILLE 141
Cdd:COG1117 92 rRVGMVFQkpNPFPK---SIYDNVAYG---L-RLHGIKSK----------------------SELDE-----IVEESLRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 142 AGIDKEfhyglmanV-----APGWKL------RVLLAQALFANPDILLLDEPTNNLD-IHT--ITWLANELnKRKCTMII 207
Cdd:COG1117 138 AALWDE--------VkdrlkKSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTakIEELILEL-KKDYTIVI 208
|
...
gi 1180383029 208 ISH 210
Cdd:COG1117 209 VTH 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-518 |
1.13e-05 |
|
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: 45.78 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 349 AVIGENGVGKTTflrcLVNELKSNEGEIKWsenatfgycpQDSTKDFDNDLTLFdwMSQWRTakhndlMVRGMLGRLLFt 428
Cdd:cd03238 25 VVTGVSGSGKST----LVNEGLYASGKARL----------ISFLPKFSRNKLIF--IDQLQF------LIDVGLGYLTL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 429 addsNKKARNCSGGEKNRLLFGKLMMQDV--NVLVMDEPTNHMDMEAIEALNNALK---DFAGTLIFVSHDREFVSSlAT 503
Cdd:cd03238 82 ----GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLSS-AD 156
|
170 180
....*....|....*....|
gi 1180383029 504 RIIDI-----KDKQVIDFQG 518
Cdd:cd03238 157 WIIDFgpgsgKSGGKVVFSG 176
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-288 |
1.15e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlsqdqfafeqysvvdavimGDVELWKVKQE 98
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK--------------------------GSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 99 RDRIYSLPEMSEEDGMkvadlesvfaeMDGYTAESRAE---EILLEAGIDKeFHYGLMANVAPGWKLRVLLAQALFANPD 175
Cdd:PRK13545 96 LNGQLTGIENIELKGL-----------MMGLTKEKIKEiipEIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 176 ILLLDEPTNNLDiHTITWLA----NELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIY------PGNYEKFL-EAA 244
Cdd:PRK13545 164 ILVIDEALSVGD-QTFTKKCldkmNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDEFLkKYN 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1180383029 245 GLQREQLLAENAKKSAEIDE--LQDFVNRFGANASKAKQASSRAKK 288
Cdd:PRK13545 243 QMSVEERKDFREEQISQFQHglLQEDQTGRERKRKKGKKTSRKFKK 288
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-485 |
1.22e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.08 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 342 LEAGAKLAVIGENGVGKTTFLRCLVN--ELKSNEGEIKWS---ENATF----GYCPQdstkdfdNDLtlfdwmsqwrtak 412
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINgrpLDKNFqrstGYVEQ-------QDV------------- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 413 HND-LMVRGMLgrlLFTAddsnkKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFA 485
Cdd:cd03232 90 HSPnLTVREAL---RFSA-----LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
339-505 |
1.23e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDST-----------KDFDNdLT------- 400
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIalgigmvhqhfMLVPN-LTvaenivl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 ----LFDWMSQWRTAKHndlMVRGMLGRLLFTAdDSNKKARNCSGGEKNRL--LfgKLMMQDVNVLVMDEPTNHMDMEAI 474
Cdd:COG3845 104 glepTKGGRLDRKAARA---RIRELSERYGLDV-DPDAKVEDLSVGEQQRVeiL--KALYRGARILILDEPTAVLTPQEA 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1180383029 475 EALNNALKDFAG---TLIFVSHD-REfVSSLATRI 505
Cdd:COG3845 178 DELFEILRRLAAegkSIIFITHKlRE-VMAIADRV 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
162-217 |
1.52e-05 |
|
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: 46.06 E-value: 1.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKRKctMIIISHDRHFLNS 217
Cdd:cd03240 128 IRLALAETFGSNCGILALDEPTTNLDeenieesLAEIIEERKSQKNFQ--LIVITHDEELVDA 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-207 |
1.55e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.25 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGnRYGLI-GANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQFAFE-QYSVVD 83
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAG-EFKLItGPSGCGKSTLLKIVASLISPTSGTL-LFEGEDISTLKPEIYRQQvSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 84 AVIMGDVEL------WKVKQERdriyslPEMSEedgmKVADLesvfaemdgytAESRAEEILLEAGIdkefhyglmANVA 157
Cdd:PRK10247 90 PTLFGDTVYdnlifpWQIRNQQ------PDPAI----FLDDL-----------ERFALPDTILTKNI---------AELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1180383029 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDIHtitwlanelNKRKCTMII 207
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDES---------NKHNVNEII 180
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-522 |
1.55e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.03 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKW-------SENATFGYCP----------------------- 388
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYLPeerglypkmkvgeqlvylarlkg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 389 ---QDSTKDFDNDLTLFDwMSQWRtakhndlmvrgmlgrllftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEP 465
Cdd:COG4152 101 lskAEAKRRADEWLERLG-LGDRA-----------------------NKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 466 TNHMDMEAIEALNNALKDFA--G-TLIFVSHDREFVSSLATRIIDIKDKQVIdFQGTFDE 522
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAakGtTVIFSSHQMELVEELCDRIVIINKGRKV-LSGSVDE 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-212 |
1.61e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 47.25 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ----FAFE 77
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENrhvnTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 78 QY------SVVDAVIMGdVELWKV-KQE-RDRIyslpemseEDGMKVADLESvfaemdgytaesraeeilleagidkefh 149
Cdd:PRK09452 94 SYalfphmTVFENVAFG-LRMQKTpAAEiTPRV--------MEALRMVQLEE---------------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 150 yglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRK--CTMIIISHDR 212
Cdd:PRK09452 137 ---FAQRKPhqlsgGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKlgITFVFVTHDQ 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-211 |
1.67e-05 |
|
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: 45.50 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 17 FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQdqfafeqysvvdavimgdvelwkvk 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-GKPVTRRSP------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 97 qeRDRIyslpemseEDGMkvadlesvfaemdGYTAESRAEE-ILLEAGIdkefhyglMANVAPGWKL------RVLLAQA 169
Cdd:cd03215 70 --RDAI--------RAGI-------------AYVPEDRKREgLVLDLSV--------AENIALSSLLsggnqqKVVLARW 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1180383029 170 LFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHD 211
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAkaeIYRLIRELADAGKAVLLISSE 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-211 |
1.75e-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: 47.37 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 31 GLIGANGCGKSTFMKILSGaLVPSAGNVSITpGLKVGNLSQDQFafeqysvvdavimgdvelwkvKQERDRI-------Y 103
Cdd:COG4172 316 GLVGESGSGKSTLGLALLR-LIPSEGEIRFD-GQDLDGLSRRAL---------------------RPLRRRMqvvfqdpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 104 -SL-PEMSEED----GMKVadlesVFAEMDGYTAESRAEEILLEAGIDKEfhyglMANVAP-----GWKLRVLLAQALFA 172
Cdd:COG4172 373 gSLsPRMTVGQiiaeGLRV-----HGPGLSAAERRARVAEALEEVGLDPA-----ARHRYPhefsgGQRQRIAIARALIL 442
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 173 NPDILLLDEPTNNLDI---HTITWLANELNKR-KCTMIIISHD 211
Cdd:COG4172 443 EPKLLVLDEPTSALDVsvqAQILDLLRDLQREhGLAYLFISHD 485
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
1.84e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.31 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILS--GALVPsagNVSIT------------PGLKV 66
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTITgsivynghniysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 67 GNLSQD-QFAFEQ-----YSVVDAVIMGdvelWKVKQERDRiyslpemseedgmKVADlESVFAEMDGYTAESRAEEILL 140
Cdd:PRK14239 82 VDLRKEiGMVFQQpnpfpMSIYENVVYG----LRLKGIKDK-------------QVLD-EAVEKSLKGASIWDEVKDRLH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 141 EAGIdkefhyGLmanvAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRKCTMIIISH 210
Cdd:PRK14239 144 DSAL------GL----SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLglKDDYTMLLVTR 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
159-211 |
2.00e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.64 E-value: 2.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMII-ISHD 211
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTAIImITHD 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
2.11e-05 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 45.54 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 13 AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItPGlkvgnlsqdQFAF-EQYS-VVDAVImgdv 90
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PG---------SIAYvSQEPwIQNGTI---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 91 elwkvkqeRDRIyslpemseedgmkvadlesVF-AEMDgytaESRAEEIL----LEAGIdKEFHYGLM-------ANVAP 158
Cdd:cd03250 83 --------RENI-------------------LFgKPFD----EERYEKVIkacaLEPDL-EILPDGDLteigekgINLSG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN-----ELNKRKcTMIIISHDRHFL 215
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNK-TRILVTHQLQLL 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-513 |
2.21e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.16 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVN------------ELKSNE--------GEIKWS 379
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagshiELLGRTvqregrlaRDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 380 ENATfGYCPQ-----DSTKDFDNDL-----------TLFDWMSQWRTAKHNDLMVR-GMlgrllftADDSNKKARNCSGG 442
Cdd:PRK09984 85 RANT-GYIFQqfnlvNRLSVLENVLigalgstpfwrTCFSWFTREQKQRALQALTRvGM-------VHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 443 EKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG----TLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
438-521 |
2.79e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 438 NCSGGEKNRL-LFGKLMMqDVNVLVMDEPTNHMD----MEAIEALNNaLKDFAGTLIFVSHDREFVSSLATRIIDIKDKQ 512
Cdd:PRK13651 165 ELSGGQKRRVaLAGILAM-EPDFLVFDEPTAGLDpqgvKEILEIFDN-LNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
....*....
gi 1180383029 513 VIDFQGTFD 521
Cdd:PRK13651 243 IIKDGDTYD 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
315-510 |
3.10e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKD 394
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 ----FDNDLTLFDWMSQWRTAKHNDLMVRGMLG--------------RLLFTAD---DSNKKARNCSGGEKNRLLFGKLM 453
Cdd:PRK09700 81 gigiIYQELSVIDELTVLENLYIGRHLTKKVCGvniidwremrvraaMMLLRVGlkvDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 454 MQDVNVLVMDEPTNHMDMEAIE---ALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKD 510
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDylfLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKD 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-376 |
3.10e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.69 E-value: 3.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI 376
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
155-302 |
3.31e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTI-----TWLANELnkRKCTMIIISHDRHFLNSV----CTHMADI 225
Cdd:PLN03130 740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGrqvfdKCIKDEL--RGKTRVLVTNQLHFLSQVdriiLVHEGMI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 226 D----YGELRIYPGNYEKFLEAAGlQREQLLAENAKKSAEIDELQDFVNrfgANASKAKQASSRAKKMDKIKLDEVKASS 301
Cdd:PLN03130 818 KeegtYEELSNNGPLFQKLMENAG-KMEEYVEENGEEEDDQTSSKPVAN---GNANNLKKDSSSKKKSKEGKSVLIKQEE 893
|
.
gi 1180383029 302 R 302
Cdd:PLN03130 894 R 894
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
440-525 |
3.50e-05 |
|
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: 45.22 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM--EAI--EALNNALKDFagTLIFVSHdRefVSSL--ATRIIDIKDKQV 513
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAesEKLvqEALDRAMKGR--TTIVIAH-R--LSTIrnADLIAVLQNGQV 215
|
90
....*....|..
gi 1180383029 514 IDfQGTFDEYLA 525
Cdd:cd03249 216 VE-QGTHDELMA 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-224 |
3.52e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.31 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 32 LIGANGCGKSTFMKILSGaLVPSAGNVSItpglkvgnlsqDQFAFEQYSVVD-AVIMGdvelWKVKQERDrIYSLP---- 106
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIQF-----------AGQPLEAWSAAElARHRA----YLSQQQTP-PFAMPvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 107 -EMSEEDGMKVADLESVFAEMdgytaesrAEEILLEagiDKefhYGLMANVAPG--WKlRVLLAQALF-----ANPD--I 176
Cdd:PRK03695 90 lTLHQPDKTRTEAVASALNEV--------AEALGLD---DK---LGRSVNQLSGgeWQ-RVRLAAVVLqvwpdINPAgqL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 177 LLLDEPTNNLDIHTITWLaNELNKRKC----TMIIISHDrhfLNSVCTHmAD 224
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAAL-DRLLSELCqqgiAVVMSSHD---LNHTLRH-AD 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-78 |
3.77e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 3.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpgLKVGNLSQDQFAFEQ 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL----FERQSIKKDLCTYQK 74
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
388-526 |
4.17e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQDSTKDFDNDLTLFDwmsqwRTAKHNDLMVRGMLGRLLFTAD------DSNKKARNCSGGEKNRL-LFGKLMMQDVNVL 460
Cdd:TIGR00630 437 SIREAHEFFNQLTLTP-----EEKKIAEEVLKEIRERLGFLIDvgldylSLSRAAGTLSGGEAQRIrLATQIGSGLTGVL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 461 -VMDEPT-------NHmdmEAIEALNNaLKDFAGTLIFVSHDREFVSSlATRIIDIKDK------QVIdFQGTFDEYLAS 526
Cdd:TIGR00630 512 yVLDEPSiglhqrdNR---RLINTLKR-LRDLGNTLIVVEHDEDTIRA-ADYVIDIGPGagehggEVV-ASGTPEEILAN 585
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
320-528 |
6.38e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGF-DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGE-------IKWSENA------TFG 385
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlikgepIKYDKKSllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 386 YCPQDS-------TKDFD---NDLTLFDWMSQWRTAKHNDLMVRGMLGRllftaddSNKKARNCSGGEKNRLLFGKLMMQ 455
Cdd:PRK13639 82 IVFQNPddqlfapTVEEDvafGPLNLGLSKEEVEKRVKEALKAVGMEGF-------ENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180383029 456 DVNVLVMDEPTNHMDMEAIEALNNALKDF---AGTLIFVSHDREFVSSLATRIIDIKDKQVIDfQGTFDEYLASIE 528
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIK-EGTPKEVFSDIE 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-211 |
6.49e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.00 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPLFE-----NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSA-----GNVSITPGLK----VGNLSQ 71
Cdd:PRK13645 11 NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETgqtivGDYAIPANLKkikeVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 72 D---QFAFEQYSVVDAVIMGDVELWKVkqerdriySLPEMSEEDGMKVADLESVFAEMDGYTAESRAEeilleagidkef 148
Cdd:PRK13645 91 EiglVFQFPEYQLFQETIEKDIAFGPV--------NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFE------------ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 149 hyglmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKRkctMIIISHD 211
Cdd:PRK13645 151 -------LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeedfINLFERLNKEYKKR---IIMVTHN 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-471 |
6.55e-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: 46.06 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 340 FLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSenATFGYCPQDS------TKD------------------- 394
Cdd:TIGR01271 447 FKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS--GRISFSPQTSwimpgtIKDniifglsydeyrytsvika 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 395 --FDNDLTLFdwmsqwrtaKHNDLMVRGMLGRLLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:TIGR01271 525 cqLEEDIALF---------PEKDKTVLGEGGITL-------------SGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-209 |
6.66e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 6.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIIS 209
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAkaeIYRLIRELAAEGKAVIVIS 451
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-525 |
8.30e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.20 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 305 PSLSF--DEGKKMYRQALEVNKLGHGFDGETL--FSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIK--- 377
Cdd:PRK11160 322 PEVTFptTSTAAADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlng 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 378 -----WSENA---TFGYCPQ------DSTKDfdnDLTLfdwmsqwrtAKHN-------DLMVRGMLGRLLftaddSNKKA 436
Cdd:PRK11160 402 qpiadYSEAAlrqAISVVSQrvhlfsATLRD---NLLL---------AAPNasdealiEVLQQVGLEKLL-----EDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 437 RNC---------SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEALnnaLKDFAG--TLIFVSHDREFVSSLa 502
Cdd:PRK11160 465 LNAwlgeggrqlSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILEL---LAEHAQnkTVLMITHRLTGLEQF- 540
|
250 260
....*....|....*....|...
gi 1180383029 503 TRIIDIKDKQVIDfQGTFDEYLA 525
Cdd:PRK11160 541 DRICVMDNGQIIE-QGTHQELLA 562
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
339-526 |
8.49e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEG-------------EIKWSENATFGycpqdstkdfDNDL--TLFD 403
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvirgtvayvpQVSWIFNATVR----------DNILfgSPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 404 WMSQWR----TAKHNDLmvrgmlgRLLFTADDSNKKAR--NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME-AIEA 476
Cdd:PLN03130 707 PERYERaidvTALQHDL-------DLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 477 LNNALKDFAG--TLIFVSHDREFVSSLaTRIIDIKDKQVIDfQGTFDEYLAS 526
Cdd:PLN03130 780 FDKCIKDELRgkTRVLVTNQLHFLSQV-DRIILVHEGMIKE-EGTYEELSNN 829
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-505 |
8.89e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.39 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 349 AVIGENGVGKTTFLRCLVNELKSNEG-------EIKWSENA---TFGYCPQDSTkdFDNDLT-----LFDWMSQWRTAKH 413
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGtvlvggkDIETNLDAvrqSLGMCPQHNI--LFHHLTvaehiLFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 414 NDLMVRGMLgrllftaDDS------NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG- 486
Cdd:TIGR01257 1038 AQLEMEAML-------EDTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSg 1110
|
170 180
....*....|....*....|
gi 1180383029 487 -TLIFVSHDREFVSSLATRI 505
Cdd:TIGR01257 1111 rTIIMSTHHMDEADLLGDRI 1130
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-514 |
8.93e-05 |
|
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: 43.64 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQD---STKDFDNDLtlfdwMSQWRTAKHND 415
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQENNL-----FAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 416 LmvrGMLGRLLFTADDSNK----------------KARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDmeaiEALNN 479
Cdd:cd03298 93 L---GLSPGLKLTAEDRQAievalarvglaglekrLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD----PALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1180383029 480 ALKDFAG--------TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03298 166 EMLDLVLdlhaetkmTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
430-526 |
9.54e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 430 DDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM---EAIEALNNALKDfAGTLIFVSHDREFVSSLATRII 506
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVA 223
|
90 100
....*....|....*....|
gi 1180383029 507 DIKDKQVIDFqGTFDEYLAS 526
Cdd:PRK14246 224 FLYNGELVEW-GSSNEIFTS 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-518 |
1.06e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELnKRKCTM--IIISHDrhfLNSVcTHMADidygelriy 233
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLREL-QQELNMglLFITHN---LSIV-RKLAD--------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 234 pgnyekflEAAGLQREQLLAENAKKSAeidelqdfvnrFGANASKAKQASSRAKKMDkiklDEVKASSRMSPSLSFDEGK 313
Cdd:PRK15134 226 --------RVAVMQNGRCVEQNRAATL-----------FSAPTHPYTQKLLNSEPSG----DPVPLPEPASPLLDVEQLQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 314 KMY--RQALEVNKLGHgfdgETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSnEGEI--------KWSENAT 383
Cdd:PRK15134 283 VAFpiRKGILKRTVDH----NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIwfdgqplhNLNRRQL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 384 FGYCP------QDSTKDFDNDLTLFDWMSQ-------WRTAKHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFG 450
Cdd:PRK15134 358 LPVRHriqvvfQDPNSSLNPRLNVLQIIEEglrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIA 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 451 KLMMQDVNVLVMDEPTNHMD---MEAIEALNNALK-DFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDfQG 518
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDktvQAQILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE-QG 508
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
329-505 |
1.10e-04 |
|
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: 43.76 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 329 FDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIkwsenaTFGycpqdstkdfDNDLT-------- 400
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI------LLD----------GKDITnlpphkrp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 401 ---------LFDWMSQW-------RTAKHN----DLMVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVL 460
Cdd:cd03300 74 vntvfqnyaLFPHLTVFeniafglRLKKLPkaeiKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1180383029 461 VMDEPTNHMDMEAIEALNNALKDFAG----TLIFVSHDREFVSSLATRI 505
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-510 |
1.16e-04 |
|
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: 43.47 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 350 VIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFGYCPQDSTKD------------------FDNDLTLFDWMSQWRTA 411
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysvayaaqkpwllnatVEENITFGSPFNKQRYK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 412 KHNDLMVRGMLGRLLFTADDSNKKAR--NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNA-----LKDF 484
Cdd:cd03290 112 AVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDD 191
|
170 180
....*....|....*....|....*.
gi 1180383029 485 AGTLIFVSHDREFVSSlATRIIDIKD 510
Cdd:cd03290 192 KRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
439-509 |
1.22e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 439 CSGGEKNR----LLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVsSLATRIIDIK 509
Cdd:cd03227 78 LSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkgaQVIVITHLPELA-ELADKLIHIK 154
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-526 |
1.41e-04 |
|
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: 43.44 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 330 DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRcLVNEL-KSNEGEIK--------WSENA---TFGYCPQdSTKDF-- 395
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFidgedireQDPVElrrKIGYVIQ-QIGLFph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 396 ----DND---LTLFDWMSQWRTAKHNDLMvrGMLGrlLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNH 468
Cdd:cd03295 90 mtveENIalvPKLLKWPKEKIRERADELL--ALVG--LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 469 MDMEAIEALNNAL----KDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFqGTFDEYLAS 526
Cdd:cd03295 166 LDPITRDQLQEEFkrlqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEILRS 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-210 |
1.53e-04 |
|
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: 42.92 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALvpsagnvsITPGLKvgnlsqdqfafeqysvvdavimGDVE 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR--------TGLGVS----------------------GEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 92 LWKVKQERDRIYSLPEMSEEDGMKVADLeSVFaEMDGYTAESRaeeilleagidkefhyGLMAnvapGWKLRVLLAQALF 171
Cdd:cd03213 70 INGRPLDKRSFRKIIGYVPQDDILHPTL-TVR-ETLMFAAKLR----------------GLSG----GERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1180383029 172 ANPDILLLDEPTNNLD-------IHTITWLANElnkrKCTMIIISH 210
Cdd:cd03213 128 SNPSLLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIH 169
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
440-525 |
1.79e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 43.08 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFAGTLI---FVSHDREFVSSLATRIIDIKDKQVIDf 516
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGRIIE- 221
|
90 100
....*....|....*....|
gi 1180383029 517 QGT-----------FDEYLA 525
Cdd:COG4161 222 QGDashftqpqteaFAHYLS 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
126-224 |
2.02e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 43.90 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 126 MDGYTAESRAEEILLEAGI-DKEFhyglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLAN 196
Cdd:COG4172 125 LSGAAARARALELLERVGIpDPER----RLDAYPhqlsgGQRQRVMIAMALANEPDLLIADEPTTALDVTVqaqILDLLK 200
|
90 100
....*....|....*....|....*....
gi 1180383029 197 ELNKR-KCTMIIISHDrhfLNSVcTHMAD 224
Cdd:COG4172 201 DLQRElGMALLLITHD---LGVV-RRFAD 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
331-493 |
2.20e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.97 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 331 GETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLvnelksneGEI---------KWSENATFgYCPQ------------ 389
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELwpvyggrltKPAKGKLF-YVPQrpymtlgtlrdq 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 ----DSTKDF-DNDLTLFDWMSQWRTAKHNDLMVRGmlGRLLFTADDSNKkarnCSGGEKNRLLFGKLMMQDVNVLVMDE 464
Cdd:TIGR00954 535 iiypDSSEDMkRRGLSDKDLEQILDNVQLTHILERE--GGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180
....*....|....*....|....*....
gi 1180383029 465 PTNHMDMEAIEALNNALKDFAGTLIFVSH 493
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-245 |
2.57e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 43.66 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEQYSVVdavimgdve 91
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN-GQPIADYSEAALR-QAISVV--------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 92 lwkvkQERDRIYSlpeMSEEDGMKVADLESVFAEMdgytaesraEEILLEAGIDKefhygLMANVAP------------- 158
Cdd:PRK11160 420 -----SQRVHLFS---ATLRDNLLLAAPNASDEAL---------IEVLQQVGLEK-----LLEDDKGlnawlgeggrqls 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 -GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISHDRHFLnsvcTHMADI---DYGELR 231
Cdd:PRK11160 478 gGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILELLAEHAQNK-TVLMITHRLTGL----EQFDRIcvmDNGQII 552
|
250
....*....|....
gi 1180383029 232 IYpGNYEKFLEAAG 245
Cdd:PRK11160 553 EQ-GTHQELLAQQG 565
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
437-526 |
2.62e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.80 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 437 RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDfagtlifVSHDR-EFV-----SSL--ATRIIDI 508
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGRtTFIiahrlSTVrnADRILVF 542
|
90
....*....|....*...
gi 1180383029 509 KDKQVIDfQGTFDEYLAS 526
Cdd:PRK13657 543 DNGRVVE-SGSFDELVAR 559
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-493 |
2.77e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCL-----VNELKSNEGEIK------WSENA----- 382
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRlfgrniYSPDVdpiev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 383 ------TFGY-CPQDSTKDFDNDLTLFDWMSQWRTAKHNDLMVRGMLGRLLF---TADDSNKKARNCSGGEKNRLLFGKL 452
Cdd:PRK14267 84 rrevgmVFQYpNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1180383029 453 MMQDVNVLVMDEPTNHMD---MEAIEALNNALKDfAGTLIFVSH 493
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTH 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
315-514 |
3.02e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 315 MYRQALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCL--VNELKSNEGEIKWSENATFGYCPQDST 392
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 393 KD----FDNDLTLFDWMS---------QWRTAK--HNDLMVRG---MLGRLLFTAdDSNKKARNCSGGEKNRLLFGKLMM 454
Cdd:PRK13549 81 RAgiaiIHQELALVKELSvleniflgnEITPGGimDYDAMYLRaqkLLAQLKLDI-NPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 455 QDVNVLVMDEPTNHMDMEAIEALNNALKDFAG---TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-210 |
3.13e-04 |
|
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: 42.10 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQF--GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI------TPGL-----KVGNLSQD 72
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdisKIGLhdlrsRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 73 QFAFE-----------QYSvvdavimgDVELWKVKQE---RDRIYSLPEMseedgmkvadLESVFAEMDgytaesraeei 138
Cdd:cd03244 87 PVLFSgtirsnldpfgEYS--------DEELWQALERvglKEFVESLPGG----------LDTVVEEGG----------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 139 lleagidkefhyglmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:cd03244 138 ---------------ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-187 |
3.20e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.33 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 5 ANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPS-------AGNVSIT-PGLK-VGNLSQDQFA 75
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftgtilANNRKPTkQILKrTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 76 FEQYSVVDAVIMgdVELWKvkqerdriysLPE-MSEEDGMKVAdlESVFAEMdGYTaesRAEEILleagIDKEFHYGlma 154
Cdd:PLN03211 152 YPHLTVRETLVF--CSLLR----------LPKsLTKQEKILVA--ESVISEL-GLT---KCENTI----IGNSFIRG--- 206
|
170 180 190
....*....|....*....|....*....|...
gi 1180383029 155 nVAPGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PLN03211 207 -ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-510 |
3.34e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.17 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 307 LSFDEGKKMY---RQALEvnklghgfdgetlfsGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWS---- 379
Cdd:PRK10908 2 IRFEHVSKAYlggRQALQ---------------GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 380 ---ENATFGYCPQDSTKDFDNDLTLFDwmsqwRTAKHN---DLMVRGMLG----RLLFTADDSN---KKARN----CSGG 442
Cdd:PRK10908 67 trlKNREVPFLRRQIGMIFQDHHLLMD-----RTVYDNvaiPLIIAGASGddirRRVSAALDKVgllDKAKNfpiqLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 443 EKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF---AGTLIFVSHDREFVSSLATRIIDIKD 510
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-261 |
3.43e-04 |
|
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: 43.78 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglKVGNLSQdQFAFEQYSV 81
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQ-QAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 VDAVIMGdvelwkvKQERDRIYSlpemseedgmKVADLESVFAEMDGYTAESRAEeiLLEAGIdkefhyglmaNVAPGWK 161
Cdd:TIGR00957 716 RENILFG-------KALNEKYYQ----------QVLEACALLPDLEILPSGDRTE--IGEKGV----------NLSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL--------NKrkcTMIIISHDRHFL--NSVCTHMADIDYGELR 231
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpegvlkNK---TRILVTHGISYLpqVDVIIVMSGGKISEMG 843
|
250 260 270
....*....|....*....|....*....|....*.
gi 1180383029 232 IYP------GNYEKFLEAAGLQREQLLAENAKKSAE 261
Cdd:TIGR00957 844 SYQellqrdGAFAEFLRTYAPDEQQGHLEDSWTALV 879
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
440-525 |
3.44e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 42.31 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGK-LMMQDvNVLVMDEPTNHMDMEAIEALNNALKDFAGTLI---FVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK11124 143 SGGQQQRVAIARaLMMEP-QVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVE 221
|
90 100
....*....|....*....|.
gi 1180383029 516 fQGT-----------FDEYLA 525
Cdd:PRK11124 222 -QGDascftqpqteaFKNYLS 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-58 |
3.65e-04 |
|
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: 42.28 E-value: 3.65e-04
10 20
....*....|....*....|....*...
gi 1180383029 31 GLIGANGCGKSTFMKILSGALVPSAGNV 58
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSI 60
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-241 |
3.92e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV---------SITPGLKvGNLSQ-DQFAFEQysvvdaVIM 87
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrngevsviAISAGLS-GQLTGiENIEFKM------LCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 88 GdvelWKVKQERDRiysLPEMSEedgmkvadlesvFAEMDgytaesraeeilleagidkEFHYGLMANVAPGWKLRVLLA 167
Cdd:PRK13546 114 G----FKRKEIKAM---TPKIIE------------FSELG-------------------EFIYQPVKKYSSGMRAKLGFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 168 QALFANPDILLLDEPtnnLDIHTITWLANELNK------RKCTMIIISHDRHFLNSVCTHMADI------DYGELRIYPG 235
Cdd:PRK13546 156 INITVNPDILVIDEA---LSVGDQTFAQKCLDKiyefkeQNKTIFFVSHNLGQVRQFCTKIAWIeggklkDYGELDDVLP 232
|
....*.
gi 1180383029 236 NYEKFL 241
Cdd:PRK13546 233 KYEAFL 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
330-495 |
4.20e-04 |
|
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: 42.15 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 330 DGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVnELKSNEGEI-------------KWSEnaTFGYCPQDS---TK 393
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIqidgvswnsvplqKWRK--AFGVIPQKVfifSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 394 DFDNDLTLFD-WMSQ--WRTAKHNDL--MVRGMLGRLLFTADDSNkkarnC--SGGEKNRLLFGKLMMQDVNVLVMDEPT 466
Cdd:cd03289 92 TFRKNLDPYGkWSDEeiWKVAEEVGLksVIEQFPGQLDFVLVDGG-----CvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|
gi 1180383029 467 NHMDMEAIEALNNALKD-FAGTLIFVSHDR 495
Cdd:cd03289 167 AHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
433-508 |
4.23e-04 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.86 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 433 NKKARNCSGGEKNRL-LFGKLMMQDVNVL-VMDEPT----NHMDMEAIEALNNaLKDFAGTLIFVSHDREFVsSLATRII 506
Cdd:cd03270 132 SRSAPTLSGGEAQRIrLATQIGSGLTGVLyVLDEPSiglhPRDNDRLIETLKR-LRDLGNTVLVVEHDEDTI-RAADHVI 209
|
..
gi 1180383029 507 DI 508
Cdd:cd03270 210 DI 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-216 |
4.73e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQF----GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGAlvpSAGNVSITPglkvgnlsqDQFAFEqysv 81
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTA---------DRMRFD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgDVELWKVK-QERDR--------IYSLPEMSEEDGMKVAdlESVFAEMDGYTAES-----------RAEEILLE 141
Cdd:PRK15093 72 -------DIDLLRLSpRERRKlvghnvsmIFQEPQSCLDPSERVG--RQLMQNIPGWTYKGrwwqrfgwrkrRAIELLHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 142 AGIDKefHYGLMAN----VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMI-IISHDRH 213
Cdd:PRK15093 143 VGIKD--HKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqIFRLLTRLNQNNNTTIlLISHDLQ 220
|
...
gi 1180383029 214 FLN 216
Cdd:PRK15093 221 MLS 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
342-522 |
4.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 342 LEAGAKLAVIGENGVGKTTFLRCLVNELKSNEG---EIKwsenATFGYCPQDS----TKDFDNDLTLFDWMSQ--WR--- 409
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELSHAETssvVIR----GSVAYVPQVSwifnATVRENILFGSDFESEryWRaid 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 410 -TAKHNDLMvrgmlgrlLFTADDSNK---KARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME-AIEALNNALKD- 483
Cdd:PLN03232 716 vTALQHDLD--------LLPGRDLTEigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDe 787
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1180383029 484 -FAGTLIFVSHDREFVsSLATRIIDIKDKqVIDFQGTFDE 522
Cdd:PLN03232 788 lKGKTRVLVTNQLHFL-PLMDRIILVSEG-MIKEEGTFAE 825
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-238 |
5.08e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeqysvvdavimgdvelwkvkqerdriyslp 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 107 emseedgmkvadlesVFAEMDGYTAESRAEEILLEAGIDKEFHYGLManvapgwKLRVLLAQALFANPDILLLDEPTNNL 186
Cdd:smart00382 34 ---------------IYIDGEDILEEVLDQLLLIIVGGKKASGSGEL-------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 187 DIHT---------ITWLANELNKRKCTMIIISHDRHFLNSvcthMADIDYGELRIYPGNYE 238
Cdd:smart00382 92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGP----ALLRRRFDRRIVLLLIL 148
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-60 |
5.32e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.48 E-value: 5.32e-04
10 20
....*....|....*....|....*....
gi 1180383029 32 LIGANGCGKSTFMKILSGALVPSAGNVSI 60
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-255 |
5.34e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.52 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 13 AEPLFENISAkfgnGNRYGLIGANGCGKSTFMKILSGALvPSAGNVSITpGLKVGNLS------------QDQFAFEQyS 80
Cdd:PRK11174 366 AGPLNFTLPA----GQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKIN-GIELRELDpeswrkhlswvgQNPQLPHG-T 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 81 VVDAVIMGDvelwkvkqerdriyslPEMSEEDGMKVADLesvfaemdgytaeSRAEEIL--LEAGIDKEFHYGlMANVAP 158
Cdd:PRK11174 439 LRDNVLLGN----------------PDASDEQLQQALEN-------------AWVSEFLplLPQGLDTPIGDQ-AAGLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRHFLnsvcTHMADI---DYGELrIY 233
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQLEDL----AQWDQIwvmQDGQI-VQ 563
|
250 260
....*....|....*....|..
gi 1180383029 234 PGNYEKFLEAAGLQREqLLAEN 255
Cdd:PRK11174 564 QGDYAELSQAGGLFAT-LLAHR 584
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
154-209 |
7.37e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 7.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIIS 209
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakYEIYKLINQLVQQGVAIIVIS 462
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-526 |
7.56e-04 |
|
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: 41.32 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF-AG-TLIFVSHDREFVSSlATRIIDIKDKQVIDfQ 517
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-Q 217
|
....*....
gi 1180383029 518 GTFDEYLAS 526
Cdd:cd03252 218 GSHDELLAE 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
163-221 |
8.49e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.10 E-value: 8.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 163 RVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKR--KCTMIIISHdRHFLNSVCTH 221
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDR 552
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
440-500 |
8.55e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 8.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 440 SGGEKN------RLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNN----ALKDFAG--TLIFVSHDREFVSS 500
Cdd:PRK01156 803 SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSV 875
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-209 |
8.73e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 8.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 164 VLLAQALFANPDILLLDEPTNNLD------IHTITwlaNELNKRKCTMIIIS 209
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDvgakyeIYTII---NELAAEGKGVIVIS 461
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
339-471 |
9.46e-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: 41.38 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 339 DFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATFgyCPQDS------TKD------------------ 394
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISF--SSQFSwimpgtIKEniifgvsydeyryksvvk 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 395 ---FDNDLTLFdwmsqwrTAKHNDLMVRGMLgrllftaddsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:cd03291 135 acqLEEDITKF-------PEKDNTVLGEGGI---------------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
1.02e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILS--GALVPSAgnvsitpglkvgnLSQDQFAFEQY 79
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGF-------------RVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 80 SVVDavimGDVELWKVkqeRDRI-------YSLPEMSEEDGMKVADLESVFAEMDGYTAESRAEEILLEAGIDKEFHYGL 152
Cdd:PRK14243 78 NLYA----PDVDPVEV---RRRIgmvfqkpNPFPKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSGL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180383029 153 maNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-IHT--ITWLANELnKRKCTMIIISHD 211
Cdd:PRK14243 151 --SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTlrIEELMHEL-KEQYTIIIVTHN 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
153-228 |
1.02e-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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 153 MANVAPGWKLRVLLAQALFANPD--ILLLDEPTNNLDIHTITWLANELNK---RKCTMIIISHDRHFLNSvcthmAD--I 225
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlidLGNTVILIEHNLDVLSS-----ADwiI 159
|
...
gi 1180383029 226 DYG 228
Cdd:cd03238 160 DFG 162
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
440-525 |
1.02e-03 |
|
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: 40.68 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME---AI-EALNNALKDfaGTLIFVSHDREFVSSlATRIIDIKDKQVID 515
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDTEserLVqAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
90
....*....|
gi 1180383029 516 fQGTFDEYLA 525
Cdd:cd03251 217 -RGTHEELLA 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-493 |
1.12e-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: 40.55 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 340 FLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEI-------------KWSENatFGYCPQDSTkdfdndltLF---- 402
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhDLRSR--ISIIPQDPV--------LFsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 403 ----DWMSQ------WRTAK--HNDLMVRGMLGRLLFTADDSNKkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:cd03244 95 rsnlDPFGEysdeelWQALErvGLKEFVESLPGGLDTVVEEGGE---NLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180
....*....|....*....|....*
gi 1180383029 471 MEAIEALNNALKD-FAG-TLIFVSH 493
Cdd:cd03244 172 PETDALIQKTIREaFKDcTVLTIAH 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
440-504 |
1.18e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.53 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNAL----KDFAGTLIFVSHDrefvSSLATR 504
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD----LQLAAR 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-211 |
1.25e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 6 NITMQFGAEPL----FENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVSitpglkvgnlsQDQFAFEQYsv 81
Cdd:PRK11022 8 KLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVM-----------AEKLEFNGQ-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 82 vdavimgDVELWKVKQERDRIYSLPEMSEEDGMKVAD---------LESVFAEMDG--YTAESRAEEILLEAGI-DKEFH 149
Cdd:PRK11022 74 -------DLQRISEKERRNLVGAEVAMIFQDPMTSLNpcytvgfqiMEAIKVHQGGnkKTRRQRAIDLLNQVGIpDPASR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180383029 150 YglmaNVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKC-TMIIISHD 211
Cdd:PRK11022 147 L----DVYPhqlsgGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqAQIIELLLELQQKENmALVLITHD 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-59 |
1.49e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS 59
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-522 |
1.76e-03 |
|
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: 40.02 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 319 ALEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWS-ENATfGYCPQDSTKDFD- 396
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgEDAT-DVPVQERNVGFVf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 397 ------NDLTLFDWMS-----QWRTAKHNDLMVRGMLGRLLFTADDSNKKAR---NCSGGEKNRLLFGKLMMQDVNVLVM 462
Cdd:cd03296 81 qhyalfRHMTVFDNVAfglrvKPRSERPPEAEIRAKVHELLKLVQLDWLADRypaQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 463 DEPTNHMDMEAIEALNNALK----DFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFqGTFDE 522
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV-GTPDE 223
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-216 |
2.09e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL--------NKRKCTMIIISHDRHFLN 216
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsQQRNFQLLVITHDEDFVE 1274
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
2.29e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.12 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 1 MISTANITMQFGAEPLF--ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGnvsitpglkvgnlsqdQFAFEQ 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG----------------EIFYNN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 79 YSVVDAvimgdvELWKVKQERDRIYSLPEmSEEDGMKVA-----DLE--SV-FAEMDGYTAESRAEEILLEAGiDKEFHy 150
Cdd:PRK13648 71 QAITDD------NFEKLRKHIGIVFQNPD-NQFVGSIVKydvafGLEnhAVpYDEMHRRVSEALKQVDMLERA-DYEPN- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180383029 151 glmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRK-CTMIIISHD 211
Cdd:PRK13648 142 ----ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDarqNLLDLVRKVKSEHnITIISITHD 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
143-210 |
3.25e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 3.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 143 GIDKEFHYGlMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:PLN03232 1360 GLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAH 1428
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-49 |
3.55e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1180383029 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG 49
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-506 |
4.19e-03 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 39.36 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENATF----------GYCPQ 389
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlpprerrvGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 390 dstkDFDndltLFDWMS-----------QWRTAKHNDLMVRGMLGrlLFTADD-SNKKARNCSGGEKNRLLFGKLMMQDV 457
Cdd:COG1118 83 ----HYA----LFPHMTvaeniafglrvRPPSKAEIRARVEELLE--LVQLEGlADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1180383029 458 NVLVMDEPtnhmdMEAIEA---------LNNALKDFAGTLIFVSHDREFVSSLATRII 506
Cdd:COG1118 153 EVLLLDEP-----FGALDAkvrkelrrwLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-517 |
5.24e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 349 AVIGENGVGKTTFLRCLVNELKSNEGEIKWS-ENATFgycpQDSTKDFDNDLTLFDwmSQWRTAKHNDLMVRGMLGRL-- 425
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQgKEIDF----KSSKEALENGISMVH--QELNLVLQRSVMDNMWLGRYpt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 426 --LFTAD------------------DSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALN---NALK 482
Cdd:PRK10982 102 kgMFVDQdkmyrdtkaifdeldidiDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFtiiRKLK 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1180383029 483 DFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQ 517
Cdd:PRK10982 182 ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQ 216
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-58 |
5.35e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 5.35e-03
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
340-372 |
5.77e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.62 E-value: 5.77e-03
10 20 30
....*....|....*....|....*....|....
gi 1180383029 340 FLLEAGAKLAVI-GENGVGKTTFLRCLVNELKSN 372
Cdd:COG3267 37 YALAQGGGFVVLtGEVGTGKTTLLRRLLERLPDD 70
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-532 |
6.53e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 38.34 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 320 LEVNKLGHGFDGETLFSGGDFLLEAGAKLAVIGENGVGKTTFLRCLVNELKSNEGEIKWSENAT------------FGYC 387
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhararrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 388 PQDST-----KDFDNDLTLF----DWMSQWRTAKHNDLMVRGMLGRLlftaddSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:PRK10895 84 PQEASifrrlSVYDNLMAVLqirdDLSAEQREDRANELMEEFHIEHL------RDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180383029 459 VLVMDEPTNHMD---MEAIEALNNALKDFAGTLIFVSHDREFVSSLATRIIDIKDKQVIDfQGTFDEYLASIEEKKI 532
Cdd:PRK10895 158 FILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA-HGTPTEILQDEHVKRV 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-59 |
7.59e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 37.86 E-value: 7.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180383029 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS 59
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL 59
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-211 |
8.25e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.15 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 20 ISAKFGNGNRYGLIGANGCGKSTFMKILSGALVpsagnvsitpglkvgnlsqdqfAFEQYSVVDAVIMGDVELWKVKQER 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE----------------------EFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 100 DRIYSLPEmSEEDGMKVADLESVFAEMDGYTAES---RAEEILLEAGIdKEFHYGLMANVAPGWKLRVLLAQALFANPDI 176
Cdd:PRK13642 84 GMVFQNPD-NQFVGATVEDDVAFGMENQGIPREEmikRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1180383029 177 LLLDEPTNNLDI---HTITWLANEL-NKRKCTMIIISHD 211
Cdd:PRK13642 162 IILDESTSMLDPtgrQEIMRVIHEIkEKYQLTVLSITHD 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
149-209 |
8.30e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 8.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180383029 149 HYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIIS 209
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVgakFEIYQLIAELAKKDKGIIIIS 448
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
422-506 |
8.44e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 38.47 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180383029 422 LGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD------MEA-IEALNNALKDfagTLIFVSHD 494
Cdd:PRK11000 123 LAHLL------DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLHKRLGR---TMIYVTHD 193
|
90
....*....|..
gi 1180383029 495 REFVSSLATRII 506
Cdd:PRK11000 194 QVEAMTLADKIV 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
162-211 |
9.27e-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: 36.95 E-value: 9.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1180383029 162 LRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHD 211
Cdd:cd03227 88 LALILALASLKPRPLYILDEIDRGLDPrdgQALAEAILEHLVKGAQVIVITHL 140
|
|
| |
