|
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: 1100.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEFS 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDAVIMGDVELWKVKQERERIYSLPEMSEDDGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKF 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 241 LEAAGLQREQLLAENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDEVKSSSRMSPSLSFDEGKKMYRQAL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 321 EVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKDFDNDLT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 401 LFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNA 480
Cdd:PRK15064 401 LFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499648994 481 LKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGSFDEYLAS 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: 691.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEFSVVDAV 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 IMGDVELWKVKQERERIYSLPEMSEDDGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVL 165
Cdd:COG0488 83 LDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 166 LAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKFLEAAG 245
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 246 LQREQLLAENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDEVKsSSRMSPSLSFDEGKKMYRQALEVNKI 325
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPP-RRDKTVEIRFPPPERLGKKVLELEGL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 326 GHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDStKDFDNDLTLFDWM 405
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 406 SQWRTAKhNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQ 485
Cdd:COG0488 401 RDGAPGG-TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499648994 486 GTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGSFDEYLA 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 ... |
15-525 |
1.09e-80 |
|
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: 262.18 E-value: 1.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEFSVVDAVIMGDVELWK 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 95 VKQERERIYSLpeMSE-DDGM-----KVAELESVFAEMDGYTAESRAEeILLEAgidkefhygLM-----ANVAP---GW 160
Cdd:TIGR03719 99 ALDRFNEISAK--YAEpDADFdklaaEQAELQEIIDAADAWDLDSQLE-IAMDA---------LRcppwdADVTKlsgGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKF 240
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 241 LEaaglQREQLLAENAKKSAE----IDELQDFVNRfganASKAKQASSRAKkmdkIKLDEVKSSSRMSPSLSFDE----- 311
Cdd:TIGR03719 247 LE----QKQKRLEQEEKEESArqktLKRELEWVRQ----SPKGRQAKSKAR----LARYEELLSQEFQKRNETAEiyipp 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 312 GKKMYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQdS 391
Cdd:TIGR03719 315 GPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-S 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 392 TKDFDNDLTLFDWMSQwrtakHNDLMV--------RGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMD 463
Cdd:TIGR03719 394 RDALDPNKTVWEEISG-----GLDIIKlgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 464 EPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIK-DKQVIDFQGSFDEYLA 525
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEE 531
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-523 |
2.39e-80 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 263.57 E-value: 2.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEfS 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDAVIMGDVELWKVKQEreriysLPEMSE-DDGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANErNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEK 239
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 240 F--LEAAGLQREQLLAENakKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDeVKSSSRMSPSLSFDEGKKMYR 317
Cdd:PRK10636 234 FevQRATRLAQQQAMYES--QQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELI-APAHVDNPFHFSFRAPESLPN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 318 QALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKDFDN 397
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 DLTLFDWMSqwRTA-KHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEA 476
Cdd:PRK10636 391 DESPLQHLA--RLApQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499648994 477 LNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGSFDEY 523
Cdd:PRK10636 469 LTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-503 |
6.17e-76 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 251.79 E-value: 6.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEFS 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDAVIMGDVELWKVKQERERIYSLPEMSEDDGM--KVAELESVFAEMDGYTAESRAEEILLEAGIDKEfhyGLMANVAP 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYE 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 239 KFLEAaglqREQLLAENAKKSAEIDE--LQDFV------------NRFGANASKA--KQASSRAKKMDKIKLdevksssr 302
Cdd:PRK11147 240 QYLLE----KEEALRVEELQNAEFDRklAQEEVwirqgikarrtrNEGRVRALKAlrRERSERREVMGTAKM-------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 303 mspslSFDEGKKMYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENA 382
Cdd:PRK11147 308 -----QVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 383 TFGYCPQdSTKDFDNDLTLFDWMSQWRtakhNDLMVRG----MLGRL---LFtaddSNKKARN----CSGGEKNRLLFGK 451
Cdd:PRK11147 383 EVAYFDQ-HRAELDPEKTVMDNLAEGK----QEVMVNGrprhVLGYLqdfLF----HPKRAMTpvkaLSGGERNRLLLAR 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499648994 452 LMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLAT 503
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVT 505
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-532 |
6.89e-72 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 239.25 E-value: 6.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEFSVVDAVIMGDVELWK 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 95 VKQERERIYSlpEMSEDDGM------KVAELESVFAEMDGYTAESRAEeILLEAgidkefhygLM-----ANVAP---GW 160
Cdd:PRK11819 101 ALDRFNEIYA--AYAEPDADfdalaaEQGELQEIIDAADAWDLDSQLE-IAMDA---------LRcppwdAKVTKlsgGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKF 240
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 241 LEaaglQREQLLAENAKKSAE----IDELQDFVNrfgANAsKAKQASSRAKkmdkIKLDEVKSSSRMSPSLSFDE----- 311
Cdd:PRK11819 249 LE----QKAKRLAQEEKQEAArqkaLKRELEWVR---QSP-KARQAKSKAR----LARYEELLSEEYQKRNETNEifipp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 312 GKKMYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQdS 391
Cdd:PRK11819 317 GPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ-S 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 392 TKDFDNDLTLFDWMSQwrtakHNDLMV--------RGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMD 463
Cdd:PRK11819 396 RDALDPNKTVWEEISG-----GLDIIKvgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 464 EPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIK-DKQVIDFQGSFDEYlascEEKKV 532
Cdd:PRK11819 471 EPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEY----EEDKK 536
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-523 |
3.37e-63 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 219.35 E-value: 3.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILsgALVPSAGnvsITPGLKVGNLSQDQFAfEEFSV 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDG---IPKNCQILHVEQEVVG-DDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDAVIMGDVELWKVKQERERIYS----LPE--------MSEDDGMK----VAELESVFAEM---DGYTAESRAEEILLEA 142
Cdd:PLN03073 252 LQCVLNTDIERTQLLEEEAQLVAqqreLEFetetgkgkGANKDGVDkdavSQRLEEIYKRLeliDAYTAEARAASILAGL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 143 GIDKEFHYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHM 222
Cdd:PLN03073 332 SFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 223 ADIDYGELRIYPGNYEKFLEAaglQREQLlaENAKKSAEIDE-----LQDFVNRFGANASKAKQASSRAKKMDKIK-LDE 296
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERT---REEQL--KNQQKAFESNErsrshMQAFIDKFRYNAKRASLVQSRIKALDRLGhVDA 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 297 VKSSSRMSPSLSFDEGKKMyRQALEVNKIGHGF-DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGE 375
Cdd:PLN03073 487 VVNDPDYKFEFPTPDDRPG-PPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 376 VKWSENATFGYCPQDSTKDFDNDLTLFDWMSQ-WRTAKHNDLmvRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMM 454
Cdd:PLN03073 566 VFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRcFPGVPEQKL--RAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 455 QDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGSFDEY 523
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-512 |
3.86e-49 |
|
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: 166.08 E-value: 3.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQdstkdfdndl 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 tlfdwmsqwrtakhndlmvrgmlgrlLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNN 479
Cdd:cd03221 71 --------------------------L-------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 499648994 480 ALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQ 512
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-529 |
2.25e-46 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 169.48 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 322 VNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDStkDFDNDLTL 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP--PLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 402 FDW-----------MSQWRTAKHN------DLM--------------------VRGMLGRLLFTADDSNKKARNCSGGEK 444
Cdd:COG0488 79 LDTvldgdaelralEAELEELEAKlaepdeDLErlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 445 NRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGSFDEYL 524
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
....*
gi 499648994 525 ASCEE 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 |
2.14e-43 |
|
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: 150.68 E-value: 2.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQdqfafeefsvvdav 85
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 imgdvelwkvkqereriyslpeMSeddgmkvaelesvfaemdgytaesraeeilleagidkefhyglmanvaPGWKLRVL 165
Cdd:cd03221 71 ----------------------LS------------------------------------------------GGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 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 |
1.62e-31 |
|
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: 119.81 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafEEFSV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV----------------LGKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDavimgdvelwKVKQERERIYSLPE-MSEDDGMKVAELesvfaemdgytaesraeeilleagidkeFHYGLmanvapGW 160
Cdd:cd03230 65 KK----------EPEEVKRRIGYLPEePSLYENLTVREN----------------------------LKLSG------GM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 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 |
1.34e-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: 116.50 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpgLKVGNLSQDQFAFEEFS 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI---DGEDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDavimGDVELWkvkqereriyslpemsedDGMKVAELESVFAE---MDGYTAESRAEEILLEAGIDKEFHYGLMaNVA 157
Cdd:COG4555 78 VLP----DERGLY------------------DRLTVRENIRYFAElygLFDEELKKRIEELIELLGLEEFLDRRVG-ELS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELrIYP 234
Cdd:COG4555 135 TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQ 213
|
250
....*....|....
gi 499648994 235 GNYEKFLEAAGLQR 248
Cdd:COG4555 214 GSLDELREEIGEEN 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
1.41e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 116.32 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQfafeefsv 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-GEDVARDPAEV-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgdvelwkvkqeRERIYSLPEMSE-DDGMKVAELESVFAE---MDGYTAESRAEEIL----LEAGIDKEF-HYGL 152
Cdd:COG1131 72 -----------------RRRIGYVPQEPAlYPDLTVRENLRFFARlygLPRKEARERIDELLelfgLTDAADRKVgTLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 153 manvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:COG1131 135 ------GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEllrELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
.
gi 499648994 230 L 230
Cdd:COG1131 209 I 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
1.02e-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: 112.96 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpgLKVGNLSQDQFAFeefs 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRDAREDY---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvdavimgdvelwkvkqeRERIYSLPemsEDDGMK----VAELESVFAEMDGY-TAESRAEEIL----LEAGIDKEFHYg 151
Cdd:COG4133 74 ------------------RRRLAYLG---HADGLKpeltVRENLRFWAALYGLrADREAIDEALeavgLAGLADLPVRQ- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 152 LMAnvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRKCTMIII-SHDRHFLNSV 218
Cdd:COG4133 132 LSA----GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAahLARGGAVLLtTHQPLELAAA 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-229 |
1.06e-27 |
|
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: 108.49 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGlkvgnlsqdqfafeefsvvdav 85
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK---------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 imgDVELWKVKQERERIYSLPEMSeddgmkvaelesvfaemdgytaesraeeilleagidkefhyglmanvaPGWKLRVL 165
Cdd:cd00267 62 ---DIAKLPLEELRRRIGYVPQLS------------------------------------------------GGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 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 |
3.14e-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: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI------TPGLKVGNLSQdQF 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 75 AFEE---FSVVDAVIMGdveLWKvkqeRERIYSLPemSEDDGMKVAE-LESVfaEMDGYtaesraeeilleagIDKEFHy 150
Cdd:COG1121 85 EVDWdfpITVRDVVLMG---RYG----RRGLFRRP--SRADREAVDEaLERV--GLEDL--------------ADRPIG- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 151 glmanvapgwKL------RVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTH 221
Cdd:COG1121 139 ----------ELsggqqqRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYFDR 208
|
250 260
....*....|....*....|....*..
gi 499648994 222 MADIDYGelRIYPGNYEKFLEAAGLQR 248
Cdd:COG1121 209 VLLLNRG--LVAHGPPEEVLTPENLSR 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-526 |
3.50e-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: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW------SENATFGYCPQDST 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 393 kdFDND--LTLFDWMSQWRTAKhndlmvRGMLGRLlfTADDsNKKARNC-----------------SGGEKNRLLFGKLM 453
Cdd:COG1121 86 --VDWDfpITVRDVVLMGRYGR------RGLFRRP--SRAD-REAVDEAlervgledladrpigelSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 454 MQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRIIDIKDKQVidFQGSFDEYLAS 526
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-506 |
1.05e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 113.46 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQF--GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVSitpglkvGNLsqdqfafeE 78
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIS-------GEV--------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 79 FSVVDAVIMGDVELWK----VKQEreriyslPeMSEDDGMKVAElESVFA----EMDGYTAESRAEEILLEAGIDKEFHY 150
Cdd:COG1123 68 LDGRDLLELSEALRGRrigmVFQD-------P-MTQLNPVTVGD-QIAEAlenlGLSRAEARARVLELLEAVGLERRLDR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 151 GLmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDRHFLNSVCTHMADID 226
Cdd:COG1123 139 YP-HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 227 YGELRiypgnyEKFLEAAGLQREQLLAEnakksaeidelqdfVNRFGANASKAKQASSRAKKMdkIKLDEVKsssrmsps 306
Cdd:COG1123 218 DGRIV------EDGPPEEILAAPQALAA--------------VPRLGAARGRAAPAAAAAEPL--LEVRNLS-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 307 LSFDEGKKMYRQALEvnkighgfdgemlfsGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KW 378
Cdd:COG1123 268 KRYPVRGKGGVRAVD---------------DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltKL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 379 SENAT------FGYCPQDSTKDFDNDLTLFDWMSQ------WRTAKHNDLMVRGMLGRLLFTADDSNKKARNCSGGEKNR 446
Cdd:COG1123 333 SRRSLrelrrrVQMVFQDPYSSLNPRMTVGDIIAEplrlhgLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQR 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 447 LLFGKLMMQDVNVLVMDEPTNHMD-------MEAIEALNnalKDFQGTLIFVSHDREFVSSLATRII 506
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQ---RELGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-221 |
9.59e-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: 104.92 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITP------GLKVGNLSQdQFAFE-E 78
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQ-RRSIDrD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 79 F--SVVDAVIMGdveLWKvkqereRIYSLPEMSEDDgmkvaelesvfaemdgytaESRAEEILLEAGIdKEFHYGLMANV 156
Cdd:cd03235 83 FpiSVRDVVLMG---LYG------HKGLFRRLSKAD-------------------KAKVDEALERVGL-SELADRQIGEL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 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 |
1.17e-25 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 105.90 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TP--GL-------KVGNL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgRDlaSLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 70 SQDQFAFEEFSVVDAVIMGdvelwkvkqereRI-Y--SLPEMSEDDgmkvaelesvfaemdgytaESRAEEILLEAGI-- 144
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG------------RYpHlgLFGRPSAED-------------------REAVEEALERTGLeh 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 145 --DKEFHyglmanvapgwKL------RVLLAQALFANPDILLLDEPTNNLDI-HTITWLA--NELNK-RKCTMIIISHDr 212
Cdd:COG1120 130 laDRPVD-----------ELsggerqRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLEllRRLAReRGRTVVMVLHD- 197
|
250
....*....|....
gi 499648994 213 hfLN---SVCTHMA 223
Cdd:COG1120 198 --LNlaaRYADRLV 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-529 |
1.07e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 108.11 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKDFDNdlTLFDWMSQW---------- 408
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEG--TVYDFVAEGieeqaeylkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 409 ------------------RTAK------HNDL-----MVRGMLGRLLFTADdsnKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:PRK11147 101 yhdishlvetdpseknlnELAKlqeqldHHNLwqlenRINEVLAQLGLDPD---AALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 460 LVMDEPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFQGSFDEYLASCEE 529
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEE 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-249 |
1.58e-24 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 102.03 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----TPGLKVGNLSQ----------DQFaFE 77
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRRkvglvfqnpdDQL-FA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 78 EfSVVDAVIMGdvelwkvkqereriyslPE---MSEDDgmkvaelesvfaemdgytAESRAEEILLEAGIDKefhyglMA 154
Cdd:COG1122 91 P-TVEEDVAFG-----------------PEnlgLPREE------------------IRERVEEALELVGLEH------LA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 155 NVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLA---NELNKRKCTMIIISHDRHFLNSVCTHMADID 226
Cdd:COG1122 129 DRPPhelsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLellKRLNKEGKTVIIVTHDLDLVAELADRVIVLD 208
|
250 260
....*....|....*....|...
gi 499648994 227 YGELrIYPGNYEKFLEAAGLQRE 249
Cdd:COG1122 209 DGRI-VADGTPREVFSDYELLEE 230
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-297 |
1.02e-23 |
|
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: 94.95 E-value: 1.02e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 223 ADIDYGELRIYPGNYEKFLEAAGLQREQLLAENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDEV 297
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEK 75
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
1.28e-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: 98.69 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsQDQfafeefsvvdavimgDVE 91
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----------DGK---------------DLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 92 LWKVKQERERIYSLPEMSEDD--GMKVAElESVFA----EMDGYTAESRAEEILLEAGIDKefhyglMANVAP-----GW 160
Cdd:cd03225 67 KLSLKELRRKVGLVFQNPDDQffGPTVEE-EVAFGlenlGLPEEEIEERVEEALELVGLEG------LRDRSPftlsgGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:cd03225 140 KQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-514 |
7.49e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 97.81 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KWSENA---TFGYC 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 388 PQDSTKDFDndLTLFD--------WMSQWRTAKHNDL-MVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:COG1120 81 PQEPPAPFG--LTVRElvalgrypHLGLFGRPSAEDReAVEEAL-ERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 459 VLVMDEPTNHMD-------MEAIEALNnalKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:COG1120 158 LLLLDEPTSHLDlahqlevLELLRRLA---RERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
328-506 |
1.30e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 96.06 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 328 GFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK------WSENATFGYCPQDSTKDFDNDLTL 401
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSIDRDFPISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 402 FD----------WMSQWRTAKHNDLmVRGMLGRL-LFtaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:cd03235 88 RDvvlmglyghkGLFRRLSKADKAK-VDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 499648994 471 MEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRII 506
Cdd:cd03235 165 PKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVL 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-247 |
2.26e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 100.35 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAfeEFsvvdav 85
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAY--DF------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 imgdvelwkvkqereriyslpemsEDDgmkvaelESVFAEMDGYTAESRAEEI-------LLEAG--IDKEfhyglMANV 156
Cdd:PRK15064 396 ------------------------END-------LTLFDWMSQWRQEGDDEQAvrgtlgrLLFSQddIKKS-----VKVL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 157 APGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGN 236
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGT 519
|
250
....*....|.
gi 499648994 237 YEKFLEAAGLQ 247
Cdd:PRK15064 520 YEEYLRSQGIE 530
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
2.72e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 96.03 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGA----EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAf 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD-GRPVTRRRRKAFR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 77 eefsvvdavimGDVELwkVKQEreriyslPEMSEDDGMKVAE-LESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMAN 155
Cdd:COG1124 79 -----------RRVQM--VFQD-------PYASLHPRHTVDRiLAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK----RKCTMIIISHDRhflnSVCTHMAD 224
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDlreeRGLTYLFVSHDL----AVVAHLCD 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-232 |
4.82e-22 |
|
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: 94.21 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSqdqfafEEFSV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD-GKSYQKNI------EALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDAVImgdvelwkvkqERERIYslPEMSEDDGMKVAELESVFAEmdgytaeSRAEEILLEAGIDKEFH-----YGLmanv 156
Cdd:cd03268 74 IGALI-----------EAPGFY--PNLTARENLRLLARLLGIRK-------KRIDEVLDVVGLKDSAKkkvkgFSL---- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 157 apGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRI 232
Cdd:cd03268 130 --GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
5.36e-22 |
|
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: 94.81 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 -------FEEFSVVDAVIMGdVELwkvkQERERIYSLPEMSEDDgmkvaelesvfaemdgyTAESRAEEILLEAGIDKEF 148
Cdd:cd03219 80 tfqiprlFPELTVLENVMVA-AQA----RTGSGLLLARARREER-----------------EARERAEELLERVGLADLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 149 HYgLMANVAPGWKLRVLLAQALFANPDILLLDEPT---NNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADI 225
Cdd:cd03219 138 DR-PAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
....*
gi 499648994 226 DYGEL 230
Cdd:cd03219 217 DQGRV 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-510 |
7.14e-22 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 92.31 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 321 EVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKDFdndlt 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 401 lfdwmsqwrtakhndlmvrGMLGRLlftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNA 480
Cdd:cd00267 76 -------------------GYVPQL--------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|...
gi 499648994 481 LKDFQG---TLIFVSHDREFVSSLATRIIDIKD 510
Cdd:cd00267 123 LRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-513 |
1.61e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 91.69 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW-----SENAT-----FGYCPQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdiKKEPEevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 DSTkdfdndltLFDWMSqwrtakhndlmVRGMLgrllftaddsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHM 469
Cdd:cd03230 81 EPS--------LYENLT-----------VRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499648994 470 DMEAIEALNNALKDF---QGTLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:cd03230 127 DPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-522 |
1.99e-21 |
|
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: 93.38 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWsenatFGYCPQDSTKDFDNDL 399
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-----DGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 T-------LFDWMsqwrTAKHNDLMV---RGMLGRLLFTA-----------DDSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:COG4555 77 GvlpdergLYDRL----TVRENIRYFaelYGLFDEELKKRieeliellgleEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 459 VLVMDEPTNHMDMEAIEALNN---ALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGSFDE 522
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDE 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-515 |
2.79e-21 |
|
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: 97.18 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG--ALVPSAG----NVSITPglKVGNLSQDQFA 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyHVALCE--KCGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 FEEFSVVDAVI-MGDVELWKV-----KQERERIYSLPE----MSEDDGMKVAELESVfaEMDGYTAES---RAEEILLEA 142
Cdd:TIGR03269 79 GEPCPVCGGTLePEEVDFWNLsdklrRRIRKRIAIMLQrtfaLYGDDTVLDNVLEAL--EEIGYEGKEavgRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 143 GIDKEFHYgLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHDRHFLNSV 218
Cdd:TIGR03269 157 QLSHRITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 219 CTHMADIDYGELriypgnyekfleaaglqreqllaenaKKSAEIDELqdfVNRFGANASKAKQASSRAKKMDKIKLDEVK 298
Cdd:TIGR03269 236 SDKAIWLENGEI--------------------------KEEGTPDEV---VAVFMEGVSEVEKECEVEVGEPIIKVRNVS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 299 sssrmSPSLSFDEG--KKMYRQALEVnkighgFDGEMlfsggdllleagakLAVIGENGVGKTTFLRCLVDELKSLEGEV 376
Cdd:TIGR03269 287 -----KRYISVDRGvvKAVDNVSLEV------KEGEI--------------FGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 377 ------KWSENATFGYCPQDSTKDFDNDL----------TLFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSNKKARNC- 439
Cdd:TIGR03269 342 nvrvgdEWVDMTKPGPDGRGRAKRYIGILhqeydlyphrTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEIl 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 -------SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDI 508
Cdd:TIGR03269 422 dkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
....*..
gi 499648994 509 KDKQVID 515
Cdd:TIGR03269 502 RDGKIVK 508
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-230 |
4.09e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.42 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvGNLSQDQFafeefsv 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL------DGKPLSAM------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgDVELWkvkqeRERIYSLPEMSEDDGMKVAE-LESVFAEMDGYTAESRAEEILLEAGIDKEFhygLMANVAP-- 158
Cdd:COG4619 68 -------PPPEW-----RRQVAYVPQEPALWGGTVRDnLPFPFQLRERKFDRERALELLERLGLPPDI---LDKPVERls 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 159 -GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:COG4619 133 gGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-242 |
4.49e-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: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVG-------NLSQDQF 74
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAyvdqsrdALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 75 AFEEFSV-VDAVIMGDVELwkvkQERERIYSLPEMSEDDGMKVAELESvfaemdgytaesraeeilleagidkefhyglm 153
Cdd:TIGR03719 403 VWEEISGgLDIIKLGKREI----PSRAYVGRFNFKGSDQQKKVGQLSG-------------------------------- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 154 anvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFLNSVCTH-MADIDYGELRI 232
Cdd:TIGR03719 447 -----GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHiLAFEGDSHVEW 521
|
250
....*....|
gi 499648994 233 YPGNYEKFLE 242
Cdd:TIGR03719 522 FEGNFSEYEE 531
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
7.04e-21 |
|
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: 89.97 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFG--AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeef 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 sVVDAVimgDVELWKVKQERERIYSLPEmseDDgmkvaELesvfaeMDGytaeSRAEEILleAGidkefhyglmanvapG 159
Cdd:cd03246 60 -RLDGA---DISQWDPNELGDHVGYLPQ---DD-----EL------FSG----SIAENIL--SG---------------G 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSV 218
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAHRPETLASA 162
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-216 |
1.29e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 95.21 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEEFSVV--DAVIM-G 88
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPASWR-RQIAWVpqNPYLFaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 89 DVelwkvkqeRE--RIYSlPEMSEDDGMKVAE---LESVFAEM-DGYtaesraEEILLEAGidkefhyglmANVAPGWKL 162
Cdd:COG4988 426 TI--------REnlRLGR-PDASDEELEAALEaagLDEFVAALpDGL------DTPLGEGG----------RGLSGGQAQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 163 RVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRHFLN 216
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLALLA 536
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
1.54e-20 |
|
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: 91.25 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA----- 75
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 --------FEEFSVVDAVIMGdvelwkvKQERERIYSLPEMSEDDGMKVAELEsvfaemdgytAESRAEEILLEAGIDKE 147
Cdd:COG0411 83 rtfqnprlFPELTVLENVLVA-------AHARLGRGLLAALLRLPRARREERE----------ARERAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 148 FHYgLMANVAPGWKLRVLLAQALFANPDILLLDEPT---NNLDIHTITWLANELNK-RKCTMIIISHDRHFLNSVCTHMA 223
Cdd:COG0411 146 ADE-PAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIV 224
|
....*..
gi 499648994 224 DIDYGEL 230
Cdd:COG0411 225 VLDFGRV 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-251 |
1.86e-20 |
|
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: 95.29 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS------------QDQFAFEEf 79
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-GIDLRQIDpaslrrqigvvlQDVFLFSG- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 SVVDAVIMGDvelwkvkqereriyslPEMSEDDGMKVAE---LESVFAEM-DGYtaesraEEILLEAGidkefhyglmAN 155
Cdd:COG2274 564 TIRENITLGD----------------PDATDEEIIEAARlagLHDFIEALpMGY------DTVVGEGG----------SN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRHFLNsvcthMAD----IDYGE 229
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIR-----LADriivLDKGR 686
|
250 260
....*....|....*....|....*.
gi 499648994 230 LrIYPGNYEKFLEAAG----LQREQL 251
Cdd:COG2274 687 I-VEDGTHEELLARKGlyaeLVQQQL 711
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
1.96e-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: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFG----AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQfaf 76
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLLSGKE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 77 eefsvvdavimgdvelwkVKQERERIyslpemseddGM-----------KVAE-----LEsvFAEMDGYTAESRAEEILL 140
Cdd:cd03258 77 ------------------LRKARRRI----------GMifqhfnllssrTVFEnvalpLE--IAGVPKAEIEERVLELLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 141 EAGI-DKEFHYglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFL 215
Cdd:cd03258 127 LVGLeDKADAY--PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRElGLTIVLITHEMEVV 204
|
250
....*....|....*
gi 499648994 216 NSVCTHMADIDYGEL 230
Cdd:cd03258 205 KRICDRVAVMEKGEV 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
2.36e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 11 FGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQ-----DQFAFeefSVVDAV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPL---TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 IMGdveLWkvkqeRERIYSLPemseddgmkvaelesvfaemdgYTAESRA--EEILLEAGIDkEFHYGLMANVAPGWKLR 163
Cdd:NF040873 79 AMG---RW-----ARRGLWRR----------------------LTRDDRAavDDALERVGLA-DLAGRQLGELSGGQRQR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRH 213
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDAESrerIIALLAEEHARGATVVVVTHDLE 180
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
2.73e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 328 GFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKDFDNDLTLFDWMSQ 407
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 408 WRTAKhndlmvRGMLGRLlfTADD----------------SNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:NF040873 81 GRWAR------RGLWRRL--TRDDraavddalervgladlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 499648994 472 EAIEALNNALKDFQG---TLIFVSHDREFVSSlATRII 506
Cdd:NF040873 153 ESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCV 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-224 |
3.67e-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: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEP-LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefsvvda 84
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL------------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 85 vimgDVELWKVKQERERIYSLPEMSEDdgmkvaEL--ESVFAE-----MDGYTAESRAEEILLEAGID--KEFHyglman 155
Cdd:cd03226 60 ----NGKPIKAKERRKSIGYVMQDVDY------QLftDSVREElllglKELDAGNEQAETVLKDLDLYalKERH------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 156 vaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRKCTMIIISHDRHFLNSVCT---HMAD 224
Cdd:cd03226 124 --PlslsgGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmeRVGELIRELAAQGKAVIVITHDYEFLAKVCDrvlLLAN 201
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-522 |
7.92e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.58 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK------WSENAT----FGYCPQDSTkdFDNDLT---LFDWM 405
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVPQEPA--LYPDLTvreNLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 406 SQWR--TAKHNDLMVRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALK 482
Cdd:COG1131 98 ARLYglPRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499648994 483 DF--QGTLIFVS-HDREFVSSLATRIIDIKDKQVIdFQGSFDE 522
Cdd:COG1131 176 ELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRIV-ADGTPDE 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-514 |
1.03e-19 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 86.72 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 321 EVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWsenatfgycpqdstkdfdNDLT 400
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------------DGKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 401 LFDWMSQWRtAKHndlmvRGMLGRLLFTADDSNKKARNC---SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD------- 470
Cdd:cd03214 63 LASLSPKEL-ARK-----IAYVPQALELLGLAHLADRPFnelSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqiel 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499648994 471 MEAIEALNnalKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03214 137 LELLRRLA---RERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-514 |
1.36e-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: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSEN--------ATFGYCPQDSTKDFDNDlTLFDWMSQWRT 410
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDVDYQLFTD-SVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 411 AKHNDLM-VRGMLGRL-LFTADDsnKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF--QG 486
Cdd:cd03226 99 ELDAGNEqAETVLKDLdLYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELaaQG 176
|
170 180
....*....|....*....|....*....
gi 499648994 487 TLIFV-SHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03226 177 KAVIViTHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-211 |
3.19e-19 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 85.18 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefsvvdav 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 iMG-DVELWKVKQERERIYSLPEMSEDdgMKVAEL-ESVFAEMDGytaesraeeilleagidkefhyglmanvapGWKLR 163
Cdd:cd03214 59 -DGkDLASLSPKELARKIAYVPQALEL--LGLAHLaDRPFNELSG------------------------------GERQR 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLDIH----TITWLANELNKRKCTMIIISHD 211
Cdd:cd03214 106 VLLARALAQEPPILLLDEPTSHLDIAhqieLLELLRRLARERGKTVVMVLHD 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-506 |
7.19e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.87 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITPG----LKV--GNLSQDQFAfeefsvvdAVIMGDVelwKVKQERERIYS 104
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevLKRfrGTELQNYFK--------KLYNGEI---KVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 105 LPEMSedDGmKVAEL------ESVFAEMdgytaesrAEEILLEAGIDKEFhyglmaNVAPGWKL-RVLLAQALFANPDIL 177
Cdd:PRK13409 172 IPKVF--KG-KVRELlkkvdeRGKLDEV--------VERLGLENILDRDI------SELSGGELqRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 178 LLDEPTNNLDIH---TITWLANELNKRKcTMIIISHDRHFLNsvctHMAD---IDYGElriyPGNYEKFLEAAGLQ---- 247
Cdd:PRK13409 235 FFDEPTSYLDIRqrlNVARLIRELAEGK-YVLVVEHDLAVLD----YLADnvhIAYGE----PGAYGVVSKPKGVRvgin 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 248 ---REQLLAENAkksaeidelqdfvnRFGANASKAKQASSRAKKMDKIKLDevksssrmspslsFDEGKKMYRQ-ALEVN 323
Cdd:PRK13409 306 eylKGYLPEENM--------------RIRPEPIEFEERPPRDESERETLVE-------------YPDLTKKLGDfSLEVE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 324 KiGHGFDGEMLfsggdllleagaklAVIGENGVGKTTFLRCLVDELKSLEGEVKWSEnaTFGYCPQDSTKDFdnDLTLFD 403
Cdd:PRK13409 359 G-GEIYEGEVI--------------GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--KISYKPQYIKPDY--DGTVED 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 404 WMSQWRTAKH-----NDLMVRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME----AI 474
Cdd:PRK13409 420 LLRSITDDLGssyykSEIIKPLQLERLL------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVA 493
|
490 500 510
....*....|....*....|....*....|..
gi 499648994 475 EALNNALKDFQGTLIFVSHDREFVSSLATRII 506
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
1.69e-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: 82.31 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 17 FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsQDQfafeefsvvdavimgDVELWKVK 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL----------DGQ---------------DLTDDERK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 97 QERERIYSLP-EMSEDDGMKVAE---LESVFAEMDGYTAESRAEEILLEAGI---DKEFHYGLMANVAPGWKLRVLLAQA 169
Cdd:pfam00005 56 SLRKEIGYVFqDPQLFPRLTVREnlrLGLLLKGLSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARA 135
|
170
....*....|....*
gi 499648994 170 LFANPDILLLDEPTN 184
Cdd:pfam00005 136 LLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
2.08e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.32 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFG----AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAf 76
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERELA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 77 eefsvvdavimgdvELWkvkqeRERI-------YSLPEMSeddgmkVAE---LESVFAEMDGYTAESRAEEILLEAGI-D 145
Cdd:COG1136 82 --------------RLR-----RRHIgfvfqffNLLPELT------ALEnvaLPLLLAGVSRKERRERARELLERVGLgD 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 146 KEFHYglmanvaPGwKL------RVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRK-CTMIIISHDRH 213
Cdd:COG1136 137 RLDHR-------PS-QLsggqqqRVAIARALVNRPKLILADEPTGNLDSKTgeeVLELLRELNRELgTTIVMVTHDPE 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-512 |
3.43e-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: 83.29 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 321 EVNKIGHGFDG--EMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKD---- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 395 FDN-D-----LTLFD----WMSQWRTAKHNDLM-VRGMLGRLlftaDDSNKKARNC---SGGEKNRLLFGKLMMQDVNVL 460
Cdd:cd03225 81 FQNpDdqffgPTVEEevafGLENLGLPEEEIEErVEEALELV----GLEGLRDRSPftlSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 461 VMDEPTNHMDMEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRIIDIKDKQ 512
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
3.99e-18 |
|
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: 82.95 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefsvvdav 85
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 imGDVELWKVKQERERI------YSL-PEMSEDD----GMKVaelesvfAEMDGYTAESRAEEILLEAGID---KEFHYG 151
Cdd:cd03259 60 --DGRDVTGVPPERRNIgmvfqdYALfPHLTVAEniafGLKL-------RGVPKAEIRARVRELLELVGLEgllNRYPHE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 152 LMAnvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHDR 212
Cdd:cd03259 131 LSG----GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELkelqRELGITTIYVTHDQ 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-289 |
4.50e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 87.70 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFE-EFSVVDA 84
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDpEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 85 VIMGdvelwkvKQEreriyslpemseddgmkvaelesvfAEMDGytaesRAEEILleaGIDKEFHYGLMANVAP------ 158
Cdd:PRK11147 404 LAEG-------KQE-------------------------VMVNG-----RPRHVL---GYLQDFLFHPKRAMTPvkalsg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 GWKLRVLLAQaLFANP-DILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHDRHFL-NSVCTHMADIDYGELRIYPGN 236
Cdd:PRK11147 444 GERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGG 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 237 YEKfleaAGLQREQLLAENAKKSAEIDElqdfvnrfgANASKAKQASSRAKKM 289
Cdd:PRK11147 523 YHD----ARQQQAQYLALKQPAVKKKEE---------AAAPKAETVKRSSKKL 562
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
5.01e-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: 82.92 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAE----PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ---- 73
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 74 ------FAFEEFSVvdavimgdvelwkvkqereriysLPEMSEDDGmkvAELESVFAEMDGYTAESRAEEILLEAGIDKE 147
Cdd:cd03255 80 rrrhigFVFQSFNL-----------------------LPDLTALEN---VELPLLLAGVPKKERRERAEELLERVGLGDR 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 148 FHY------GlmanvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDR 212
Cdd:cd03255 134 LNHypselsG-------GQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNKeAGTTIVVVTHDP 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-506 |
5.80e-18 |
|
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: 87.15 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITPG----LKV--GNLSQDQFAfeefsvvdAVIMGDVelwKVKQERERIYS 104
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevLKRfrGTELQDYFK--------KLANGEI---KVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 105 LPEMSedDGmKVAELesvfaeMDGYTAESRAEEIL----LEAGIDKEfhyglMANVAPGWKLRVLLAQALFANPDILLLD 180
Cdd:COG1245 172 IPKVF--KG-TVREL------LEKVDERGKLDELAeklgLENILDRD-----ISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 181 EPTNNLDIH---TITWLANELNKRKCTMIIISHDRHFLNsvctHMAD---IDYGElriyPGNY-------------EKFL 241
Cdd:COG1245 238 EPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILD----YLADyvhILYGE----PGVYgvvskpksvrvgiNQYL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 242 EAaglqreQLLAENAkksaeidelqdfvnRFGANASKAKQASSRAKKMDKIKLDevksssrmspslsFDEGKKMYRQ-AL 320
Cdd:COG1245 310 DG------YLPEENV--------------RIRDEPIEFEVHAPRREKEEETLVE-------------YPDLTKSYGGfSL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 321 EVNkighgfdgemlfsGGDLllEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwSENATFGYCPQDSTKDFdnDLT 400
Cdd:COG1245 357 EVE-------------GGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDY--DGT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 401 LFDWMSQWRTAK------HNDLMVRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD---- 470
Cdd:COG1245 418 VEEFLRSANTDDfgssyyKTEIIKPLGLEKLL------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqr 491
|
490 500 510
....*....|....*....|....*....|....*.
gi 499648994 471 MEAIEALNNALKDFQGTLIFVSHDREFVSSLATRII 506
Cdd:COG1245 492 LAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-235 |
6.64e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.15 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkVGNLSQDQFafEEFSVVDAVIMGdvelwkvkQE 98
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-----AGLVPWKRR--KKFLRRIGVVFG--------QK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 99 RERIYSLPemseddgmkVAELESVFAEM---DGYTAESRAEEI--LLEAGidkEFHYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:cd03267 104 TQLWWDLP---------VIDSFYLLAAIydlPPARFKKRLDELseLLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 174 PDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDRHFLNSVCTHMADIDYGELrIYPG 235
Cdd:cd03267 172 PEILFLDEPTIGLDVVAqenIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
1.71e-17 |
|
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: 81.14 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPL-FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAFEEF 79
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAaLHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIA-GEDVNRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 SVvdAVIMGDVELwkvkqereriysLPEMSeddgmkVAELESVFAEMDGYTA---ESRAEEILLEAGI-DKEFHYGLmaN 155
Cdd:TIGR02673 80 RI--GVVFQDFRL------------LPDRT------VYENVALPLEVRGKKEreiQRRVGAALRQVGLeHKADAFPE--Q 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRH 213
Cdd:TIGR02673 138 LSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLserILDLLKRLNKRGTTVIVATHDLS 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
1.88e-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: 81.36 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAE----PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI------TPGLKVGNLSQ 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 72 DQFAFEEFSVVDAVIMGdvelwkvkqereriyslPEMSeddGMKVAElesvfaemdgytAESRAEEILLEAGIDK-EFHY 150
Cdd:cd03293 81 QDALLPWLTVLDNVALG-----------------LELQ---GVPKAE------------ARERAEELLELVGLSGfENAY 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 151 glmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIISHD 211
Cdd:cd03293 129 -------PhqlsgGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
2.09e-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: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpgLKVgnlsqdqfaF-EEF 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGND-----VRL---------FgERR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 svvdavimGDVELWKVKQereRI-YSLPEMSED--DGMKVAE-----LESVFAEMDGYTAE--SRAEEILLEAGI----D 145
Cdd:COG1119 69 --------GGEDVWELRK---RIgLVSPALQLRfpRDETVLDvvlsgFFDSIGLYREPTDEqrERARELLELLGLahlaD 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 146 KEFHyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH-------TITWLANElnkRKCTMIIISH 210
Cdd:COG1119 138 RPFG-----TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGarelllaLLDKLAAE---GAPTLVLVTH 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
2.74e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.87 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAE-PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA---- 75
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 -----FEEFsvvdavimgdvelwkvkqereRIysLPEMSeddgmkVAE-----LEsvFAEMDGYTAESRAEEILLEAGI- 144
Cdd:COG2884 80 rigvvFQDF---------------------RL--LPDRT------VYEnvalpLR--VTGKSRKEIRRRVREVLDLVGLs 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 145 DKEFHYglmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLN 216
Cdd:COG2884 129 DKAKAL-------PhelsgGEQQRVAIARALVNRPELLLADEPTGNLDPETsweIMELLEEINRRGTTVLIATHDLELVD 201
|
.
gi 499648994 217 S 217
Cdd:COG2884 202 R 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
3.67e-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: 80.62 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQD--------- 72
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAelyrlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 ----QFA--FEEFSVVDavimgDVELWkvkqereriysLPEMSEDDgmkvaelESVFAEmdgytaesRAEEILLEAGIdK 146
Cdd:cd03261 80 gmlfQSGalFDSLTVFE-----NVAFP-----------LREHTRLS-------EEEIRE--------IVLEKLEAVGL-R 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 147 EFHYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-IHT--ITWLANELNKRKC-TMIIISHDRHFLNSVCTHM 222
Cdd:cd03261 128 GAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpIASgvIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRI 207
|
....*...
gi 499648994 223 ADIDYGEL 230
Cdd:cd03261 208 AVLYDGKI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
4.22e-17 |
|
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: 79.93 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGnRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeEFSV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-------------------RIDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDAVIMGDvELwkvkqeRERIYSLP-EMSEDDGMKVAELESVFA---EMDGYTAESRAEEILLEAGIDkEFHYGLMANVA 157
Cdd:cd03264 61 QDVLKQPQ-KL------RRRIGYLPqEFGVYPNFTVREFLDYIAwlkGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 158 PGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCtmIIIS-HDRHFLNSVCTHMADIDYGELR 231
Cdd:cd03264 133 GGMRRRVGIAQALVGDPSILIVDEPTAGLDPeerIRFRNLLSELGEDRI--VILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
334-513 |
6.62e-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: 78.41 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 334 LFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KWSENA---TFGYCPQDstkdfdndLTLF 402
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGYLPQD--------DELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 403 DwmsqwRTAKHNDLmvrgmlgrllftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALK 482
Cdd:cd03246 89 S-----GSIAENIL-----------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....
gi 499648994 483 DFQ---GTLIFVSHDREFVSSlATRIIDIKDKQV 513
Cdd:cd03246 141 ALKaagATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-230 |
7.28e-17 |
|
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: 83.41 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfeefsvvdavimgdvELWKVKQ 97
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-GKDLTKLSRRSLR---------------ELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 98 ereRIYSLPEMSEDDGMKVAE-----LEsVFAEMDGYTAESRAEEILLEAGIDKEFhyglmANVAP-----GWKLRVLLA 167
Cdd:COG1123 346 ---MVFQDPYSSLNPRMTVGDiiaepLR-LHGLLSRAERRERVAELLERVGLPPDL-----ADRYPhelsgGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 168 QALFANPDILLLDEPTNNLDIHTITWLAN---ELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNllrDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
7.33e-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: 79.92 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG-----ALVPSAGNVSITPG------------- 63
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 64 LKVGNLSQDQFAFEeFSVVDAVIMGDvelwKVKQERERiyslpemseddgmkvaelesvfAEMDGytaesRAEEILLEAG 143
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL----RLHGIKLK----------------------EELDE-----RVEEALRKAA 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 144 IDKEFHYGLMA-NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISHD 211
Cdd:cd03260 129 LWDEVKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIStakIEELIAELKKEY-TIVIVTHN 199
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
342-467 |
1.12e-16 |
|
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: 76.92 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW-----------SENATFGYCPQDSTkdFDNDLT---------- 400
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQ--LFPRLTvrenlrlgll 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 401 LFDWMSQWRTAKHNDLMVRgmLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTN 467
Cdd:pfam00005 86 LKGLSKREKDARAEEALEK--LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
1.16e-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: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAE----PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT------PGLKVGnls 70
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 71 qdqFAFEEF------SVVDAVIMGdvelwkvkqereriyslPEMSeddGMKVAElesvfaemdgytAESRAEEILLEAGI 144
Cdd:COG1116 84 ---VVFQEPallpwlTVLDNVALG-----------------LELR---GVPKAE------------RRERARELLELVGL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 145 -DKEFHYglmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTI----TWLANELNKRKCTMIIISHD 211
Cdd:COG1116 129 aGFEDAY-------PhqlsgGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
1.25e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 77.61 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDqfafeefsvvdav 85
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDE------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 imgdvelwkVKQERERIyslpemseddGMkvaelesVFAEMDGYTAESRAEEILleagidkefhYGLmanvAPGWKLRVL 165
Cdd:cd03229 71 ---------LPPLRRRI----------GM-------VFQDFALFPHLTVLENIA----------LGL----SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 166 LAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITrreVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
4.01e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFafeefs 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vVDAVIMGDVelwkvkqerERIYSL-PEMSEDDGMKVaeLESVFAEMdgytaesraeeiLLEAGIDKefhyglmanVAPG 159
Cdd:PRK09544 78 -LDTTLPLTV---------NRFLRLrPGTKKEDILPA--LKRVQAGH------------LIDAPMQK---------LSGG 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 160 WKLRVLLAQALFANPDILLLDEPTNNLDIH-------TITWLANELNkrkCTMIIISHDRHFLnsvcthMADID 226
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvalydLIDQLRRELD---CAVLMVSHDLHLV------MAKTD 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
6.44e-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: 76.86 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvGNLSQDQfafeefsvVD-AVIMGDVELwkVK 96
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL------DGTDIRQ--------LDpADLRRNIGY--VP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 97 QE--------RERI-YSLPEMSEDDGMKVAELesvfaemdgytaesraeeilleAGIDkEF---H---YGLM-----ANV 156
Cdd:cd03245 85 QDvtlfygtlRDNItLGAPLADDERILRAAEL----------------------AGVT-DFvnkHpngLDLQigergRGL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 157 APGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKC--TMIIISHDRHFLNSV 218
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
8.23e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV----SITPGLKVGnlsqdqFAFE-EFSVVDAVIMgdvelw 93
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngRVSALLELG------AGFHpELTGRENIYL------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 94 kvkqeRERIYslpemseddGMKVAELESVFaemdgytaesraEEILLEAGIDKEFHyglmanvAP------GWKLRVLLA 167
Cdd:COG1134 112 -----NGRLL---------GLSRKEIDEKF------------DEIVEFAELGDFID-------QPvktyssGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 168 QALFANPDILLLDEptnnldihtitWLA--------------NELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIY 233
Cdd:COG1134 159 VATAVDPDILLVDE-----------VLAvgdaafqkkclariRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-510 |
1.20e-15 |
|
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: 74.92 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWS-ENATFGycpQDSTKDFDN- 397
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDL---EDELPPLRRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 ------DLTLFDWMSqwrtakhndlmVRGMLGRLLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:cd03229 78 igmvfqDFALFPHLT-----------VLENIALGL-------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499648994 472 EA---IEALNNALKDFQG-TLIFVSHDREFVSSLATRIIDIKD 510
Cdd:cd03229 134 ITrreVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-243 |
1.26e-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: 76.56 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA--FEE 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKELYelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 79 FSVV---DAvimgdveLWkvkqereriyslpemsedDGMKVAE------LEsvFAEMDGYTAESRAEEILLEAGIDKefH 149
Cdd:COG1127 84 IGMLfqgGA-------LF------------------DSLTVFEnvafplRE--HTDLSEAEIRELVLEKLELVGLPG--A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 150 YGLManvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLNSVCT 220
Cdd:COG1127 135 ADKM----PselsgGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELRDElGLTSVVVTHDLDSAFAIAD 210
|
250 260
....*....|....*....|...
gi 499648994 221 HMADIDYGELrIYPGNYEKFLEA 243
Cdd:COG1127 211 RVAVLADGKI-IAEGTPEELLAS 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.37e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.39 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefsv 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgdvelwkvkqereriyslpemsedDGMKVAelesvFAEmdgyTAESRAeeilleAGIdkEFHYGLmanvAPGWK 161
Cdd:cd03216 60 ------------------------------DGKEVS-----FAS----PRDARR------AGI--AMVYQL----SVGER 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499648994 162 LRVLLAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLfkvIRRLRAQGVAVIFISH 140
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
329-506 |
1.52e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 76.29 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 329 FDGEMLFSGGDLLLEA-------GAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWsENATFGYCPQDSTKDFdnDLTL 401
Cdd:cd03237 2 TYPTMKKTLGEFTLEVeggsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADY--EGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 402 FDWM----------SQWRTAKHNDLMVRGMLGRLLftaddsnkkaRNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:cd03237 79 RDLLssitkdfythPYFKTEIAKPLQIEQILDREV----------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 499648994 472 EAIEALNNALKDF----QGTLIFVSHDREFVSSLATRII 506
Cdd:cd03237 149 EQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-514 |
1.56e-15 |
|
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: 75.70 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 340 LLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW-------------SENatFGYCPQDSTKDF----DNdLTLF 402
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlRRN--IGYVPQDVTLFYgtlrDN-ITLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 403 DwmsqwRTAKHNDLMVRGMLGRLL-FTADDSN-------KKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAI 474
Cdd:cd03245 102 A-----PLADDERILRAAELAGVTdFVNKHPNgldlqigERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499648994 475 EALNNALKDFQG--TLIFVSHdREFVSSLATRIIDIKDKQVI 514
Cdd:cd03245 177 ERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-211 |
1.58e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 75.41 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 26 NGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGL---------------KVGNLSQDQFAFEEFSVVDAVIMGdv 90
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 91 elWKVKQERERIYSLPEMSEddgmkVAELESvfaemdgytaesraeeiLLEAGIDKefhyglmanVAPGWKLRVLLAQAL 170
Cdd:cd03297 100 --LKRKRNREDRISVDELLD-----LLGLDH-----------------LLNRYPAQ---------LSGGEKQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499648994 171 FANPDILLLDEPTNNLDIHTITWLANELNKRK----CTMIIISHD 211
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELKQIKknlnIPVIFVTHD 191
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
2.10e-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: 78.93 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-----------TPGLKVGNLSQDqfaFEEFS 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdreTFGKHIGYLPQD---VELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 -VVDAVI--MGD-------VELWKVKQERERIYSLPemseddgmkvaelesvfaemDGYtaesraEEILLEAGidkefhy 150
Cdd:TIGR01842 406 gTVAENIarFGEnadpekiIEAAKLAGVHELILRLP--------------------DGY------DTVIGPGG------- 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 151 glmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSV 218
Cdd:TIGR01842 453 ---ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANaikALKARGITVVVITHRPSLLGCV 520
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-230 |
3.11e-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: 74.49 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQD--------- 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLTDDKKNinelrqkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 ----QFA-FEEFSVVDAVIMGDVELWKvkqereriyslpeMSEDDgmkvaelesvfaemdgytAESRAEEILLEAGI-DK 146
Cdd:cd03262 80 mvfqQFNlFPHLTVLENITLAPIKVKG-------------MSKAE------------------AEERALELLEKVGLaDK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 147 EFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMA 223
Cdd:cd03262 129 ADAYP--AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
....*..
gi 499648994 224 DIDYGEL 230
Cdd:cd03262 207 FMDDGRI 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-249 |
3.87e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.28 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI---TPglkvgnlSQDQFAF-EEFSVVdaviMGD-VEL 92
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyVP-------FKRRKEFaRRIGVV----FGQrSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 93 W---------KVKQErerIYSLPEmseddgmkvAELESVFAEMDgytaesraeEIL-LEAGIDKefhyglmanvaP---- 158
Cdd:COG4586 108 WwdlpaidsfRLLKA---IYRIPD---------AEYKKRLDELV---------ELLdLGELLDT-----------Pvrql 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 --GWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNK-RKCTMIIISHDrhflnsvcthMADI------- 225
Cdd:COG4586 156 slGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNReRGTTILLTSHD----------MDDIealcdrv 225
|
250 260
....*....|....*....|....*..
gi 499648994 226 ---DYGELrIYPGNYEKFLEAAGLQRE 249
Cdd:COG4586 226 iviDHGRI-IYDGSLEELKERFGPYKT 251
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
4.58e-15 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 74.46 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 17 FENISAKFGNGNRY-----------------GLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeef 79
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSI--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 svvdavIMGDVELWKVKQERERIY-------------SLpemseDDGMKVAELesvFAE-------MDGYTAESRAEEIL 139
Cdd:cd03257 63 ------IFDGKDLLKLSRRLRKIRrkeiqmvfqdpmsSL-----NPRMTIGEQ---IAEplrihgkLSKKEARKEAVLLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 140 LEA-GIDKEFhyglmANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIIS 209
Cdd:cd03257 129 LVGvGLPEEV-----LNRYPhelsgGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFIT 203
|
250 260
....*....|....*....|.
gi 499648994 210 HDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03257 204 HDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
4.89e-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: 72.80 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefsvvdavimGDVE 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI---------------------------DGVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 92 LWKVKQE--RERIYSLPEmseddgmkvaelESVFaeMDGytaeSRAEEILleAGidkefhyglmanvapGWKLRVLLAQA 169
Cdd:cd03228 66 LRDLDLEslRKNIAYVPQ------------DPFL--FSG----TIRENIL--SG---------------GQRQRIAIARA 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499648994 170 LFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRH 213
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAHRLS 156
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
348-514 |
7.21e-15 |
|
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: 73.69 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 348 LAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENAT----------FGYCPQDSTkdFDNDLTLFD---WMSQWR--TAK 412
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrkaarqsLGYCPQFDA--LFDELTVREhlrFYARLKglPKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 413 HNDLMVRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG--TLIF 490
Cdd:cd03263 109 EIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIIL 187
|
170 180
....*....|....*....|....
gi 499648994 491 VSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03263 188 TTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-525 |
9.11e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 77.11 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEM--LFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK--------WSENA---TFG 385
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 386 YCPQD----STKDFDNdLTLFDwmsqwRTAKHNDLM-----VRgmLGRLLFTADDS-----NKKARNCSGGEKNRLLFGK 451
Cdd:COG4987 413 VVPQRphlfDTTLREN-LRLAR-----PDATDEELWaalerVG--LGDWLAALPDGldtwlGEGGRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 452 LMMQDVNVLVMDEPTNHMD--MEA--IEALNNALKDfqGTLIFVSHDREFVsSLATRIIDIKDKQVIDfQGSFDEYLA 525
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDaaTEQalLADLLEALAG--RTVLLITHRLAGL-ERMDRILVLEDGRIVE-QGTHEELLA 558
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-230 |
1.07e-14 |
|
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: 74.07 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF-AFEEfsvvdavimgDVELw 93
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRrAFRR----------DVQL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 94 kVKQERERIYSlPEMSEddGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:TIGR02769 93 -VFQDSPSAVN-PRMTV--RQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 174 PDILLLDEPTNNLDIH---TITWLANELNKRKCT-MIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVlqaVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-245 |
1.15e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 76.73 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEEFSVV--DAVIM-- 87
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDLR-RRIAVVpqRPHLFdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 88 -------------GDVELWKVkqereriyslpemseddgMKVAELESVFAEM-DGYtaesraEEILLEAGidkefhyglm 153
Cdd:COG4987 424 tlrenlrlarpdaTDEELWAA------------------LERVGLGDWLAALpDGL------DTWLGEGG---------- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL-----NKrkcTMIIISHDRHFLNSVcTHMADIDYG 228
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLlealaGR---TVLLITHRLAGLERM-DRILVLEDG 545
|
250
....*....|....*..
gi 499648994 229 ELrIYPGNYEKFLEAAG 245
Cdd:COG4987 546 RI-VEQGTHEELLAQNG 561
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
1.58e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 72.79 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGnvsitpglkvgnlsqdqfafeefsv 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vDAVIMGDVELWKVKQERERIYSLPEM-SEDDGMKVAELESVFAEMDGYTAESRAEEI--LLEAGIDKEFHYGLMANVAP 158
Cdd:cd03265 56 -RATVAGHDVVREPREVRRRIGIVFQDlSVDDELTGWENLYIHARLYGVPGAERRERIdeLLDFVGLLEAADRLVKTYSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIII-SHDRHFLNSVCTHMADIDYGELR 231
Cdd:cd03265 135 GMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahVWEYIEKLKEEFGMTILLtTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-233 |
1.96e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.57 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 17 FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT------PGLKVGnlsqdqfaFE-EFSVVDAVIMgd 89
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsslLGLGGG--------FNpELTGRENIYL-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 90 velwkvkqeRERIYslpemseddGMKVAELESVFAEMdgytaESRAEeilLEAGIDKEF-HYglmanvAPGWKLRVLLAQ 168
Cdd:cd03220 108 ---------NGRLL---------GLSRKEIDEKIDEI-----IEFSE---LGDFIDLPVkTY------SSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 169 ALFANPDILLLDEptnnldihtitWLA--------------NELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIY 233
Cdd:cd03220 156 ATALEPDILLIDE-----------VLAvgdaafqekcqrrlRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-189 |
2.57e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-----------TPGLKVGNL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 70 SQD-QFAFEeFSVVDAVIMGDVelwkvkqereriyslPEMSEddgmkvaelesvFAEMDgyTAESRAEEILLEAGIDKEF 148
Cdd:PRK09536 83 PQDtSLSFE-FDVRQVVEMGRT---------------PHRSR------------FDTWT--ETDRAAVERAMERTGVAQF 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499648994 149 HYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH 189
Cdd:PRK09536 133 ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
330-527 |
2.75e-14 |
|
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: 75.64 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK-------------WSENatFGYCPQDstkDF- 395
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpasLRRQ--IGVVLQD---VFl 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 396 ------DNdLTLFD-WMSQ---WRTAK----HNDLMVR--------GMLGRLLftaddsnkkarncSGGEKNRLLFGKLM 453
Cdd:COG2274 561 fsgtirEN-ITLGDpDATDeeiIEAARlaglHDFIEALpmgydtvvGEGGSNL-------------SGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 454 MQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG--TLIFVSHDREFVsSLATRIIDIKDKQVIDfQGSFDEYLASC 527
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHEELLARK 700
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-529 |
3.11e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPGLK----VGN 68
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInninynklDHKLAaqlgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 69 LSQDQFAFEEFSVVDAVIMGDVELWKVKqereriyslpemseddGMKVAElesvFAEMdgytaESRAEEILLEAGIDKEF 148
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVC----------------GVNIID----WREM-----RVRAAMMLLRVGLKVDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 149 HYgLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISHDRHFLNSVC---THM 222
Cdd:PRK09700 140 DE-KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICdryTVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 223 ADidygelriypGNYekfleaaglqreqlLAENAKKSAEIDEL------QDFVNRFGANASKAKQASSRAkkmdkikLDE 296
Cdd:PRK09700 219 KD----------GSS--------------VCSGMVSDVSNDDIvrlmvgRELQNRFNAMKENVSNLAHET-------VFE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 297 VKsssrmsPSLSFDEGKkmyrqaleVNKIGhgfdgemlFSggdllLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV 376
Cdd:PRK09700 268 VR------NVTSRDRKK--------VRDIS--------FS-----VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 377 KWSENATFGYCPQDSTKD-------------FDNDLTLFDWMSQWRTAKHNDLmvRGMLGrlLFTADDSNKKARN----- 438
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKgmayitesrrdngFFPNFSIAQNMAISRSLKDGGY--KGAMG--LFHEVDEQRTAENqrell 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 439 ---C----------SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEALNNALKDfQGTLIFVshdrefVSSLA 502
Cdd:PRK09700 397 alkChsvnqnitelSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLAD-DGKVILM------VSSEL 469
|
570 580
....*....|....*....|....*..
gi 499648994 503 TRIIDIKDKQVIDFQGSFDEYLASCEE 529
Cdd:PRK09700 470 PEIITVCDRIAVFCEGRLTQILTNRDD 496
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
3.24e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 75.09 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAF------EEFSVVDAV 85
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRrvsvcaQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 IMGDVELWKvkqereriyslPEMSEDDGMKVAE---LESVFAEmdgytaesraeeilLEAGIDKEFHYGlMANVAPGWKL 162
Cdd:TIGR02868 425 VRENLRLAR-----------PDATDEELWAALErvgLADWLRA--------------LPDGLDTVLGEG-GARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 163 RVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHD 211
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAalSGRTVVLITHH 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
331-530 |
3.43e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 75.28 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 331 GEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLR--------------------------------CLVD----------- 367
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttalqCVLNtdiertqllee 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 368 ELKSLEGEVKWSENATFGYCPQDSTKDFDND------------LTLFD-WMSQWRTAkhndlmvrGMLGRLLFTADDSNK 434
Cdd:PLN03073 269 EAQLVAQQRELEFETETGKGKGANKDGVDKDavsqrleeiykrLELIDaYTAEARAA--------SILAGLSFTPEMQVK 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 435 KARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLV 420
|
250
....*....|....*.
gi 499648994 515 DFQGSFDEYLASCEEK 530
Cdd:PLN03073 421 TYKGDYDTFERTREEQ 436
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-522 |
4.05e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 72.08 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KWSENA--------T 383
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPPHEiarlgigrT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 384 FgycpQDsTKDFDNdLTLFDWMsqwRTAKHNDLMVRGMLGRLLFTADDSNKKARNC-----------------SGGEKNR 446
Cdd:cd03219 81 F----QI-PRLFPE-LTVLENV---MVAAQARTGSGLLLARARREEREARERAEELlervgladladrpagelSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 447 LLFGKLMMQDVNVLVMDEPT---NHMDMEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIdikdkqVIDF-----QG 518
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT------VLDQgrviaEG 225
|
....
gi 499648994 519 SFDE 522
Cdd:cd03219 226 TPDE 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
5.06e-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: 74.63 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQF-GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----TPGLK-------VGNL 69
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADadswrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 70 SQDQFAFEEfSVVDAVIMGDvelwkvkqereriyslPEMSEDDGMKVAELesvfAEMDGYTAEsraeeilLEAGIDKEFH 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR----------------PDASDAEIREALER----AGLDEFVAA-------LPQGLDTPIG 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 150 YGlMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISHDRH 213
Cdd:TIGR02857 454 EG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeaeVLEALRALAQGR-TVLLVTHRLA 518
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-231 |
5.93e-14 |
|
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: 71.00 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITPGLK-----VGNLSQDQFAFEEFSVVDAV-IM 87
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingySIRTDRKaarqsLGYCPQFDALFDELTVREHLrFY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 88 GdvelwkvkqereRIYSLPEmseddgmkvaelESVFAEMDGYtaesrAEEILLEAGIDKEFHyglmaNVAPGWKLRVLLA 167
Cdd:cd03263 100 A------------RLKGLPK------------SEIKEEVELL-----LRVLGLTDKANKRAR-----TLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 168 QALFANPDILLLDEPTNNLDIHT--ITW-LANELnKRKCTMIIISHDRHFLNSVCTHMADIDYGELR 231
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASrrAIWdLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
5.96e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.73 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA----- 75
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN-GRPLADWSPAELArrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 --------FeEFSVVDAVIMGDVELWKVKQERERIYslpemseDDGMKVAELESvFAEMDgYTAESRAEeilleagidke 147
Cdd:PRK13548 81 lpqhsslsF-PFTVEEVVAMGRAPHGLSRAEDDALV-------AAALAQVDLAH-LAGRD-YPQLSGGE----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 148 fhyglmanvapgwKLRVLLAQAL--FANPD----ILLLDEPTNNLDI---HTITWLANEL-NKRKCTMIIISHDrhfLN 216
Cdd:PRK13548 140 -------------QQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqHHVLRLARQLaHERGLAVIVVLHD---LN 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-231 |
6.40e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.86 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPL----FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVgnLSQDQFAF 76
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDV--VKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 77 EEFSVVDAvimgdvelwkvkqeRERIYslpemsedDGMKVAELESVFAE---MDGYTAESRAEEILLEAGIdKEFHYGLM 153
Cdd:cd03266 78 RRLGFVSD--------------STGLY--------DRLTARENLEYFAGlygLKGDELTARLEELADRLGM-EELLDRRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03266 135 GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
.
gi 499648994 231 R 231
Cdd:cd03266 215 V 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-213 |
6.81e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 71.31 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQF--GAEPL--FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ--- 73
Cdd:COG4181 8 IIELRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDArar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 74 -------FAFEEFSVvdavimgdvelwkvkqereriysLPEMSeddgmkvAeLESVF--AEMDGYT-AESRAEEILLEAG 143
Cdd:COG4181 87 lrarhvgFVFQSFQL-----------------------LPTLT-------A-LENVMlpLELAGRRdARARARALLERVG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 144 I-DKEFHYglmanvaP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNK-RKCTMIIISHDRH 213
Cdd:COG4181 136 LgHRLDHY-------PaqlsgGEQQRVALARAFATEPAILFADEPTGNLDAATgeqIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-506 |
7.14e-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: 70.63 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkWSENATF----------GYCPQ 389
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDVtgvpperrniGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 DstkdfdndLTLFDWMSQW-------RTAKHNDLMVRGMLGRLLFTADDS---NKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:cd03259 80 D--------YALFPHLTVAeniafglKLRGVPKAEIRARVRELLELVGLEgllNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 460 LVMDEPTNHMDMEAIEALNNALKDFQG----TLIFVSHDREFVSSLATRII 506
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-226 |
8.06e-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: 70.93 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlsqdqfafEEFSVVDAVIMGDVELWK 94
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR---------------HDGGWVDLAQASPREILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 95 VKqeRERI-Y------SLPEMSEDDgmKVAE--LEsvfAEMDGYTAESRAEEILLEAGIDKEFHyglmaNVAP-----GW 160
Cdd:COG4778 90 LR--RRTIgYvsqflrVIPRVSALD--VVAEplLE---RGVDREEARARARELLARLNLPERLW-----DLPPatfsgGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADID 226
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-513 |
1.55e-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: 69.83 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KWSE-------NATFGYCPQDstkdFD--NDLTL 401
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEkelaafrRRHIGFVFQS----FNllPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 402 FD-----WMSQWRTAKHNDLMVRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----- 470
Cdd:cd03255 100 LEnvelpLLLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDsetgk 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499648994 471 --MEAIEALNnalKDFQGTLIFVSHDREFVsSLATRIIDIKDKQV 513
Cdd:cd03255 178 evMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-210 |
1.61e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.79 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpgLKVGNLSQDQFAFEEFSV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV---LGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDAVIMGDVELwkvkQEREriySLPEMSEDDGMKVAELESVFAemdgytaeSRAEEILLEAGIDKEfhyglMANVAPGWK 161
Cdd:PRK13536 119 VPQFDNLDLEF----TVRE---NLLVFGRYFGMSTREIEAVIP--------SLLEFARLESKADAR-----VSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 162 LRVLLAQALFANPDILLLDEPTNNLDIHT--ITW--LANELNKRKcTMIIISH 210
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLARGK-TILLTTH 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-526 |
1.95e-13 |
|
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: 69.84 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK-----WSENA---------TFG 385
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSeaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 386 YCPQDSTKdFDnDLTLFD----WMSQWRTAKHND-----LMVRGMLGrllfTADDSNKKARNCSGGEKNRLLFGKLMMQD 456
Cdd:cd03261 81 MLFQSGAL-FD-SLTVFEnvafPLREHTRLSEEEireivLEKLEAVG----LRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 457 VNVLVMDEPTNHMD---MEAIEALNNALKD-FQGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGSFDEYLAS 526
Cdd:cd03261 155 PELLLYDEPTAGLDpiaSGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRAS 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-518 |
2.87e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.11 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEM--LFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenaTFGYCPQDSTKDfdn 397
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI------TLDGVPVSDLEK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 dlTLFDWMSQWRTAKHndlmvrgmlgrlLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEA 473
Cdd:cd03247 72 --ALSSLISVLNQRPY------------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499648994 474 IEALNNALKDfqGTLIFVSHDREFVSSlATRIIDIKDKQVIdFQG 518
Cdd:cd03247 138 LSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKII-MQG 178
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
3.14e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpgLKVGNLSQDQFAFEEFsVVDAVIMGDV--ELWKV 95
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI--FKDEKNKKKTKEKEKV-LEKLVIQKTRfkKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 96 KQERERI--------YSLPEMS-EDD--------GMKVAElesvfaemdgytAESRAEEILLEAGIDKEFHYGLMANVAP 158
Cdd:PRK13651 101 KEIRRRVgvvfqfaeYQLFEQTiEKDiifgpvsmGVSKEE------------AKKRAAKYIELVGLDESYLQRSPFELSG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRKCTMIIISHD 211
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQgvkEILEIFDNLNKQGKTIILVTHD 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-233 |
3.68e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.46 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgNLSQDQFAfeefsv 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-------DGKPLDIA------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgdvelwkvkqERERIYSLPemsEDDG----MKVAELESVFAEMDGYT---AESRAEEILleagidKEFHYGLMA 154
Cdd:cd03269 68 ----------------ARNRIGYLP---EERGlypkMKVIDQLVYLAQLKGLKkeeARRRIDEWL------ERLELSEYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 155 NV-----APGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADID 226
Cdd:cd03269 123 NKrveelSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLN 202
|
....*..
gi 499648994 227 YGELRIY 233
Cdd:cd03269 203 KGRAVLY 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-518 |
6.04e-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: 67.99 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAkLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSE----------NATFGYCPQ 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 DstkdfdndltlFDWMSQWRT--------------AKHNDLMVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQ 455
Cdd:cd03264 80 E-----------FGVYPNFTVrefldyiawlkgipSKEVKARVDEVL-ELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 456 DVNVLVMDEPTNHMDMEAIEALNNALKDFQGTLIFV--SHDREFVSSLATRIIDIKDKQVIdFQG 518
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-531 |
6.67e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRC--LVDELKSleGEVKwsenatFGYCPQDSTKDFD 396
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEA--GTIR------VGDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 397 NDLTLFDWMSQW-------------RTAKHN----DLMVRGM-------LGRLLFT----ADDSNKKARNCSGGEKNRLL 448
Cdd:PRK11264 75 QQKGLIRQLRQHvgfvfqnfnlfphRTVLENiiegPVIVKGEpkeeataRARELLAkvglAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 449 FGKLMMQDVNVLVMDEPTNHMDMEAI-EALNN--ALKDFQGTLIFVSHDREFVSSLATRIIDIkDKQVIDFQGSFDEYLA 525
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFM-DQGRIVEQGPAKALFA 233
|
....*.
gi 499648994 526 SCEEKK 531
Cdd:PRK11264 234 DPQQPR 239
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
339-526 |
9.68e-13 |
|
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: 70.56 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK-------------WSENatFGYCPQDSTkdfdndltLF--- 402
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdldpasWRRQ--IAWVPQNPY--------LFagt 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 403 --------------DWMSQW-RTAKHNDLmVRGMLGRLLFTADDSnkkARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTN 467
Cdd:COG4988 427 irenlrlgrpdasdEELEAAlEAAGLDEF-VAALPDGLDTPLGEG---GRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 468 HMDMEAIEALNNALKD-FQG-TLIFVSHDREFVsSLATRIIDIKDKQVIDfQGSFDEYLAS 526
Cdd:COG4988 503 HLDAETEAEILQALRRlAKGrTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAK 561
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-210 |
9.89e-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: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVgnlsqdQFAfeefSVVDA- 84
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-GEPV------RFR----SPRDAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 85 ---VIMgdvelwkVKQEReriySL-PEMSeddgmkVAelESVF-------------AEMdgytaESRAEEILLEAGIDke 147
Cdd:COG1129 78 aagIAI-------IHQEL----NLvPNLS------VA--ENIFlgreprrgglidwRAM-----RRRARELLARLGLD-- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 148 fhyglmanVAPGWKLR---------VLLAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISH 210
Cdd:COG1129 132 --------IDPDTPVGdlsvaqqqlVEIARALSRDARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISH 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
1.30e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.85 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglKVGN--------LSQD 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI------RVGDitidtarsLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 Q-----------FAFEEF------SVVDAVIMGDVELWKVKQEReriyslpemseddgmkvaelesvfaemdgytAESRA 135
Cdd:PRK11264 77 KglirqlrqhvgFVFQNFnlfphrTVLENIIEGPVIVKGEPKEE-------------------------------ATARA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 136 EEILLEAGID-KEFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANElnKRkcTMII 207
Cdd:PRK11264 126 RELLAKVGLAgKETSYP--RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQE--KR--TMVI 199
|
250 260
....*....|....*....|.
gi 499648994 208 ISHDRHFLNSVCTHMADIDYG 228
Cdd:PRK11264 200 VTHEMSFARDVADRAIFMDQG 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-222 |
1.37e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----------TPG-LKVGNLS 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdKDGqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 71 QDQFAFEEFSVVdaviMGDVELWKVKQERERIYSLPemSEDDGMKVAElesvfaemdgytAESRAEEILLEAGIDKEFHY 150
Cdd:PRK10619 86 QLRLLRTRLTMV----FQHFNLWSHMTVLENVMEAP--IQVLGLSKQE------------ARERAVKYLAKVGIDERAQG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 151 GLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHM 222
Cdd:PRK10619 148 KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHV 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-247 |
1.41e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfeefsvvdav 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAFA---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 imgdvelwkvkqeRERIYSLPEMSEDDGMKVAELESV-----FAEMDGYTAESRA--EEILLEAGIdKEFHYGLMANVAP 158
Cdd:PRK10575 85 -------------RKVAYLPQQLPAAEGMTVRELVAIgrypwHGALGRFGAADREkvEEAISLVGL-KPLAHRLVDSLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDI-HTITWLA--NELNK-RKCTMIIISHDRHFLNSVCTHMADIDYGELrIYP 234
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEM-IAQ 229
|
250
....*....|...
gi 499648994 235 GNYEKFLEAAGLQ 247
Cdd:PRK10575 230 GTPAELMRGETLE 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
1.60e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefs 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvdavimGDVELWKV--KQERERIYSLPE-MSEDDGMKVAEL--------ESVFAEMDGyTAESRAEEILLEAGIDkEFH 149
Cdd:PRK11231 62 -------GDKPISMLssRQLARRLALLPQhHLTPEGITVRELvaygrspwLSLWGRLSA-EDNARVNQAMEQTRIN-HLA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 150 YGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI-HTITW--LANELNKRKCTMIIISHDrhfLNSVC 219
Cdd:PRK11231 133 DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInHQVELmrLMRELNTQGKTVVTVLHD---LNQAS 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-522 |
1.81e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 67.21 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGF-DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENatfgycpqDSTKDFDND 398
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--------DINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 399 LTlfdwmsQWR----------------TAKHNDLMvrGMLGRL--------LFT----------------ADDSNKKARN 438
Cdd:cd03256 73 LR------QLRrqigmifqqfnlierlSVLENVLS--GRLGRRstwrslfgLFPkeekqralaalervglLDKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 439 CSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKD----FQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
....*...
gi 499648994 515 dFQGSFDE 522
Cdd:cd03256 225 -FDGPPAE 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
3.64e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAE--PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafee 78
Cdd:PRK13632 7 MIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 79 fsvvDAVIMGDVELWKVKQERERIYSLPE------MSEDDgmkVA-ELESV---FAEMDGYTAESrAEEILLEAGIDKEF 148
Cdd:PRK13632 69 ----DGITISKENLKEIRKKIGIIFQNPDnqfigaTVEDD---IAfGLENKkvpPKKMKDIIDDL-AKKVGMEDYLDKEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 149 HyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANEL-NKRKCTMIIISHD 211
Cdd:PRK13632 141 Q-----NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLrKTRKKTLISITHD 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
4.38e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQD-------- 72
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVNDPKVDerlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 -----QF-AFEEFSVVDAVIMGDVelwKVKqereriyslpemseddGMKVAElesvfaemdgytAESRAEEILLEAGI-D 145
Cdd:PRK09493 80 gmvfqQFyLFPHLTALENVMFGPL---RVR----------------GASKEE------------AEKQARELLAKVGLaE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 146 KEFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHM 222
Cdd:PRK09493 129 RAHHYP--SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
....*.
gi 499648994 223 ADIDYG 228
Cdd:PRK09493 207 IFIDKG 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-230 |
4.53e-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: 65.51 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAE-PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAFEEFS 80
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-GQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VvdAVIMGDVELwkvkqereriysLPEMSEDDGMKVAeLESVfaEMDGYTAESRAEEILLEAGIdKEFHYGLMANVAPGW 160
Cdd:cd03292 80 I--GVVFQDFRL------------LPDRNVYENVAFA-LEVT--GVPPREIRKRVPAALELVGL-SHKHRALPAELSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-210 |
5.87e-12 |
|
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: 65.71 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAE-PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEEFSVV-- 82
Cdd:cd03253 5 NVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLR-RAIGVVpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 83 DAVIMGDVELWKVKqereriYSLPEMSEDD---GMKVAELESVFAEM-DGYtaesraEEILLEAGidkefhygLManVAP 158
Cdd:cd03253 83 DTVLFNDTIGYNIR------YGRPDATDEEvieAAKAAQIHDKIMRFpDGY------DTIVGERG--------LK--LSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
330-494 |
9.36e-12 |
|
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: 67.39 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KWSEN---ATFGYCPQDSTkdfdnd 398
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVCAQDAH------ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 399 ltLFDwmsqwrTAKHNDLMV---------------RGMLGRLLFTADDS-----NKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:TIGR02868 420 --LFD------TTVRENLRLarpdatdeelwaaleRVGLADWLRALPDGldtvlGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 499648994 459 VLVMDEPTNHMDMEAIEALNNALKD-FQG-TLIFVSHD 494
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAaLSGrTVVLITHH 529
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-506 |
9.53e-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: 65.22 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK--------WSENAT---FGYCP 388
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARarrVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 389 QDStkDFDNDLTLFDWMSQWRT---------AKHNDLMVRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:TIGR03873 82 QDS--DTAVPLTVRDVVALGRIphrslwagdSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499648994 460 LVMDEPTNHMDMEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRII 506
Cdd:TIGR03873 159 LLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVV 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
331-477 |
9.57e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 331 GEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWS-ENATFGYCPQDST----KDFDND-LTLFDW 404
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEACHylghRNAMKPaLTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 405 MSQWRTAKHN-DLMVRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEAL 477
Cdd:PRK13539 94 LEFWAAFLGGeELDIAAALEAVgL--APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-218 |
1.08e-11 |
|
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: 67.08 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-----------TPGLKVGNLSQDQ--FA--- 75
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreELGRHIGYLPQDVelFDgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 ------FEEFS---VVDAVIMGDVElwkvkqerERIYSLPemseddgmkvaelesvfaemDGYtaesraEEILLEAGidk 146
Cdd:COG4618 423 aeniarFGDADpekVVAAAKLAGVH--------EMILRLP--------------------DGY------DTRIGEGG--- 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 147 efhyglmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITwlanELNKRKCTMIIISHDRHFLNSV 218
Cdd:COG4618 466 -------ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLLAAV 533
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-211 |
1.09e-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: 64.90 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGL--------------KVGNLSQDQFAFEEFSVVD 83
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQIGMIFQQFNLIERLSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 84 AVIMGdvelwkvkqereriySLPEMSeddgmKVAELESVFAEMDGYtaesRAEEILLEAGIDkEFHYGLMANVAPGWKLR 163
Cdd:cd03256 98 NVLSG---------------RLGRRS-----TWRSLFGLFPKEEKQ----RALAALERVGLL-DKAYQRADQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKrkcTMIIISHD 211
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQ 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
1.10e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF-AFEefsvvdavimGDV 90
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRkAFR----------RDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 91 ELwkVKQE-------RERIyslpemseddGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLR 163
Cdd:PRK10419 92 QM--VFQDsisavnpRKTV----------REIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRKCT-MIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVlqaGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-190 |
1.15e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.11 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT------PGLKVGNLSQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 75 AFEEFSVVDAVIMGdVELWKV-KQEReriyslpemseddgmkvaelesvfaemdgytaESRAEEILLEAGIDkEFHYGLM 153
Cdd:PRK11248 81 LLPWRNVQDNVAFG-LQLAGVeKMQR--------------------------------LEIAHQMLKKVGLE-GAEKRYI 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT 190
Cdd:PRK11248 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
1.20e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.60 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI----TPG------LKVGNLSQ 71
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepVPSrarharQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 72 DQFAFEEFSVVDAV-IMGDVELWKVKQERERIYSLPEMseddgmkvAELESvfaemdgyTAESRAEEIlleagidkefhy 150
Cdd:PRK13537 88 FDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEF--------AKLEN--------KADAKVGEL------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 151 glmanvAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDY 227
Cdd:PRK13537 140 ------SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPqarHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
.
gi 499648994 228 G 228
Cdd:PRK13537 214 G 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-514 |
1.44e-11 |
|
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: 64.06 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLF----SGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSEN-------------- 381
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 382 ATFGYCPQDSTKDFDNDLTLFD-----WMSQWRTAKHNDLMVRGMLGRLLFTADDS--NKKARNCSGGEKNRLLFGKLMM 454
Cdd:cd03257 82 KEIQMVFQDPMSSLNPRMTIGEqiaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 455 QDVNVLVMDEPTNHMDM----EAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03257 162 LNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-212 |
1.79e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.55 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlsqDQfafeefsv 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN----------GR-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgDVELWKVKQEReRI------YSL-PEMSEDD----GMKVAELESvfAEmdgytAESRAEEILLEAGIDKefhy 150
Cdd:COG1118 65 -------DLFTNLPPRER-RVgfvfqhYALfPHMTVAEniafGLRVRPPSK--AE-----IRARVEELLELVQLEG---- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 151 glMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTI----TWLANELNKRKCTMIIISHDR 212
Cdd:COG1118 126 --LADRYPsqlsgGQRQRVALARALAVEPEVLLLDEPFGALDAKVRkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-211 |
1.90e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 64.02 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF-AFEEFSVVDavimgdvelWKVK 96
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-GKQITEPGPDRMvVFQNYSLLP---------WLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 97 qeRERIY-----SLPEMSEDDGMKVAElESVfaEMDGYT--AESRAEEIlleagidkefhyglmanvAPGWKLRVLLAQA 169
Cdd:TIGR01184 72 --RENIAlavdrVLPDLSKSERRAIVE-EHI--ALVGLTeaADKRPGQL------------------SGGMKQRVAIARA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499648994 170 LFANPDILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHD 211
Cdd:TIGR01184 129 LSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
330-511 |
2.11e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.56 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenatfgYCPQDSTkdfdndlTLFdwMSQwR 409
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGED-------LLF--LPQ-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 410 TakhndLMVRGML-GRLLFTADDsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTL 488
Cdd:cd03223 73 P-----YLPLGTLrEQLIYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITV 141
|
170 180
....*....|....*....|...
gi 499648994 489 IFVSHdREFVSSLATRIIDIKDK 511
Cdd:cd03223 142 ISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
2.15e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 63.90 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS----------Q 71
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-GEDATDVPvqernvgfvfQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 72 DQFAFEEFSVVDAVIMGdvelWKVKQERERiysLPEmseddgmkvaelesvfAEMDGytaesRAEEILLEAGIDKefhyg 151
Cdd:cd03296 82 HYALFRHMTVFDNVAFG----LRVKPRSER---PPE----------------AEIRA-----KVHELLKLVQLDW----- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 152 lMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT----ITWLANELNKRKCTMIIISHD 211
Cdd:cd03296 129 -LADRYPaqlsgGQRQRVALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHD 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-514 |
2.16e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 63.45 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENA-------TFGYCPQDstKDFDNDLTLFD---WMSQWRTA 411
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnRIGYLPEE--RGLYPKMKVIDqlvYLAQLKGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 412 KHNDLM--VRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG--- 486
Cdd:cd03269 101 KKEEARrrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagk 179
|
170 180
....*....|....*....|....*...
gi 499648994 487 TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03269 180 TVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
2.48e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.95 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfeefs 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATTPSRELA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvdavimgdvelwKV----KQE---------RERI------YSLPEMSEDDGMKVAE-LEsvFAEMDGYtAESRAEEIll 140
Cdd:COG4604 75 -------------KRlailRQEnhinsrltvRELVafgrfpYSKGRLTAEDREIIDEaIA--YLDLEDL-ADRYLDEL-- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 141 eAGidkefhyglmanvapGWKLRVLLAQALFANPDILLLDEPTNNLDIH-------TITWLANELNKrkcTMIIISHD 211
Cdd:COG4604 137 -SG---------------GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKhsvqmmkLLRRLADELGK---TVVIVLHD 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
2.58e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 32 LIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ----------FAFEEFSVVDAV-IMGDVELWKV-KQER 99
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQMDEEAraklrakhvgFVFQSFMLIPTLnALENVELPALlRGES 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 100 ERiyslpemseddgmkvaelesvfaemdgyTAESRAEEILLEAGIDKEFHYgLMANVAPGWKLRVLLAQALFANPDILLL 179
Cdd:PRK10584 120 SR----------------------------QSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 499648994 180 DEPTNNLDIHT---ITWLANELNKR-KCTMIIISHD 211
Cdd:PRK10584 171 DEPTGNLDRQTgdkIADLLFSLNREhGTTLILVTHD 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-506 |
4.16e-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: 62.97 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLvDELKSLEGEVKWSENATFGycPQDSTKDFDNDL 399
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGAPDEGEVLLD--GKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 -------------TLFD-----------WMSQWRTAKHNDLMVRGMLGR-LLFTADDSNKKARNCSGGEKNRLLFGKLMM 454
Cdd:cd03260 78 elrrrvgmvfqkpNPFPgsiydnvayglRLHGIKLKEELDERVEEALRKaALWDEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 455 QDVNVLVMDEPTNHMD---MEAIEALNNALKDfQGTLIFVSHDREFVSSLATRII 506
Cdd:cd03260 158 NEPEVLLLDEPTSALDpisTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTA 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
348-514 |
4.51e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 62.70 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 348 LAVIGENGVGKTTFLRCLVDELKSLEGEVKWSenatfGYCPQDSTKDFD------------NDLTLFDWMS--------- 406
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-----GTVLFDSRKKINlppqqrkiglvfQQYALFPHLNvrenlafgl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 407 -QWRTAKHNDLmVRGMLGRLlftADDSNKKAR--NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNN 479
Cdd:cd03297 101 kRKRNREDRIS-VDELLDLL---GLDHLLNRYpaQLSGGEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*
gi 499648994 480 ALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03297 177 IKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
6.11e-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: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAfEEFSVV--DAVIM-G 88
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-GVDIRDLTLESLR-RQIGVVpqDTFLFsG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 89 DVelwkvkqeRERI-YSLPEMSEDD---GMKVAELESVFAEM-DGYtaesraEEILLEAGidkefhyglmANVAPGWKLR 163
Cdd:COG1132 429 TI--------RENIrYGRPDATDEEveeAAKAAQAHEFIEALpDGY------DTVVGERG----------VNLSGGQRQR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
6.23e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSqdqfafeefSVVDAVIMgdvelwkvKQE 98
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLS---------SAAKAELR--------NQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 99 RERIYS----LPEMS--EDDGMKVaelesVFAEMDGYTAESRAEEILLEAGIDKEFHYgLMANVAPGWKLRVLLAQALFA 172
Cdd:PRK11629 89 LGFIYQfhhlLPDFTalENVAMPL-----LIGKKKPAEINSRALEMLAAVGLEHRANH-RPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499648994 173 NPDILLLDEPTNNLDIHT---ITWLANELNKRKCT-MIIISHD 211
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNadsIFQLLGELNRLQGTaFLVVTHD 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-187 |
6.76e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAeplF---ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITPG-----LKVGNLSQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGdiatrRRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 qfAF---EEFSVvdavimgdvelwkvKQERE---RIYSLPEmsEDDGMKVAELESVFAEMDgyTAESRAEEILLeaGIdk 146
Cdd:NF033858 347 --AFslyGELTV--------------RQNLElhaRLFHLPA--AEIAARVAEMLERFDLAD--VADALPDSLPL--GI-- 402
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499648994 147 efhyglmanvapgwKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:NF033858 403 --------------RQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
6.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.26 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFafeefsvvdavimgdveLWKVKQE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKY-----------------IRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 99 RERIYSLPE--MSEDDgmkvAELESVFA----EMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQALFA 172
Cdd:PRK13646 87 IGMVFQFPEsqLFEDT----VEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499648994 173 NPDILLLDEPTNNLD-------IHTITWLANELNKrkcTMIIISHD 211
Cdd:PRK13646 163 NPDIIVLDEPTAGLDpqskrqvMRLLKSLQTDENK---TIILVSHD 205
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-230 |
6.93e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvGNLSQdQFAFEEFS----- 80
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLD-----GEHIQ-HYASKEVArrigl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 -VVDAVIMGDVELwkvkQE---RERIYSLPEMS----EDDgmkvaelesvfaemDGYTAESRAEEI--LLEAGIDkefhy 150
Cdd:PRK10253 86 lAQNATTPGDITV----QElvaRGRYPHQPLFTrwrkEDE--------------EAVTKAMQATGIthLADQSVD----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 151 glmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI-HTITWLA--NELNKRK-CTMIIISHDrhfLNSVC---THMA 223
Cdd:PRK10253 143 ----TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNREKgYTLAAVLHD---LNQACryaSHLI 215
|
....*..
gi 499648994 224 DIDYGEL 230
Cdd:PRK10253 216 ALREGKI 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
8.76e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglkvgnlsqdqfafeefs 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvdavimGDVELWKVkqeRERIYSLpemSEDDGMK----VAELESVFAEMDGyTAESRAEEIL----LEAGIDKEFHYgL 152
Cdd:PRK13539 64 -------GDIDDPDV---AEACHYL---GHRNAMKpaltVAENLEFWAAFLG-GEELDIAAALeavgLAPLAHLPFGY-L 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499648994 153 MAnvapGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN 196
Cdd:PRK13539 129 SA----GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
9.75e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFAF---EEFSVVdavimgdvelwk 94
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-GQDVATLDADALAQlrrEHFGFI------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 95 vkqeRERIYSLPEMSEDDGMkvaELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGlMANVAPGWKLRVLLAQALFANP 174
Cdd:PRK10535 92 ----FQRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499648994 175 DILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHD 211
Cdd:PRK10535 164 QVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
1.26e-10 |
|
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: 61.58 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS-----ITPgLK-----VGNLSQDQFAFEEFSVVDAVIM 87
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkdITN-LPpekrdISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 88 GdveLWKVKQERERIyslpemseddgmkvaelesvfaemdgytaESRAEEILLEAGIDKEFHYGlMANVAPGWKLRVLLA 167
Cdd:cd03299 95 G---LKKRKVDKKEI-----------------------------ERKVLEIAEMLGIDHLLNRK-PETLSGGEQQRVAIA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499648994 168 QALFANPDILLLDEPTNNLDIHTITWLANELNK----RKCTMIIISHD 211
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-522 |
1.40e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYcpqdSTKDFDNDL 399
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML----SSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 TLFD---------------------WMSQW-RTAKHNDLMVRGMLGRLlFTADDSNKKARNCSGGEKNRLLFGKLMMQDV 457
Cdd:PRK11231 79 ALLPqhhltpegitvrelvaygrspWLSLWgRLSAEDNARVNQAMEQT-RINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 458 NVLVMDEPTNHMD-------MEAIEALNNALKdfqgTLIFVSHDREFVSSLATRIIDIKDKQVIDfQGSFDE 522
Cdd:PRK11231 158 PVVLLDEPTTYLDinhqvelMRLMRELNTQGK----TVVTVLHDLNQASRYCDHLVVLANGHVMA-QGTPEE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-278 |
1.54e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQFAFEEfS 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLLALRQ-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDAVIMGDVELWKVKQERERIYSLPEMSeddgmkVAELESVFAEMDGYTaesraeeiLLEAgidKEFHYGLMANVAPGW 160
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDSDIAFSLRNLG------VPEAEITRRVDEALT--------LVDA---QHFRHQPIQCLSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 161 KLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKrkctMIIISHDRHFLNSVCTHMADIDYGELRIY 233
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 234 --PGNY---EKFLEAAGLQREQLLAENAKKSAEIDELQ-DFVNRFGANASK 278
Cdd:PRK13638 218 gaPGEVfacTEAMEQAGLTQPWLVKLHTQLGLPLCKTEtEFFHRMQKCAFR 268
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-526 |
2.09e-10 |
|
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: 63.00 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKS---LEGEVKWSENATF-----------GYCPQDSTKDFdNDLTLFDW 404
Cdd:COG1123 26 SLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLelsealrgrriGMVFQDPMTQL-NPVTVGDQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 405 M----------SQWRTAKHNDLMVRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM--- 471
Cdd:COG1123 105 IaealenlglsRAEARARVLELLEAVGLERRL------DRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttq 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 472 -EAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGSFDEYLAS 526
Cdd:COG1123 179 aEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV-EDGPPEEILAA 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
339-526 |
2.48e-10 |
|
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: 62.05 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSenatfGYCPQDSTKDFD------------NDLTLFdwms 406
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-----GRTLFDSRKGIFlppekrrigyvfQEARLF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 407 qwrtaKHndLMVRGML--GRLLFTADDSN-----------------KKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTN 467
Cdd:TIGR02142 88 -----PH--LSVRGNLryGMKRARPSERRisferviellgighllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 468 HMDM----EAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFqGSFDEYLAS 526
Cdd:TIGR02142 161 ALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWAS 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-514 |
2.67e-10 |
|
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: 58.98 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKdfdndl 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 tlfdwmsqwrtakhndlmvrgmLG-RLLFtaddsnkkarNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALN 478
Cdd:cd03216 75 ----------------------AGiAMVY----------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 499648994 479 NALKDF--QG-TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03216 123 KVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-208 |
3.63e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsQDQF------AFEEfsvvdavimgdveLWK-VKQER 99
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGER------------QSQFshitrlSFEQ-------------LQKlVSDEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 100 ERIYS--LPEMSEDDGMKVAELEsvfaeMDGYTAESRAEEILLEAGI----DKEFHYglmanVAPGWKLRVLLAQALFAN 173
Cdd:PRK10938 84 QRNNTdmLSPGEDDTGRTTAEII-----QDEVKDPARCEQLAQQFGItallDRRFKY-----LSTGETRKTLLCQALMSE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 499648994 174 PDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIII 208
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAEllaSLHQSGITLVLV 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
3.92e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.65 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefs 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvdavimGDVELWKVKQERERI------YSL-PEMSeddgmkVAE-----LEsvFAEMDGYTAESRAEEIL----LEAgi 144
Cdd:COG3842 65 -------DGRDVTGLPPEKRNVgmvfqdYALfPHLT------VAEnvafgLR--MRGVPKAEIRARVAELLelvgLEG-- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 145 dkefhyglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHDR 212
Cdd:COG3842 128 --------LADRYPhqlsgGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-210 |
4.69e-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: 59.94 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAE--PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGL------------KVG 67
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-GHdvrdytlaslrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 68 NLSQDQFAFEefsvvDAVimgdvelwkvkqeRERI-YSLPEMSEDDGMKVAEL---ESVFAEM-DGYtaesraEEILLEA 142
Cdd:cd03251 80 LVSQDVFLFN-----DTV-------------AENIaYGRPGATREEVEEAARAanaHEFIMELpEGY------DTVIGER 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 143 GIdkefhyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISH 210
Cdd:cd03251 136 GV----------KLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlVQAALERLMKNR-TTFVIAH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
322-498 |
4.80e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 322 VNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKDFDNDLTL 401
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 402 FDWMSQWRTAKHNDLM---VRGMLGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEAL- 477
Cdd:PRK09544 87 NRFLRLRPGTKKEDILpalKRVQAGHLI------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALy 160
|
170 180
....*....|....*....|....
gi 499648994 478 ---NNALKDFQGTLIFVSHDREFV 498
Cdd:PRK09544 161 dliDQLRRELDCAVLMVSHDLHLV 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-508 |
4.90e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.40 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW------SENAT-----FGYCP 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddveALSARaasrrVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 389 QDSTKDFDND------------LTLFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSnkkarnCSGGEKNRLLFGKLMMQD 456
Cdd:PRK09536 84 QDTSLSFEFDvrqvvemgrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTS------LSGGERQRVLLARALAQA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 457 VNVLVMDEPTNHMDM-EAIEALNNA--LKDFQGTLIFVSHDREfvssLATRIIDI 508
Cdd:PRK09536 158 TPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDLD----LAARYCDE 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-254 |
6.01e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQF-GAEPLfENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVgnlsqdQFAfeefSVVDA 84
Cdd:PRK11288 9 GIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-GQEM------RFA----STTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 85 VIMGDVELWkvkQErerIYSLPEMSeddgmkVAE------LESVFAEMDGYTAESRAEEILLEAGIDkefhyglmanVAP 158
Cdd:PRK11288 77 LAAGVAIIY---QE---LHLVPEMT------VAEnlylgqLPHKGGIVNRRLLNYEAREQLEHLGVD----------IDP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 GWKLRVL---------LAQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISH--DRHF-LNSVCTHMA 223
Cdd:PRK11288 135 DTPLKYLsigqrqmveIAKALARNARVIAFDEPTSSLSAREIEQLfrvIRELRAEGRVILYVSHrmEEIFaLCDAITVFK 214
|
250 260 270
....*....|....*....|....*....|..
gi 499648994 224 DidygelriypGNY-EKFLEAAGLQREQLLAE 254
Cdd:PRK11288 215 D----------GRYvATFDDMAQVDRDQLVQA 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-481 |
6.49e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.04 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCP----------- 388
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsiargllylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 389 QDSTKdfdNDLTLFDWMSQWRtAKHNDLMVRGMLGRLLFTADDsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNH 468
Cdd:cd03231 81 APGIK---TTLSVLENLRFWH-ADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|...
gi 499648994 469 MDMEAIEALNNAL 481
Cdd:cd03231 156 LDKAGVARFAEAM 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-230 |
7.87e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 16 LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglKVGNLSQDQFAfeefsvVDAVimgdvelwKV 95
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQ------IDAI--------KL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 96 KQERERIYS----LPEMSEDDgmKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGL---MANVAPGWKLRVLLAQ 168
Cdd:PRK14246 89 RKEVGMVFQqpnpFPHLSIYD--NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 169 ALFANPDILLLDEPTNNLDI---HTITWLANELnKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIvnsQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
339-533 |
1.20e-09 |
|
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: 58.89 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWS---------ENATFGYCPQDSTkdfdndltLFDWMS--- 406
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQNYA--------LFPHMTvyk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 407 --------QWRTAKHNDLMVR---GMLG--RLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA 473
Cdd:cd03299 91 niayglkkRKVDKKEIERKVLeiaEMLGidHLL------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 474 IEALNNALKD----FQGTLIFVSHDREFVSSLATRIIDIKDKQVIDFqGSFDEYLASCEEKKVA 533
Cdd:cd03299 165 KEKLREELKKirkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEEVFKKPKNEFVA 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
320-514 |
1.40e-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: 60.22 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLR--CLVDELKSLEGEVKWSENATFGYCPQDSTKD--- 394
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKASNIRDTERAgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 395 -FDNDLTLFDWMSQWRTA------------KHNDLMVR---GMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVN 458
Cdd:TIGR02633 82 iIHQELTLVPELSVAENIflgneitlpggrMAYNAMYLrakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 459 VLVMDEPTNHMDMEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
1.49e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAeplF---ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPG----LK 65
Cdd:COG3845 5 ALELRGITKRFGG---VvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvrirSPRdaiaLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 66 VGNLSQDqFA-FEEFSVVDAVIMGDVELWKV----KQERERIyslPEMSEDDGM------KVAELeSVfaemdgytaesr 134
Cdd:COG3845 82 IGMVHQH-FMlVPNLTVAENIVLGLEPTKGGrldrKAARARI---RELSERYGLdvdpdaKVEDL-SV------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 135 aeeilleagidkefhyglmanvapGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANElnkrKCTMII 207
Cdd:COG3845 145 ------------------------GEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRLAAE----GKSIIF 196
|
...
gi 499648994 208 ISH 210
Cdd:COG3845 197 ITH 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-219 |
1.96e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFeefsvvdavimgdvelwkVKQERERIYSLP 106
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY------------------VPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 107 EMSEDDGMKvaeleSVFAEMdGY--TAESRAEEILLEA--GID-KEFHYGLMANVAPGWKLRVLLAQALFANPDILLLDE 181
Cdd:PRK15056 95 VLVEDVVMM-----GRYGHM-GWlrRAKKRDRQIVTAAlaRVDmVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499648994 182 PTNNLDIHT---ITWLANELNKRKCTMIIISHDRHFLNSVC 219
Cdd:PRK15056 169 PFTGVDVKTearIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-211 |
2.14e-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: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 32 LIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQF----------AFEEF------SVVDAVIMGdVELWKV 95
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLID-GQDIAAMSRKELrelrrkkismVFQSFallphrTVLENVAFG-LEVQGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 96 -KQERERiyslpemseddgmkvaelesvfaemdgytaesRAEEILLEAGIdKEFHYGLMANVAPGWKLRVLLAQALFANP 174
Cdd:cd03294 133 pRAEREE--------------------------------RAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499648994 175 DILLLDEPTNNLDIHTITWLANEL----NKRKCTMIIISHD 211
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELlrlqAELQKTIVFITHD 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-525 |
2.20e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCL--VDELKSLEGEVKWSenatFGYCPQ-------- 389
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYH----VALCEKcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 ----------DSTKDFDNDLTLFDWMSQWRTAKHNDLM----------------VRGMLGRLLFTADDSNKKA------- 436
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygddtvldnVLEALEEIGYEGKEAVGRAvdliemv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 437 ----------RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNAL----KDFQGTLIFVSHDREFVSSLA 502
Cdd:TIGR03269 157 qlshrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|...
gi 499648994 503 TRIIDIKDKQVIDfQGSFDEYLA 525
Cdd:TIGR03269 237 DKAIWLENGEIKE-EGTPDEVVA 258
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-187 |
2.21e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV--------SITPGLKVGNLSQDQFA-F 76
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMFQSYAlF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 77 EEFSVVDAVIMGdvelwkVKQEReriysLPEmseddgmkvAELESVFAEMdgytaesraeeilLEAGIDKEFHYGLMANV 156
Cdd:PRK11607 104 PHMTVEQNIAFG------LKQDK-----LPK---------AEIASRVNEM-------------LGLVHMQEFAKRKPHQL 150
|
170 180 190
....*....|....*....|....*....|.
gi 499648994 157 APGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
2.36e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 58.93 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefs 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvDAVIMGDVElwkvkqERER-I------YSL-PEMSeddgmkVAE-----LEsvFAEMDGYTAESRAEEILLEAGIDke 147
Cdd:COG3839 63 --GGRDVTDLP------PKDRnIamvfqsYALyPHMT------VYEniafpLK--LRKVPKAEIDRRVREAAELLGLE-- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 148 fHYglmANVAPGwKL------RVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHD 211
Cdd:COG3839 125 -DL---LDRKPK-QLsggqrqRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-522 |
2.38e-09 |
|
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: 57.76 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGE--------VKWSEN--ATFGYCPQ 389
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 DSTkdFDNDLTLFD---WMSQWRTAKHNDLMVR-GMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEP 465
Cdd:cd03265 81 DLS--VDDELTGWEnlyIHARLYGVPGAERRERiDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 466 TNHMDMEA-------IEALNnalKDFQGTLIFVSHDREFVSSLATRIIdIKDKQVIDFQGSFDE 522
Cdd:cd03265 159 TIGLDPQTrahvweyIEKLK---EEFGMTILLTTHYMEEAEQLCDRVA-IIDHGRIIAEGTPEE 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-211 |
2.84e-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: 57.70 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGA-EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-------TPGL----KVGNL 69
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedireQDPVelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 70 SQDQFAFEEFSVVDAV-IMGDVELWKVKQERERIYSLPEMSeddGMKVAELesvfaeMDGYTAEsraeeilleagidkef 148
Cdd:cd03295 81 IQQIGLFPHMTVEENIaLVPKLLKWPKEKIRERADELLALV---GLDPAEF------ADRYPHE---------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 149 hyglmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT-------ITWLANELNKrkcTMIIISHD 211
Cdd:cd03295 136 -------LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITrdqlqeeFKRLQQELGK---TIVFVTHD 195
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-510 |
3.15e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDelksL----EGEVKWSENATFGYCPQ---------------- 389
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARPAGARVLFLPQrpylplgtlreallyp 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 DSTKDFDnDLTLFDWMSQwrtakhndlmVRgmLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHM 469
Cdd:COG4178 450 ATAEAFS-DAELREALEA----------VG--LGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499648994 470 DMEAIEALNNALKD--FQGTLIFVSHdREFVSSLATRIIDIKD 510
Cdd:COG4178 517 DEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTG 558
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-235 |
3.55e-09 |
|
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: 57.28 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 16 LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVS---------ITPGL---KVGNLSQDQFAFEEFSVvd 83
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilfngqpRKPDQfqkCVAYVRQDDILLPGLTV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 84 avimgdvelwkvkqeRERIY-----SLPEMSeDDGMKVAELESVfaemdgytaesraeeILLEAGIDKEFHYgLMANVAP 158
Cdd:cd03234 99 ---------------RETLTytailRLPRKS-SDAIRKKRVEDV---------------LLRDLALTRIGGN-LVKGISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHD-RHFLNSVCTHMADIDYGELrIYP 234
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTalnLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI-VYS 225
|
.
gi 499648994 235 G 235
Cdd:cd03234 226 G 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
334-511 |
3.61e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 334 LFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSenatfgyCPQDstkDFDNDLTLFDWMSQWRTAKh 413
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------VPDN---QFGREASLIDAIGRKGDFK- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 414 ndlMVRGMLGRL-LFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNALKDFQGTL 488
Cdd:COG2401 114 ---DAVELLNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITL 190
|
170 180
....*....|....*....|...
gi 499648994 489 IFVSHDREFVSSLATRIIDIKDK 511
Cdd:COG2401 191 VVATHHYDVIDDLQPDLLIFVGY 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
3.93e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.83 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 11 FGAEPLFeNISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITPGLKVGNLSQDQ------FAFEEF 79
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtLITSTSKNKDIKQIRkkvglvFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 SVVDAVIMGDVEL----WKVKQEReriyslpemseddgmkvaelesvfaemdgytAESRAEEILLEAGIDKEFHYGLMAN 155
Cdd:PRK13649 97 QLFEETVLKDVAFgpqnFGVSQEE-------------------------------AEALAREKLALVGISESLFEKNPFE 145
|
170 180 190
....*....|....*....|....*....|..
gi 499648994 156 VAPGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-211 |
4.52e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.51 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglkvgnlsqdqfafeefsvVDAVIMGDVELWKVKQER-----ER 101
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRRKKiamvfQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 102 IYSLPEMSEDDGMKVAelesvfAEMDGYTAESRAE---EILLEAGIDKEFHyGLMANVAPGWKLRVLLAQALFANPDILL 178
Cdd:PRK10070 115 FALMPHMTVLDNTAFG------MELAGINAEERREkalDALRQVGLENYAH-SYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 499648994 179 LDEPTNNLDIHTITWLANEL----NKRKCTMIIISHD 211
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
4.64e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.17 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS----QDQFAFE 77
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-GTDVSRLHardrKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 78 EF------SVVDAVIMGdvelWKVKQERERiyslPEMSEDDgMKVAELesvfAEMdgytaesraeeILLEagidkefHyg 151
Cdd:PRK10851 82 HYalfrhmTVFDNIAFG----LTVLPRRER----PNAAAIK-AKVTQL----LEM-----------VQLA-------H-- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 152 lMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTIT----WLANELNKRKCTMIIISHDR 212
Cdd:PRK10851 129 -LADRYPaqlsgGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-508 |
5.41e-09 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 58.45 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGG-DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENatfgycpqdSTKDFDN 397
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPvSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---------PLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 DltlfDWMSQWRTAKHNDLMVRG------MLGRLLFTADDSNKKARNC------------------------SGGEKNRL 447
Cdd:TIGR02857 392 D----SWRDQIAWVPQHPFLFAGtiaeniRLARPDASDAEIREALERAgldefvaalpqgldtpigeggaglSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 448 LFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF-QG-TLIFVSHDREfVSSLATRIIDI 508
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRLA-LAALADRIVVL 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-187 |
5.41e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvgnlSQDqfafeefsVVDAV 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID--------GED--------VTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 ImgdvelwkvkQERE-----RIYSL-PEMSEDD----GMKvaelesvfaeMDGYTAESRAEEI--LLE----AGIDKEFh 149
Cdd:PRK11432 75 I----------QQRDicmvfQSYALfPHMSLGEnvgyGLK----------MLGVPKEERKQRVkeALElvdlAGFEDRY- 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 499648994 150 yglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PRK11432 134 ---VDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
5.73e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.34 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVP---SAGNV-----SITPG----LKVGN 68
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVllngrRLTALpaeqRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 69 LSQDQFAFEEFSVVDAVIMGdvelwkvkqereriysLPEmseddGMKVAElesvfaemdgytAESRAEEILLEAGIDKef 148
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFA----------------LPP-----TIGRAQ------------RRARVEQALEEAGLAG-- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 149 hyglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHD 211
Cdd:COG4136 126 ----FADRDPatlsgGQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-218 |
6.12e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGalvpsagnvsITPglkVGNLSQD-QFAFEEF---SV 81
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG----------VYP---HGTYEGEiIFEGEELqasNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDAVIMGDV----ELWKVKQereriyslpemseddgMKVAelESVF--AE------MDGYTAESRAEEILLEAGID---- 145
Cdd:PRK13549 77 RDTERAGIAiihqELALVKE----------------LSVL--ENIFlgNEitpggiMDYDAMYLRAQKLLAQLKLDinpa 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 146 -KEFHYGLmanvapGWKLRVLLAQALFANPDILLLDEPTNNL---DIHTITWLANELNKRKCTMIIISHDrhfLNSV 218
Cdd:PRK13549 139 tPVGNLGL------GQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISHK---LNEV 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
6.25e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 11 FGAEPLFEnISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglKVGnlsqdqfafeefsvvDAVIMGDV 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVG---------------DIVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 91 ELWKVKQERERIYSLPEMSEDDGMKVAELESV-FAEMDGYTAESRAEEILLE----AGIDKEFHYGLMANVAPGWKLRVL 165
Cdd:PRK13643 75 KQKEIKPVRKKVGVVFQFPESQLFEETVLKDVaFGPQNFGIPKEKAEKIAAEklemVGLADEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499648994 166 LAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISH 210
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-210 |
6.37e-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: 56.46 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TPGL---------KVGNLSQDQFAFEEfSVV 82
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgIDIRdisrkslrsMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 83 DAVIMGD--------VELWKVKQERERIYSLPemseddgmkvaelesvfaemDGYtaesraEEILLEAGidkefhyglmA 154
Cdd:cd03254 95 ENIRLGRpnatdeevIEAAKEAGAHDFIMKLP--------------------NGY------DTVLGENG----------G 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKcTMIIISH 210
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEaleKLMKGR-TSIIIAH 196
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
1.12e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.73 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQF-GAEPLFE---NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQFA- 75
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDGQDLTALSEKELRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 --------FEEF------SVVDAVimgdvelwkvkqereriySLPemSEDDGMKVAELESvfaemdgytaesRAEEILLE 141
Cdd:PRK11153 80 arrqigmiFQHFnllssrTVFDNV------------------ALP--LELAGTPKAEIKA------------RVTELLEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 142 AGI-DKEFHYGlmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFLN 216
Cdd:PRK11153 128 VGLsDKADRYP--AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsILELLKDINRElGLTIVLITHEMDVVK 205
|
250
....*....|....
gi 499648994 217 SVCTHMADIDYGEL 230
Cdd:PRK11153 206 RICDRVAVIDAGRL 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-502 |
1.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.20 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLvDELKSLEGEVKWSENATF-------------- 384
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFfnqniyerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 385 ------------GYCPQDSTKDFDNDLTLFDWmsqwrtakHNDLMVRGMLGRLLFTAD-------DSNKKARNCSGGEKN 445
Cdd:PRK14258 86 lrrqvsmvhpkpNLFPMSVYDNVAYGVKIVGW--------RPKLEIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 446 RLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEAL--NNALKDfQGTLIFVSHDREFVSSLA 502
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLiqSLRLRS-ELTMVIVSHNLHQVSRLS 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
343-470 |
1.13e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 55.74 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 343 EAGAKLAVIGENGVGKTTFLR---CLVDELKSLEGEV----------KWSENatFGYCPQDSTkdFDNDLTLFD---WMS 406
Cdd:cd03234 31 ESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQIlfngqprkpdQFQKC--VAYVRQDDI--LLPGLTVREtltYTA 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 407 QWRTAKHNDLMVRGML---GRLLFTADDS--NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:cd03234 107 ILRLPRKSSDAIRKKRvedVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-188 |
1.47e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlSQDQFAFEEFSvvdavimgdvelwkVKQ 97
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---------DDHPLHFGDYS--------------YRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 98 ERER-IYSLPEMSEDDGMKVAELESV----FAEMDGYTAESRAEEILLEAGI--DKEFHYGLManVAPGWKLRVLLAQAL 170
Cdd:PRK15112 87 QRIRmIFQDPSTSLNPRQRISQILDFplrlNTDLEPEQREKQIIETLRQVGLlpDHASYYPHM--LAPGQKQRLGLARAL 164
|
170
....*....|....*...
gi 499648994 171 FANPDILLLDEPTNNLDI 188
Cdd:PRK15112 165 ILRPKVIIADEALASLDM 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-210 |
1.47e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 55.24 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITP-------GLKVGNL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqDITKlpmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 70 SQDQFAFEEFSVvdavimgdvelwkvkqeRERIYSLPEMSEDDGmkvAELESvfaemdgytaesRAEEILLEAGIDKefh 149
Cdd:cd03218 81 PQEASIFRKLTV-----------------EENILAVLEIRGLSK---KEREE------------KLEELLEEFHITH--- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 150 ygLMANVAP----GWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISH 210
Cdd:cd03218 126 --LRKSKASslsgGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-211 |
1.76e-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: 54.95 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeefsvvDAV 85
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI----------------------GGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 86 IMGDVElwkvKQERE-----RIYSL-PEMSEDDGMKVAeLESVFAEMDGYTAE-SRAEEILleaGIDKEFHYgLMANVAP 158
Cdd:cd03301 63 DVTDLP----PKDRDiamvfQNYALyPHMTVYDNIAFG-LKLRKVPKDEIDERvREVAELL---QIEHLLDR-KPKQLSG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK----RKCTMIIISHD 211
Cdd:cd03301 134 GQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqqrLGTTTIYVTHD 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
2.12e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 55.85 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 17 FENISAKFGNGNR-----------------YGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDqfafeef 79
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD-GVDLTALSER------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 svvdavimgdvELWKVkqeRERIyslpemseddGM-----------KVAE-----LEsvFAEMDGYTAESRAEEIL---- 139
Cdd:COG1135 76 -----------ELRAA---RRKI----------GMifqhfnllssrTVAEnvalpLE--IAGVPKAEIRKRVAELLelvg 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 140 LEagiDKEFHYglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISHDRHFL 215
Cdd:COG1135 130 LS---DKADAY--PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsILDLLKDINRElGLTIVLITHEMDVV 204
|
250
....*....|....*
gi 499648994 216 NSVCTHMADIDYGEL 230
Cdd:COG1135 205 RRICDRVAVLENGRI 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-526 |
2.20e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.92 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV-----------KWSENATFGYCPQDST----------KDFDN 397
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVLQDTFlfsgtimeniRLGRP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 DLTLFDWMSQWRTAKHNDLMVRgmLGRLLFTAddSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEAL 477
Cdd:cd03254 103 NATDEEVIEAAKEAGAHDFIMK--LPNGYDTV--LGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 478 NNAL-KDFQG-TLIFVSHdREFVSSLATRIIDIKDKQVIDfQGSFDEYLAS 526
Cdd:cd03254 179 QEALeKLMKGrTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGTHDELLAK 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-526 |
2.42e-08 |
|
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: 55.09 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRcLV---------DELKSLeGEVKWSEN-----ATF 384
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS-LItgdlpptygNDVRLF-GERRGGEDvwelrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 385 GYCPQDSTKDFDNDLT--------LFDWMSQWRTAKHNDLM-VRGMLGRL-LftADDSNKKARNCSGGEKNRLLFGKLMM 454
Cdd:COG1119 81 GLVSPALQLRFPRDETvldvvlsgFFDSIGLYREPTDEQRErARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 455 QDVNVLVMDEPTNHMDMEAIEALNNALKDF--QG--TLIFVSHDREFVSSLATRIIDIKDKQVIDfQGSFDEYLAS 526
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHHVEEIPPGITHVLLLKDGRVVA-AGPKEEVLTS 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
338-526 |
2.61e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 55.88 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 338 GDLLLEAGAKL------AVIGENGVGKTTFLRCLVDELKSLEGEVK-----W--SENATF--------GYCPQDStkdfd 396
Cdd:COG4148 12 GGFTLDVDFTLpgrgvtALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLqdSARGIFlpphrrriGYVFQEA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 397 ndlTLFDWMS--------QWRTAKHNDLM----VRGMLG--RLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVM 462
Cdd:COG4148 87 ---RLFPHLSvrgnllygRKRAPRAERRIsfdeVVELLGigHLL------DRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 463 DEPTNHMDMEA-------IEALNnalKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIDfQGSFDEYLAS 526
Cdd:COG4148 158 DEPLAALDLARkaeilpyLERLR---DELDIPILYVSHSLDEVARLADHVVLLEQGRVVA-SGPLAEVLSR 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-531 |
3.15e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.70 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATF------GycpqdstkdFDNDLTLFDwmsqwrtakhNd 415
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAllelgaG---------FHPELTGRE----------N- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 416 lmVRgMLGRLL-FTADDSNKKA-----------------RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME----A 473
Cdd:COG1134 109 --IY-LNGRLLgLSRKEIDEKFdeivefaelgdfidqpvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 474 IEALNNALKDfQGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGSFDE----YLASCEEKK 531
Cdd:COG1134 186 LARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLV-MDGDPEEviaaYEALLAGRE 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-232 |
3.40e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSgALVPSAGNVSITPGLKVGNlsqdQFAFEEfsv 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFN----QNIYER--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgDVELWKVKQERERIYSLPE---MSEDD----GMKVAELESVFaEMDGyTAESRAEEILLEAGIDKEFHYGLMa 154
Cdd:PRK14258 80 -------RVNLNRLRRQVSMVHPKPNlfpMSVYDnvayGVKIVGWRPKL-EIDD-IVESALKDADLWDEIKHKIHKSAL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGEL 230
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN 229
|
..
gi 499648994 231 RI 232
Cdd:PRK14258 230 RI 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-241 |
3.87e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.99 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLfeNISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPGL-KVGNLSQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalPPAErPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 72 DQFAFEEFSVVDAVIMGdvelwkvkqereriysLpemseDDGMKvaelesvfaemdgYTAESRA--EEILLEAGIdkefh 149
Cdd:COG3840 79 ENNLFPHLTVAQNIGLG----------------L-----RPGLK-------------LTAEQRAqvEQALERVGL----- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 150 YGLM----ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNK-RKCTMIIISHD----RHFlns 217
Cdd:COG3840 120 AGLLdrlpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrQEMLDLVDELCReRGLTVLMVTHDpedaARI--- 196
|
250 260
....*....|....*....|....
gi 499648994 218 vCTHMADIDYGELrIYPGNYEKFL 241
Cdd:COG3840 197 -ADRVLLVADGRI-AADGPTAALL 218
|
|
| 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 499648994 1 MISTANITMQF--GAEPLfENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--------TPGL-----K 65
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikydKKSLlevrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 66 VGNLSQ---DQ-FAFeefSVVDAVIMGDVELWKVKQERERiyslpemseddgmKVAE-LESVfaEMDGYTaesraeeill 140
Cdd:PRK13639 80 VGIVFQnpdDQlFAP---TVEEDVAFGPLNLGLSKEEVEK-------------RVKEaLKAV--GMEGFE---------- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 141 eagiDKEFHYglmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHD 211
Cdd:PRK13639 132 ----NKPPHH-----LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-506 |
4.23e-08 |
|
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: 54.01 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGE----MLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELK------SLEGEVKWSENATFGYCPQ 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 390 DSTkdfdndltLFdwmsQWRTAKHN---DLMVRGMLGRllftadDSNKKARNC-----------------SGGEKNRLLF 449
Cdd:cd03293 81 QDA--------LL----PWLTVLDNvalGLELQGVPKA------EARERAEELlelvglsgfenayphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 450 GKLMMQDVNVLVMDEPTNHMD----MEAIEALNNALKDFQGTLIFVSHDREFVSSLATRII 506
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVV 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-210 |
4.50e-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: 53.65 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 7 ITMQFGAEPLfeNISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSIT--------PGLK-VGNLSQDQFAFE 77
Cdd:cd03298 6 IRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaapPADRpVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 78 EFSVVDAVIMGDVELWKVK-QERERIyslpemseddgmkvaelesvfaemdgytaesraEEILLEAGIDkEFHYGLMANV 156
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKLTaEDRQAI---------------------------------EVALARVGLA-GLEKRLPGEL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 157 APGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNK-RKCTMIIISH 210
Cdd:cd03298 130 SGGERQRVALARVLVRDKPVLLLDEPFAALDPalrAEMLDLVLDLHAeTKMTVLMVTH 187
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-513 |
4.56e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenaTFGYCP----QDSTKDF 395
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPlaeaREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 396 DNDLTLFDWMS-----------QWRTAKHNDLMVRGMlgrllftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDE 464
Cdd:PRK11247 87 FQDARLLPWKKvidnvglglkgQWRDAALQALAAVGL-------ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 465 PTNHMD-MEAIE--ALNNALKDFQG-TLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:PRK11247 160 PLGALDaLTRIEmqDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-233 |
5.24e-08 |
|
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: 53.57 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAE--PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsqdqfafeef 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 svvDAVIMGDVELWKVkqeRERIYSLPemsEDDGMKVAELESVFAEMDGYTAESRAEEILLEAGidkefhyGLmaNVAPG 159
Cdd:cd03369 68 ---DGIDISTIPLEDL---RSSLTIIP---QDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEG-------GL--NLSQG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDrhfLNSV--CTHMADIDYGELRIY 233
Cdd:cd03369 130 QRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR---LRTIidYDKILVMDAGEVKEY 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
5.31e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.08 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKI------------------LSGALVPSAGNVSITPG 63
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 64 LKVGNLSQDQFAFEEFSVVDAVIMGdVELWKVKQERERiysLPEMSEDDGMKVAELESVFAEMDGYTAesraeeilleag 143
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKE---LDERVEWALKKAALWDEVKDRLNDYPS------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 144 idkefhyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELnKRKCTMIIISHDRHFLNSVCT 220
Cdd:PRK14267 149 -----------NLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSD 216
|
250 260
....*....|....*....|..
gi 499648994 221 HMADIDYGELrIYPGNYEKFLE 242
Cdd:PRK14267 217 YVAFLYLGKL-IEVGPTRKVFE 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-513 |
5.87e-08 |
|
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: 53.18 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYcPQDST-----------KDFD--NDLTLFDWMS-- 406
Cdd:cd03292 24 ISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRAIpylrrkigvvfQDFRllPDRNVYENVAfa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 407 -QWRTAKHNDLMVR-GMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF 484
Cdd:cd03292 103 lEVTGVPPREIRKRvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI 182
|
170 180 190
....*....|....*....|....*....|..
gi 499648994 485 Q--GTLIFVS-HDREFVSSLATRIIDIKDKQV 513
Cdd:cd03292 183 NkaGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
7.47e-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: 53.39 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI-------TPGLK--VGNLSQD 72
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnLPPHKrpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 QFAFEEFSVVDAVIMGdVELWKV-KQERERiyslpemseddgmKVAE-LESVfaEMDGYTAESRAEeilleagidkefhy 150
Cdd:cd03300 81 YALFPHLTVFENIAFG-LRLKKLpKAEIKE-------------RVAEaLDLV--QLEGYANRKPSQ-------------- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 151 glmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELnKR-----KCTMIIISHD 211
Cdd:cd03300 131 -----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL-KRlqkelGITFVFVTHD 190
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
7.73e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.87 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQF--GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGL------------KVG 67
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMvlseetvwdvrrQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 68 NLSQD---QFafeefsvVDAVIMGDVelwkvkqererIYSLpemsEDDGMKVAEL-ESVfaemdgytaESRAEEILLEAG 143
Cdd:PRK13635 85 MVFQNpdnQF-------VGATVQDDV-----------AFGL----ENIGVPREEMvERV---------DQALRQVGMEDF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 144 IDKEFHyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNkrkCTMIIISHD 211
Cdd:PRK13635 134 LNREPH-----RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKG---ITVLSITHD 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-237 |
7.79e-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: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKV------GNLSQDQFAFEEFSVVDAVIM------------GDV-E 91
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEildefrGSELQNYFTKLLEGDVKVIVKpqyvdlipkavkGKVgE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 92 LWKVKQERERIyslpemseDDGMKVAELESVfaemdgytaesraeeilLEAGIDkefhyglmaNVAPGWKLRVLLAQALF 171
Cdd:cd03236 110 LLKKKDERGKL--------DELVDQLELRHV-----------------LDRNID---------QLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 172 ANPDILLLDEPTNNLDIH---TITWLANELNKRKCTMIIISHDRhflnSVCTHMAD---IDYGElriyPGNY 237
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDL----AVLDYLSDyihCLYGE----PGAY 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-256 |
8.76e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 53.96 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpglkvgnlsqdqFAFEEFS 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL--------------WDGEPLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDavimgdvelwkvkqeRERI-YsLPemsEDDG----MKVAELESVFAEMDGYT---AESRAEEiLLEAgidkefhYGL 152
Cdd:COG4152 67 PED---------------RRRIgY-LP---EERGlypkMKVGEQLVYLARLKGLSkaeAKRRADE-WLER-------LGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 153 manvaPGW------KL------RVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRKCTMIIIS-HDrhfLNS 217
Cdd:COG4152 120 -----GDRankkveELskgnqqKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRelAAKGTTVIFSsHQ---MEL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499648994 218 V---CTHMADIDYGELRIYpGNYEKFLEAAGLQREQLLAENA 256
Cdd:COG4152 192 VeelCDRIVIINKGRKVLS-GSVDEIRRQFGRNTLRLEADGD 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
9.87e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 20 ISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITPGL------KVGNLSQDQ----FAFeefSVVDA 84
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrEVNAENekwvrsKVGLVFQDPddqvFSS---TVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 85 VIMGDVELwkvkqereriyslpemseddGMKVAELESvfaemdgytaesRAEEILLEAGIdKEFHYGLMANVAPGWKLRV 164
Cdd:PRK13647 101 VAFGPVNM--------------------GLDKDEVER------------RVEEALKAVRM-WDFRDKPPYHLSYGQKKRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499648994 165 LLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHD 211
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
1.03e-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: 54.75 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFG-AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGL-----------KVGNL 69
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 70 SQDQFAFEEfSVVDAVIMGdvelwkvkqereriySLPEMSEDDGMKVAELesvfaemdgytAESRAEEILLEAGIDKEFH 149
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLG---------------AKENVSQDEIWAACEI-----------AEIKDDIENMPLGYQTELS 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 150 YGlMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDihTIT---WLANELNKRKCTMIIISH 210
Cdd:TIGR01193 607 EE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD--TITekkIVNNLLNLQDKTIIFVAH 667
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-258 |
1.09e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQF-GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQdqfaFEEF 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSK----LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 SVVDAVIMGDVELWKVKQERERiySLPEMSEDDGMKVAELesvfaemdgytaESRAEEILLEAGIDKeFHYGLMANVAPG 159
Cdd:PRK13644 76 RKLVGIVFQNPETQFVGRTVEE--DLAFGPENLCLPPIEI------------RKRVDRALAEIGLEK-YRHRSPKTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 160 WKLRVLLAQALFANPDILLLDEPTNNLDIHT-ITWLAN--ELNKRKCTMIIISHDRHFLnsvctHMAD----IDYGELRI 232
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERikKLHEKGKTIVYITHNLEEL-----HDADriivMDRGKIVL 215
|
250 260 270
....*....|....*....|....*....|...
gi 499648994 233 yPGNYEKFLEAAGLQREQL-------LAENAKK 258
Cdd:PRK13644 216 -EGEPENVLSDVSLQTLGLtppslieLAENLKM 247
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-466 |
1.13e-07 |
|
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: 52.44 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIgHGFDGEM--LFsGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW-SENAT-----------FG 385
Cdd:cd03224 1 LEVENL-NAGYGKSqiLF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 386 YCPQDStkdfdndlTLFDWMsqwrTAKHNDLMVRGMLGRLLFTADD-------------SNKKARNCSGGEKNRLLFGKL 452
Cdd:cd03224 79 YVPEGR--------RIFPEL----TVEENLLLGAYARRRAKRKARLervyelfprlkerRKQLAGTLSGGEQQMLAIARA 146
|
170
....*....|....
gi 499648994 453 MMQDVNVLVMDEPT 466
Cdd:cd03224 147 LMSRPKLLLLDEPS 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-516 |
1.13e-07 |
|
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: 52.53 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCL--VDELKS----LEGEVKWSENATFGycpqdstkdFDNDLTLFDwmsqwrtakhND 415
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLagIYPPDSgtvtVRGRVSSLLGLGGG---------FNPELTGRE----------NI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 416 LMVRGMLG--------RLLFTADDS------NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD---ME-AIEAL 477
Cdd:cd03220 106 YLNGRLLGlsrkeideKIDEIIEFSelgdfiDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafQEkCQRRL 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 499648994 478 NNALKDfQGTLIFVSHDREFVSSLATRIIDIKDKQVIDF 516
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-226 |
1.19e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.39 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSA-GNVSITpglkvgnlsqdqfafeefsvvdavimgdvelw 93
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRIGMP-------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 94 kvkqERERIYSLPEMSeddgmkvaelesvfaemdgYTAESRAEEILLeagidkefhYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:cd03223 62 ----EGEDLLFLPQRP-------------------YLPLGTLREQLI---------YPWDDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 174 PDILLLDEPTNNLDIHTITWLANELNKRKCTMIIISHdRHFLNSVCTHMADID 226
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-230 |
1.23e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-------SITP-----GLKVGNLSQDQ 73
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddediSLLPlharaRRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 74 FAFEEFSVVDAvIMGDVELWKVKQERERiyslpemseddgmkvaelesvfaemdgytaESRAEEILleagidKEFHYGLM 153
Cdd:PRK10895 88 SIFRRLSVYDN-LMAVLQIRDDLSAEQR------------------------------EDRANELM------EEFHIEHL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 154 AN-----VAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADI 225
Cdd:PRK10895 131 RDsmgqsLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIV 210
|
....*
gi 499648994 226 DYGEL 230
Cdd:PRK10895 211 SQGHL 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-493 |
1.40e-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: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 348 LAVIGENGVGKTTFLRCLVDELKS--LEGEV--------KWSENATFGYCPQDstkdfdnDLTlfdwmsqwrtakHNDLM 417
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKIIGYVPQD-------DIL------------HPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 418 VRGMLgrlLFTAddsnkKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD-------MEAIEALNNalkdfQG-TLI 489
Cdd:cd03213 99 VRETL---MFAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRLAD-----TGrTII 165
|
....
gi 499648994 490 FVSH 493
Cdd:cd03213 166 CSIH 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-211 |
1.44e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.88 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVP-SAGNVSITpglkvgnlsqdqfafeefsvVDAVIMGDVEL 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPdDNPNSKIT--------------------VDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 93 WKVKQERERIYSLPEMS------EDDGMKVAELESV-FAEMDGYTAESRAEEILLEAgIDKEfhyglMANVAPGWKLRVL 165
Cdd:PRK13640 80 WDIREKVGIVFQNPDNQfvgatvGDDVAFGLENRAVpRPEMIKIVRDVLADVGMLDY-IDSE-----PANLSGGQKQRVA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499648994 166 LAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRK-CTMIIISHD 211
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPagkEQILKLIRKLKKKNnLTVISITHD 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
349-514 |
1.46e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 349 AVIGENGVGKTTFLRCLVDELKSLEGEVkWSENAT------------FGYCPQDSTKdfDNDLTLFDWMS---------- 406
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHiqhyaskevarrIGLLAQNATT--PGDITVQELVArgryphqplf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 407 -QWRTaKHNDLMVRGMlgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNAL 481
Cdd:PRK10253 114 tRWRK-EDEEAVTKAM--QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELN 190
|
170 180 190
....*....|....*....|....*....|...
gi 499648994 482 KDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK10253 191 REKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-229 |
1.54e-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: 54.06 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVP---------------SAGNVSITPGLKVGNLS 70
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPhgtwdgeiywsgsplKASNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 71 QDQFAFEEFSVVDAVIMGDvelwkvkqereriyslpEMSEDDGMkvaelesvfaeMDGYTAESRAEEILLEAGIDKEFHY 150
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGN-----------------EITLPGGR-----------MAYNAMYLRAKNLLRELQLDADNVT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 151 GLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDY 227
Cdd:TIGR02633 137 RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDiirDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
..
gi 499648994 228 GE 229
Cdd:TIGR02633 217 GQ 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-210 |
2.13e-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: 52.16 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLS----QDQFAFeefsvvdavimgdv 90
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLNlrwlRSQIGL-------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 91 elwkVKQE--------RERI-YSLPEMSEDDgmkvaelesvfaemdgytaesrAEEILLEAGIDK---EFHYGLMANVAP 158
Cdd:cd03249 82 ----VSQEpvlfdgtiAENIrYGKPDATDEE----------------------VEEAAKKANIHDfimSLPDGYDTLVGE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 159 -------GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNKRKC--TMIIISH 210
Cdd:cd03249 136 rgsqlsgGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
330-510 |
2.58e-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: 51.32 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWseNATFGYCPQ------DSTKD-------FD 396
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQepwiqnGTIREnilfgkpFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 397 N--------------DLTLFDwmsqwrtakHNDLMV---RGMlgrllftaddsnkkarNCSGGEKNRLLFGKLMMQDVNV 459
Cdd:cd03250 94 EeryekvikacalepDLEILP---------DGDLTEigeKGI----------------NLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 460 LVMDEP-------TNHMDMEaiEALNNALKDfQGTLIFVSHDREFVSSlATRIIDIKD 510
Cdd:cd03250 149 YLLDDPlsavdahVGRHIFE--NCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-231 |
2.61e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLS---QDQFAFEEFSVVDAVIMGdvelwkvkqeRERIY 103
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhQNMGYCPQFDAIDDLLTG----------REHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 104 SLPEMSeddGMKVAELESVfaemdgytAESRAEEILLEAGIDKefhygLMANVAPGWKLRVLLAQALFANPDILLLDEPT 183
Cdd:TIGR01257 2035 LYARLR---GVPAEEIEKV--------ANWSIQSLGLSLYADR-----LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 184 NNLDIHTITWLAN---ELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELR 231
Cdd:TIGR01257 2099 TGMDPQARRMLWNtivSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-505 |
2.81e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQfafeefs 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-GNPCARLTPAK------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 vvdAVIMGdveLWKVKQE---------RERI-YSLPEMSEDdgmkvaelesvfaemdgytaESRAEEILLEAG--IDKEF 148
Cdd:PRK15439 83 ---AHQLG---IYLVPQEpllfpnlsvKENIlFGLPKRQAS--------------------MQKMKQLLAALGcqLDLDS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 149 HYGLMaNVAPGWKLRVLlaQALFANPDILLLDEPTNNLDIHTITWL---ANELNKRKCTMIIISHDRHFLNSVCTHMADI 225
Cdd:PRK15439 137 SAGSL-EVADRQIVEIL--RGLMRDSRILILDEPTASLTPAETERLfsrIRELLAQGVGIVFISHKLPEIRQLADRISVM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 226 DYGELRIypgnyekfleaaglqreqllaenakkSAEIDELQDFVnRFGANASKAKQASSRAKKmdKIKLDEvksssrmsp 305
Cdd:PRK15439 214 RDGTIAL--------------------------SGKTADLSTDD-IIQAITPAAREKSLSASQ--KLWLEL--------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 306 slsfdEGKKMYRQA----LEVNKI-GHGFDgemlfsggDLLLE--AGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkW 378
Cdd:PRK15439 256 -----PGNRRQQAAgapvLTVEDLtGEGFR--------NISLEvrAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-M 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 379 SENATFG-------------YCPQD---STKDFDNDLT------LFDWMSQW-RTAKHNDLMVR--GMLGrLLFTadDSN 433
Cdd:PRK15439 322 LNGKEINalstaqrlarglvYLPEDrqsSGLYLDAPLAwnvcalTHNRRGFWiKPARENAVLERyrRALN-IKFN--HAE 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 434 KKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF--QGT-LIFVSHDREFVSSLATRI 505
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaQNVaVLFISSDLEEIEQMADRV 473
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
315-526 |
3.09e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 315 MYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATfgycpqDSTKD 394
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI------NLVRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 395 FDNDLTLFD--------------------W--MSQWRTAKHNDLMVRGM------------LGRLLFTADDSNKKARNCS 440
Cdd:PRK10619 75 KDGQLKVADknqlrllrtrltmvfqhfnlWshMTVLENVMEAPIQVLGLskqeareravkyLAKVGIDERAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 441 GGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAI-EALN--NALKDFQGTLIFVSHDREFVSSLATRIIDIKdKQVIDFQ 517
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIEEE 233
|
....*....
gi 499648994 518 GSFDEYLAS 526
Cdd:PRK10619 234 GAPEQLFGN 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
433-513 |
3.33e-07 |
|
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: 51.10 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 433 NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQ----GTLIFVSHDREFVSSLATRIIDI 508
Cdd:cd03301 125 DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrlgTTTIYVTHDQVEAMTMADRIAVM 204
|
....*
gi 499648994 509 KDKQV 513
Cdd:cd03301 205 NDGQI 209
|
|
| 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 499648994 132 ESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD----IHTITWLANELNKRKCTMII 207
Cdd:PRK15134 402 EQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLF 481
|
90
....*....|..
gi 499648994 208 ISHDRHFLNSVC 219
Cdd:PRK15134 482 ISHDLHVVRALC 493
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
317-528 |
3.88e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.86 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 317 RQALEVNKIGHGFDGE-MLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCL-----VDElksleGEVKW-----------S 379
Cdd:COG1132 337 RGEIEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLlrfydPTS-----GRILIdgvdirdltleS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 380 ENATFGYCPQDSTkdfdndltLFDwmsqwRTAKHNdlmVRgmLGRLlfTADDSN-----KKAR----------------- 437
Cdd:COG1132 412 LRRQIGVVPQDTF--------LFS-----GTIREN---IR--YGRP--DATDEEveeaaKAAQahefiealpdgydtvvg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 438 ----NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME---AI-EALNNALKDfqGTLIFVSHdRefVSSL--ATRIID 507
Cdd:COG1132 472 ergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTEteaLIqEALERLMKG--RTTIVIAH-R--LSTIrnADRILV 546
|
250 260
....*....|....*....|.
gi 499648994 508 IKDKQVIDfQGSFDEYLASCE 528
Cdd:COG1132 547 LDDGRIVE-QGTHEELLARGG 566
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
4.55e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.34 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQF-GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeef 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 svvdaVIMGDVELWKVKQERERIYSLPEMSEDDGMKVAELESVFA------EMDGYTAESRAEEILLEAGIDkEFHYGLM 153
Cdd:PRK13652 62 -----LIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIAfgpinlGLDEETVAHRVSSALHMLGLE-ELRDRVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGE 229
Cdd:PRK13652 136 HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
250 260
....*....|....*....|..
gi 499648994 230 LRIYPGNYEKFLEAAGLQREQL 251
Cdd:PRK13652 216 IVAYGTVEEIFLQPDLLARVHL 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
315-473 |
4.77e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.73 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 315 MYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTK- 393
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 394 ----DFDN---DLTLFDWMSQW-RTAKHNDLMVRGMLGRLLFTADDSNK---KARNCSGGEKNRLLFGKLMMQDVNVLVM 462
Cdd:PRK13537 83 gvvpQFDNldpDFTVRENLLVFgRYFGLSAAAARALVPPLLEFAKLENKadaKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170
....*....|.
gi 499648994 463 DEPTNHMDMEA 473
Cdd:PRK13537 163 DEPTTGLDPQA 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-224 |
4.80e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnLSQDQFAfeefsvvdaviMGDVELWKVKQERERIYSLP 106
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAW--------LGKDLLG-----------MKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 107 EMSEDDGMKVAE-----LESVFAEMDGYTAESRAEEILLEAgidkefhyGLMANV--------APGWKLRVLLAQALFAN 173
Cdd:PRK15079 108 LASLNPRMTIGEiiaepLRTYHPKLSRQEVKDRVKAMMLKV--------GLLPNLinryphefSGGQCQRIGIARALILE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 174 PDILLLDEPTNNLDIHTITWLANELNKRKCTM----IIISHDRhflnSVCTHMAD 224
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMglslIFIAHDL----AVVKHISD 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
324-492 |
5.45e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 324 KIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCL---VDELKSLEGEVKWS--ENATFG--------YCPQD 390
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNgiPYKEFAekypgeiiYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 391 STKDfdNDLTLFDWMSQWRTAKHNDlMVRGMlgrllftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:cd03233 92 DVHF--PTLTVRETLDFALRCKGNE-FVRGI------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|....*
gi 499648994 471 -MEAIEALN--NALKDFQGTLIFVS 492
Cdd:cd03233 151 sSTALEILKciRTMADVLKTTTFVS 175
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-275 |
5.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItpglkvgnlsQDQFAFEEFSVVDAVIMGDVELWK-VK 96
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV----------GDIYIGDKKNNHELITNPYSKKIKnFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 97 QERERI---YSLPE--MSEDDGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEF----HYGLmanvAPGWKLRVLLA 167
Cdd:PRK13631 113 ELRRRVsmvFQFPEyqLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlersPFGL----SGGQKRRVAIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 168 QALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKFLEAA 244
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPkgeHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499648994 245 GLQR------------EQLLAENAK-------KSAEIDELQDFVNRFGAN 275
Cdd:PRK13631 269 IINStsiqvprviqviNDLIKKDPKykklyqkQPRTIEQLADAINEFIKG 318
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-187 |
5.90e-07 |
|
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: 50.18 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 4 TANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGlkvgnlsqdqfafeefsvvd 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 84 avimgdvelwKVKQERERIY-SLPEMSEDDGMK--VAELESV-FAEMDGytAESRAEEILLEAGIdKEFHYGLMANVAPG 159
Cdd:cd03231 63 ----------PLDFQRDSIArGLLYLGHAPGIKttLSVLENLrFWHADH--SDEQVEEALARVGL-NGFEDRPVAQLSAG 129
|
170 180
....*....|....*....|....*...
gi 499648994 160 WKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-211 |
5.92e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.37 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV-----SITPGLKVGNLSQDQ------FAFEEFSVVDAVI 86
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyHITPETGNKNLKKLRkkvslvFQFPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 87 MGDVELwkvkqereriyslpemseddgmkvAELESVFAEMDgytAESRAEEILLEAGIDKEfhyglMANVAP-----GWK 161
Cdd:PRK13641 104 LKDVEF------------------------GPKNFGFSEDE---AKEKALKWLKKVGLSED-----LISKSPfelsgGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 162 LRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHD 211
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPegrKEMMQLFKDYQKAGHTVILVTHN 204
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-211 |
6.01e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILsgalvpsAGNVSITPG-LKVGNlsqdqfafeefsvvda 84
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI-------AGLEDITSGdLFIGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 85 VIMGDVELWK-----VKQEreriYSL-PEMSEDD----GMKVAELESvfAEMDGYTAEsrAEEIL-LEAGIDKEfhyglM 153
Cdd:PRK11000 65 KRMNDVPPAErgvgmVFQS----YALyPHLSVAEnmsfGLKLAGAKK--EEINQRVNQ--VAEVLqLAHLLDRK-----P 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANE---LNKR-KCTMIIISHD 211
Cdd:PRK11000 132 KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEisrLHKRlGRTMIYVTHD 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-509 |
8.53e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV-------KWSENATF----GYCPQdstkdFDND 398
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRFmaylGHLPG-----LKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 399 LTLFDWMS-----QWRTAKH---NDLMVRGMlgrllftADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:PRK13543 97 LSTLENLHflcglHGRRAKQmpgSALAIVGL-------AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499648994 471 MEAIEALNNALKDF---QGTLIFVSHDREFVSSLATRIIDIK 509
Cdd:PRK13543 170 LEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-224 |
8.82e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.22 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 20 ISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSAGNVSITpGLKVGNLSQDQFAfeefsvvdavimgdvelwkvkqeR 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN-GRPLSDWSAAELA-----------------------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 100 ERIY------SLPEM--------SEDDGMKVAELESVFAEMdgytaesrAEEILLEagiDKefhYGLMANVAPG--WKlR 163
Cdd:COG4138 70 HRAYlsqqqsPPFAMpvfqylalHQPAGASSEAVEQLLAQL--------AEALGLE---DK---LSRPLTQLSGgeWQ-R 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 164 VLLAQALF-----ANPD--ILLLDEPTNNLDIH----TITWLaNELNKRKCTMIIISHDrhfLNSVCTHmAD 224
Cdd:COG4138 135 VRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAqqaaLDRLL-RELCQQGITVVMSSHD---LNHTLRH-AD 201
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-210 |
9.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.79 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS-----ITPGLKVGNLSQDQ------FAFEEFSVVDAVIM 87
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervITAGKKNKKLKPLRkkvgivFQFPEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 88 GDvelwkvkqererIYSLPE---MSEDDgmkvaelesvfaemdgytAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRV 164
Cdd:PRK13634 105 KD------------ICFGPMnfgVSEED------------------AKQKAREMIELVGLPEELLARSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499648994 165 LLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRK-CTMIIISH 210
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPkgrKEMMEMFYKLHKEKgLTTVLVTH 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
9.34e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG--ALVPSA---GNVSITpglkvgnlSQDQFAf 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLD--------GQDIFK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 77 eefsvvdaviMGDVELWKVKQERERIYS-LPEMSEDD----GMKVAELESVFAEMdgytaESRAEEILLEAGIDKEFHYG 151
Cdd:PRK14247 75 ----------MDVIELRRRVQMVFQIPNpIPNLSIFEnvalGLKLNRLVKSKKEL-----QERVRWALEKAQLWDEVKDR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 152 LMA---NVAPGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELnKRKCTMIIISH 210
Cdd:PRK14247 140 LDApagKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpenTAKIESLFLEL-KKDMTIVLVTH 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-506 |
1.08e-06 |
|
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: 49.45 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenATFGYCPQDSTKDFDN-- 397
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-----IIDGLKLTDDKKNINElr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 --------DLTLFDWMsqwrTAKHNdLM-----VRGM-------LGRLLFT----ADDSNKKARNCSGGEKNRLLFGKLM 453
Cdd:cd03262 76 qkvgmvfqQFNLFPHL----TVLEN-ITlapikVKGMskaeaeeRALELLEkvglADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 454 MQDVNVLVMDEPTNHMDMEAIEALNNALKDF--QG-TLIFVSHDREFVSSLATRII 506
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-183 |
1.14e-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: 49.74 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 31 GLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQFA-------------FEEFSVVDAVIMGDVELWK--V 95
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-GRDITGLPPHERAragigyvpegrriFPELTVEENLLLGAYARRRakR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 96 KQERERIYSL-PemseddgmkvaelesVFAEMdgytAESRAeeilleagidkefhyGLMANvapGWKLRVLLAQALFANP 174
Cdd:cd03224 109 KARLERVYELfP---------------RLKER----RKQLA---------------GTLSG---GEQQMLAIARALMSRP 151
|
....*....
gi 499648994 175 DILLLDEPT 183
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
1.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAE------PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqf 74
Cdd:PRK13633 4 MIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 75 afeefsVVDAVIMGDVE-LWKVKQERERIYSLPemsedDGMKVA---ELESVFA-EMDGYTAE---SRAEEILLEAGIDK 146
Cdd:PRK13633 68 ------YVDGLDTSDEEnLWDIRNKAGMVFQNP-----DNQIVAtivEEDVAFGpENLGIPPEeirERVDESLKKVGMYE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 147 EFHYglmanvAP-----GWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTItwlaNELNKRK-CTMIIISH 210
Cdd:PRK13633 137 YRRH------APhllsgGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTI----KELNKKYgITIILITH 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
337-506 |
1.35e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 337 GGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCP--------------QDSTKDFDNDLTLF 402
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewravrsdiqmifQDPLASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 403 DWMSQWRTAKHNDL-------MVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMeAIE 475
Cdd:PRK15079 119 EIIAEPLRTYHPKLsrqevkdRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQ 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 499648994 476 A-LNNALKDFQG----TLIFVSHDREFVSSLATRII 506
Cdd:PRK15079 198 AqVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVL 233
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-520 |
1.53e-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: 49.14 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 349 AVIGENGVGKTTFLRCLvdelkslegevkwsENATFGYCPQDSTK-DFDNDLTlfdwMSQWRTAKhNDLMVRGMLGRL-- 425
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL--------------KYALTGELPPNSKGgAHDPKLI----REGEVRAQ-VKLAFENANGKKyt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 426 -----------LFT-ADDSNK----KARNCSGGEKN------RLLFGKLMMQDVNVLVMDEPTNHMDMEAIE-------A 476
Cdd:cd03240 87 itrslailenvIFChQGESNWplldMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaeiiE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499648994 477 LNNALKDFQgtLIFVSHDREFVSSLATRIIDIKDKQvidfQGSF 520
Cdd:cd03240 167 ERKSQKNFQ--LIVITHDEELVDAADHIYRVEKDGR----QKSR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
1.62e-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: 48.46 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFG--AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI--TPGLKVGNLSQDQfafe 77
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgVPVSDLEKALSSL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 78 eFSVVDavimgdvelwkvkqerERIYslpemseddgmkvaelesVFAEMdgytaesraeeilleagidkefhygLMANV- 156
Cdd:cd03247 77 -ISVLN----------------QRPY------------------LFDTT-------------------------LRNNLg 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 157 ---APGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISH 210
Cdd:cd03247 97 rrfSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqLLSLIFEVLKDK-TLIWITH 155
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-190 |
1.82e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNvsitpgLKVGN--LSQDQ----FAFEEF 79
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAGTapLAEARedtrLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 ------SVVDAVIMGDVELWKVKQEREriyslpemseddgmkvaeLESVfaemdgyTAESRAEEilleagidkefhygLM 153
Cdd:PRK11247 91 rllpwkKVIDNVGLGLKGQWRDAALQA------------------LAAV-------GLADRANE--------------WP 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT 190
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
330-514 |
2.12e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.35 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV------------KWSENATfGYCPQD------S 391
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKWVRSKV-GLVFQDpddqvfS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 392 TKDFDnDLTlFDWMSQWRTAKHNDLMVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD- 470
Cdd:PRK13647 95 STVWD-DVA-FGPVNMGLDKDEVERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDp 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499648994 471 ------MEAIEALNNALKdfqgTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK13647 172 rgqetlMEILDRLHNQGK----TVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-211 |
2.23e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSgALVPSAGNVSITPGLKVGNLSqdqfafeefsvvdavimgDVELWKVKQ 97
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVESQGGEIIFNGQRIDTLS------------------PGKLQALRR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 98 ERERIYSLPEMSEDD----GMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGLMANVAPGWKLRVLLAQALFAN 173
Cdd:PRK10261 402 DIQFIFQDPYASLDPrqtvGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALN 481
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499648994 174 PDILLLDEPTNNLDI----HTITWLANELNKRKCTMIIISHD 211
Cdd:PRK10261 482 PKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-515 |
2.54e-06 |
|
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: 48.52 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 349 AVIGENGVGKTTFLRCLVDELKSLEGevkwseNATF-GYcpqDSTKD----------FDNDLTLFDWMSQWRT----AKH 413
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAG------FATVdGF---DVVKEpaearrrlgfVSDSTGLYDRLTARENleyfAGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 414 NDLMVRGMLGRL------LFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNN---ALKDF 484
Cdd:cd03266 106 YGLKGDELTARLeeladrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREfirQLRAL 185
|
170 180 190
....*....|....*....|....*....|.
gi 499648994 485 QGTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:cd03266 186 GKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-210 |
2.89e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGN-----VSITPglKVGNLSQDQ------FAFEEFSVVDAVI 86
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgVDITD--KKVKLSDIRkkvglvFQYPEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 87 MGDVELWKVkqereriySLPEMSEDDGMKVAE-LESVFAEMDGYTAESRAEeilleagidkefhyglmanVAPGWKLRVL 165
Cdd:PRK13637 102 EKDIAFGPI--------NLGLSEEEIENRVKRaMNIVGLDYEDYKDKSPFE-------------------LSGGQKRRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499648994 166 LAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKR-KCTMIIISH 210
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHKEyNMTIILVSH 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-528 |
3.00e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.08 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenaTFGYCPQDSTK---------------D 394
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI------LFDGKPIDYSRkglmklresvgmvfqD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 395 FDNDL--------TLFDWMSQWRTAKHNDLMVRGMLGRLlFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPT 466
Cdd:PRK13636 91 PDNQLfsasvyqdVSFGAVNLKLPEDEVRKRVDNALKRT-GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 467 NHMD----MEAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVIdFQGSFDEYLASCE 528
Cdd:PRK13636 170 AGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKE 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
440-521 |
3.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNAL----KDFQGTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
....*.
gi 499648994 516 FQGSFD 521
Cdd:PRK13645 232 IGSPFE 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
339-510 |
3.48e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.10 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKD------------------FDNDLT 400
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysvayaaqkpwllnatVEENIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 401 LFDWMSQWRTAKHNDLMVRGMLGRLLFTADDSNKKAR--NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALN 478
Cdd:cd03290 101 FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 499648994 479 NA-----LKDFQGTLIFVSHDREFVSSlATRIIDIKD 510
Cdd:cd03290 181 QEgilkfLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-523 |
3.81e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.47 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCL--------------------VDELKSLEGEVKWS 379
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksagshiellgrtVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 380 ENATfGYCPQ-----DSTKDFDNDL-----------TLFDWMSQWRTAKHNDLMVR-GMlgrllftADDSNKKARNCSGG 442
Cdd:PRK09984 85 RANT-GYIFQqfnlvNRLSVLENVLigalgstpfwrTCFSWFTREQKQRALQALTRvGM-------VHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 443 EKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG----TLIFVSHDREFVSSLATRIIDIKDKQVIdFQG 518
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHVF-YDG 235
|
....*
gi 499648994 519 SFDEY 523
Cdd:PRK09984 236 SSQQF 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
409-514 |
3.86e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.72 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 409 RTAKHNDLMVRGMLGrllftaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF--QG 486
Cdd:PRK10535 121 RLLRAQELLQRLGLE------DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrdRG 194
|
90 100
....*....|....*....|....*....
gi 499648994 487 -TLIFVSHDREfVSSLATRIIDIKDKQVI 514
Cdd:PRK10535 195 hTVIIVTHDPQ-VAAQAERVIEIRDGEIV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-212 |
4.14e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.95 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 32 LIGANGCGKSTFMKILSGALVPSAGNV------------SITPGLK--VGNLSQDQFAFEEFSVVDAVIMgdvelwkvkq 97
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknREVPFLRrqIGMIFQDHHLLMDRTVYDNVAI---------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 98 ereriyslpemseddgmkvaelESVFAEMDGYTAESRAEEILLEAGI-DKEFHYGLmaNVAPGWKLRVLLAQALFANPDI 176
Cdd:PRK10908 103 ----------------------PLIIAGASGDDIRRRVSAALDKVGLlDKAKNFPI--QLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 499648994 177 LLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDR 212
Cdd:PRK10908 159 LLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-378 |
5.07e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.49 E-value: 5.07e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 499648994 330 DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW 378
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW 60
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-189 |
6.47e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 11 FGAEP--LFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnLSQDQFAF--EEFSVVDAVI 86
Cdd:PTZ00243 668 FELEPkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------WAERSIAYvpQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 87 MGDVeLWKVKQERERIYslpemsedDGMKVAELESVFAEMDGytaesRAEEILLEAGIdkefhyglmaNVAPGWKLRVLL 166
Cdd:PTZ00243 738 RGNI-LFFDEEDAARLA--------DAVRVSQLEADLAQLGG-----GLETEIGEKGV----------NLSGGQKARVSL 793
|
170 180
....*....|....*....|...
gi 499648994 167 AQALFANPDILLLDEPTNNLDIH 189
Cdd:PTZ00243 794 ARAVYANRDVYLLDDPLSALDAH 816
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
7.13e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 47.72 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG--ALVPsagNVSITpglkvgnlsqdqfafeef 79
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIP---GARVE------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 svvdavimGDVELwkvkqERERIYslpemseDDGMKVAELES----VF--------------------------AEMDGy 129
Cdd:COG1117 71 --------GEILL-----DGEDIY-------DPDVDVVELRRrvgmVFqkpnpfpksiydnvayglrlhgikskSELDE- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 130 taesRAEEILLEAGIDKEfhyglmanV-----APGWKL------RVLLAQALFANPDILLLDEPTNNLD-IHT--ITWLA 195
Cdd:COG1117 130 ----IVEESLRKAALWDE--------VkdrlkKSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTakIEELI 197
|
250
....*....|....*
gi 499648994 196 NELnKRKCTMIIISH 210
Cdd:COG1117 198 LEL-KKDYTIVIVTH 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-215 |
7.37e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 47.33 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 15 PLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGLKVGNLSQDQFAFEEFSVvdAVIMGDVELWK 94
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV--AYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 95 VKQERERIYSLPeMSEDDGMKVAELESVFAEMDGYTAESRAEeiLLEAGIdkefhyglmaNVAPGWKLRVLLAQALFANP 174
Cdd:cd03290 93 ATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTE--IGERGI----------NLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499648994 175 DILLLDEPTNNLDIHTITWLANE-----LNKRKCTMIIISHDRHFL 215
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
8.16e-06 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 46.69 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 13 AEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSItPGlKVGNLSQDQFAFEEfSVVDAVIMGdvel 92
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PG-SIAYVSQEPWIQNG-TIRENILFG---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 93 wkvKQERERIYslpemseDDGMKVAELESVFAEMDGytaesRAEEILLEAGIdkefhyglmaNVAPGWKLRVLLAQALFA 172
Cdd:cd03250 90 ---KPFDEERY-------EKVIKACALEPDLEILPD-----GDLTEIGEKGI----------NLSGGQKQRISLARAVYS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499648994 173 NPDILLLDEPTNNLDIHTITWLAN-----ELNKRKcTMIIISHDRHFL 215
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNK-TRILVTHQLQLL 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-506 |
8.99e-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: 45.83 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 345 GAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKwsenatfgycpqdstkdfdndltLFDwMSQWRTAKHNDLMVRGMLGR 424
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------YID-GEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 425 LLFTaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD---------MEAIEALNNALKDFQGTLIFVSHDR 495
Cdd:smart00382 58 KASG-----------SGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDE 126
|
170
....*....|.
gi 499648994 496 EFVSSLATRII 506
Cdd:smart00382 127 KDLGPALLRRR 137
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-514 |
9.45e-06 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 46.72 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFL------------RCLVDELKSLEGEVK-------WSENATFGY--CPQDSTKDFDN 397
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnliagfetpqsgRVLINGVDVTAAPPAdrpvsmlFQENNLFAHltVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 DLTLfdwMSQWRTAKHNDLMVRGMLGRLLftaddsnKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEA 473
Cdd:cd03298 98 GLKL---TAEDRQAIEVALARVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499648994 474 IEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-216 |
9.60e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSitpgLKVGNLSQDQFAFEE-- 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL----FERQSIKKDLCTYQKql 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 79 -FSVVDAVIMGDVELwkvkqeRERIYSLPEMSEDDgMKVAELESVFAemdgytaesraeeilLEAGIDkeFHYGLMANva 157
Cdd:PRK13540 77 cFVGHRSGINPYLTL------RENCLYDIHFSPGA-VGITELCRLFS---------------LEHLID--YPCGLLSS-- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 158 pGWKLRVLLAQALFANPDILLLDEPTNNLD---IHTITWLANELNKRKCTMIIISHDRHFLN 216
Cdd:PRK13540 131 -GQKRQVALLRLWMSKAKLWLLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLN 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
159-218 |
1.05e-05 |
|
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: 46.37 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK---RKCTMIIISHDRHFLNSV 218
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlreEGKSVLIITHYQRLLDYI 170
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-288 |
1.14e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpglkvGNLSqdqfafeeFSVVDAVIMGDVElwkvkqe 98
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK-----GSAA--------LIAISSGLNGQLT------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 99 reriyslpemseddGMKVAELESVfaeMDGYTAESRAE---EILLEAGIDKeFHYGLMANVAPGWKLRVLLAQALFANPD 175
Cdd:PRK13545 102 --------------GIENIELKGL---MMGLTKEKIKEiipEIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 176 ILLLDEPTNNLDiHTITWLA----NELNKRKCTMIIISHDRHFLNSVCTHMADIDYGELRIY------PGNYEKFL-EAA 244
Cdd:PRK13545 164 ILVIDEALSVGD-QTFTKKCldkmNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDEFLkKYN 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499648994 245 GLQREQLLAENAKKSAEIDE--LQDFVNRFGANASKAKQASSRAKK 288
Cdd:PRK13545 243 QMSVEERKDFREEQISQFQHglLQEDQTGRERKRKKGKKTSRKFKK 288
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
347-522 |
1.26e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.11 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 347 KLAVIGENGVGKTTFLRCLVDELKSLEGEVK------WSEN-----ATFGYCPQDS-------TKDFDNDLTLFDWMSQW 408
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepiTKENirevrKFVGLVFQNPddqifspTVEQDIAFGPINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 409 RTAKHNDLMVRGMLGrllfTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD----MEAIEALNNALKDF 484
Cdd:PRK13652 112 ETVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETY 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 499648994 485 QGTLIFVSHDREFVSSLATRIIdIKDKQVIDFQGSFDE 522
Cdd:PRK13652 188 GMTVIFSTHQLDLVPEMADYIY-VMDKGRIVAYGTVEE 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-267 |
1.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.15 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 19 NISAKfgNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfaFEEFSVVDAVIMGDVELWK---- 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-----------------LFDGKPIDYSRKGLMKLREsvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 95 VKQERERIYSLPEMSEDDGMKVAELESVFAEMdgytaESRAEEILLEAGI----DKEFHYglmanVAPGWKLRVLLAQAL 170
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIehlkDKPTHC-----LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 171 FANPDILLLDEPTNNLD---IHTITWLANELNKR-KCTMIIISHDRHFLNSVCTHMADIDYGELRIYPGNYEKFLEAAGL 246
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
250 260
....*....|....*....|.
gi 499648994 247 QREQLLAENAKKSAEIDELQD 267
Cdd:PRK13636 237 RKVNLRLPRIGHLMEILKEKD 257
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-376 |
1.44e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 46.69 E-value: 1.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV 376
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV 59
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-211 |
1.46e-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: 47.76 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 31 GLIGANGCGKSTFMKILSGaLVPSAGNVSITpGLKVGNLSQDQFafeefsvvdavimgdvelwkvKQERERI-------Y 103
Cdd:COG4172 316 GLVGESGSGKSTLGLALLR-LIPSEGEIRFD-GQDLDGLSRRAL---------------------RPLRRRMqvvfqdpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 104 -SL-PEMSEddGMKVAE-LESVFAEMDGYTAESRAEEILLEAGIDKEfhyglMANVAP-----GWKLRVLLAQALFANPD 175
Cdd:COG4172 373 gSLsPRMTV--GQIIAEgLRVHGPGLSAAERRARVAEALEEVGLDPA-----ARHRYPhefsgGQRQRIAIARALILEPK 445
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499648994 176 ILLLDEPTNNLDI---HTITWLANELNKR-KCTMIIISHD 211
Cdd:COG4172 446 LLVLDEPTSALDVsvqAQILDLLRDLQREhGLAYLFISHD 485
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-209 |
1.50e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.51 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALvpsagnvsitPGLKVGNLSQDQFAFEEFSVVDAVIMGDVelwKVKQ 97
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY----------PGKFEGNVFINGKPVDIRNPAQAIRAGIA---MVPE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 98 ERERIYSLPEMSEDDGMKVAELESvFAEMDGYTAEsrAEEILLEAGID----KEFHYGL-MANVAPGWKLRVLLAQALFA 172
Cdd:TIGR02633 344 DRKRHGIVPILGVGKNITLSVLKS-FCFKMRIDAA--AELQIIGSAIQrlkvKTASPFLpIGRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499648994 173 NPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIIS 209
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVgakYEIYKLINQLAQEGVAIIVVS 460
|
|
| 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 499648994 162 LRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKRKctMIIISHDRHFLNS 217
Cdd:cd03240 128 IRLALAETFGSNCGILALDEPTTNLDeenieesLAEIIEERKSQKNFQ--LIVITHDEELVDA 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
430-526 |
1.70e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.58 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 430 DDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM---EAIEALNNALKDfQGTLIFVSHDREFVSSLATRII 506
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVA 223
|
90 100
....*....|....*....|
gi 499648994 507 DIKDKQVIDFqGSFDEYLAS 526
Cdd:PRK14246 224 FLYNGELVEW-GSSNEIFTS 242
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
440-522 |
1.79e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.58 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM----EAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIdIKDKQVID 515
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII-VMNKGKCE 224
|
....*..
gi 499648994 516 FQGSFDE 522
Cdd:PRK13637 225 LQGTPRE 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-211 |
1.96e-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: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 17 FENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQdqfafeefsvvdavimgdvelwkvk 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-GKPVTRRSP------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 97 qeRERIyslpemseDDGMkvaelesvfaemdGYTAESRAEE-ILLEAGIdkefhyglMANVAPGWKL------RVLLAQA 169
Cdd:cd03215 70 --RDAI--------RAGI-------------AYVPEDRKREgLVLDLSV--------AENIALSSLLsggnqqKVVLARW 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499648994 170 LFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIISHD 211
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAkaeIYRLIRELADAGKAVLLISSE 163
|
|
| 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 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMII-ISHD 211
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTAIImITHD 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-506 |
2.05e-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: 45.12 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVnkigHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKW------------SENATFGY 386
Cdd:cd03215 4 VLEV----RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 387 CPQDSTKDfdndlTLFDWMSQWRTAkhndlmvrgMLGRLLftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPT 466
Cdd:cd03215 80 VPEDRKRE-----GLVLDLSVAENI---------ALSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499648994 467 NHMDMEAIEALNNALKDF--QGT-LIFVSHDREFVSSLATRII 506
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELadAGKaVLLISSELDELLGLCDRIL 175
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-212 |
2.33e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.86 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITpGLKVGNLSQDQ-------- 73
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENrhvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 74 -FA-FEEFSVVDAVIMGdVELWKV-KQE-RERIYslpemsedDGMKVAELESvfaemdgytaesraeeilleagidkefh 149
Cdd:PRK09452 94 sYAlFPHMTVFENVAFG-LRMQKTpAAEiTPRVM--------EALRMVQLEE---------------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 150 yglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRK--CTMIIISHDR 212
Cdd:PRK09452 137 ---FAQRKPhqlsgGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKlgITFVFVTHDQ 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-493 |
2.52e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCL-----VDELKSLEGEVK------WSENA----- 382
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRlfgrniYSPDVdpiev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 383 ------TFGY-CPQDSTKDFDNDLTLFDWMSQWRTAKHNDLMVRGMLGRLLF---TADDSNKKARNCSGGEKNRLLFGKL 452
Cdd:PRK14267 84 rrevgmVFQYpNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499648994 453 MMQDVNVLVMDEPTNHMD---MEAIEALNNALKDfQGTLIFVSH 493
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTH 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-296 |
2.78e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPGlKVGNLSQDQFAFEEfSVVDAVIMGDvelw 93
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG-SVAYVPQVSWIFNA-TVRENILFGS---- 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 94 kvKQERERIYslpemseddgmKVAELESVFAEMDGYTAESRAEeiLLEAGIdkefhyglmaNVAPGWKLRVLLAQALFAN 173
Cdd:PLN03232 704 --DFESERYW-----------RAIDVTALQHDLDLLPGRDLTE--IGERGV----------NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 174 PDILLLDEPTNNLDIHTITWLANELNK---RKCTMIIISHDRHFLNSVcTHMADIDYGELRiYPGNYEKFLEAAGLQREq 250
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMKdelKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK-EEGTFAELSKSGSLFKK- 835
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 251 lLAENAKK---SAEIDELQDFVNRFG----ANASKAKQASSRAKKMDK---IKLDE 296
Cdd:PLN03232 836 -LMENAGKmdaTQEVNTNDENILKLGptvtIDVSERNLGSTKQGKRGRsvlVKQEE 890
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-482 |
3.10e-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: 44.93 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVD--ELKSLEGEVKWS---ENATF----GYCPQdstkdfdNDLtlfdwmsqwrtak 412
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINgrpLDKNFqrstGYVEQ-------QDV------------- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 413 HND-LMVRGMLgrlLFTAddsnkKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALK 482
Cdd:cd03232 90 HSPnLTVREAL---RFSA-----LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-495 |
3.14e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVdELKSLEGE-----VKWSE------NATFGYCPQDS---TKDFDNDLTLFD-WMS 406
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEiqidgVSWNSvtlqtwRKAFGVIPQKVfifSGTFRKNLDPYEqWSD 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 407 Q--WRTAKHNDL--MVRGMLGRLLFTADDSNKKARNcsgGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALK 482
Cdd:TIGR01271 1321 EeiWKVAEEVGLksVIEQFPDKLDFVLVDGGYVLSN---GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
170
....*....|....
gi 499648994 483 D-FQGTLIFVSHDR 495
Cdd:TIGR01271 1398 QsFSNCTVILSEHR 1411
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
155-298 |
3.52e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 155 NVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTI-----TWLANELnkRKCTMIIISHDRHFLNSVcTHMADIDYGE 229
Cdd:PLN03130 740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGrqvfdKCIKDEL--RGKTRVLVTNQLHFLSQV-DRIILVHEGM 816
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 230 LRiYPGNYEKfLEAAGLQREQLLaENAKKSAEIDELQDFVNRFGANASKAKQASSRAKKMDKIKLDEVK 298
Cdd:PLN03130 817 IK-EEGTYEE-LSNNGPLFQKLM-ENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSK 882
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
3.54e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILS--GALVPsagNVSITPGLK------------- 65
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTITGSIVynghniysprtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 66 ------VGNLSQDQFAFEeFSVVDAVIMGdvelwkvkqerERIyslpemsedDGMKvaelesvfaemDGYTAESRAEEIL 139
Cdd:PRK14239 82 vdlrkeIGMVFQQPNPFP-MSIYENVVYG-----------LRL---------KGIK-----------DKQVLDEAVEKSL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499648994 140 LEAGIDKEFHYGLMAN---VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELN--KRKCTMIIISH 210
Cdd:PRK14239 130 KGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLglKDDYTMLLVTR 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-261 |
3.84e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.86 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSITPglKVGNLSQdQFAFEEFSV 81
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQ-QAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 VDAVIMGdvelwkvKQERERIYSlpemseddgmKVAELESVFAEMDGYTAESRAEeiLLEAGIdkefhyglmaNVAPGWK 161
Cdd:TIGR00957 716 RENILFG-------KALNEKYYQ----------QVLEACALLPDLEILPSGDRTE--IGEKGV----------NLSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 162 LRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL--------NKrkcTMIIISHDRHFL--NSVCTHMADIDYGELR 231
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpegvlkNK---TRILVTHGISYLpqVDVIIVMSGGKISEMG 843
|
250 260 270
....*....|....*....|....*....|....*.
gi 499648994 232 IYP------GNYEKFLEAAGLQREQLLAENAKKSAE 261
Cdd:TIGR00957 844 SYQellqrdGAFAEFLRTYAPDEQQGHLEDSWTALV 879
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-211 |
5.04e-05 |
|
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: 45.09 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 31 GLIGANGCGKSTFMKILSGALVPSAGNVsITPGLKVGnlSQDQFAFEEFSV-VDAVIMGDVelwkvkqerERIYSLPEMs 109
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVS--YKPQYIKADYEGtVRDLLSSIT---------KDFYTHPYF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 110 EDDGMKVAELESVfaemdgytaesraeeilleagIDKEfhyglMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH 189
Cdd:cd03237 96 KTEIAKPLQIEQI---------------------LDRE-----VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180
....*....|....*....|....*....
gi 499648994 190 -------TITWLAneLNKRKcTMIIISHD 211
Cdd:cd03237 150 qrlmaskVIRRFA--ENNEK-TAFVVEHD 175
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-216 |
5.68e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQF----GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGAlvpSAGNVSITPglkvgnlsqDQFAFEefsv 81
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTA---------DRMRFD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 82 vdavimgDVELWKVK-QERER--------IYSLPEMSEDDGMKVAEleSVFAEMDGYTAES-----------RAEEILLE 141
Cdd:PRK15093 72 -------DIDLLRLSpRERRKlvghnvsmIFQEPQSCLDPSERVGR--QLMQNIPGWTYKGrwwqrfgwrkrRAIELLHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 142 AGIDKefHYGLMAN----VAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMI-IISHDRH 213
Cdd:PRK15093 143 VGIKD--HKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqIFRLLTRLNQNNNTTIlLISHDLQ 220
|
...
gi 499648994 214 FLN 216
Cdd:PRK15093 221 MLS 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
345-506 |
5.78e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 345 GAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWsENATFGYCPQdstkdfdndltlfdwmsqwrtakHNDLmvrgmlgr 424
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQ-----------------------YIDL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 425 llftaddsnkkarncSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF----QGTLIFVSHDREFVSS 500
Cdd:cd03222 73 ---------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDY 137
|
....*.
gi 499648994 501 LATRII 506
Cdd:cd03222 138 LSDRIH 143
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
339-528 |
6.00e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEG-------------EVKWSENATFGycpqdstkdfDNDLTLFDWM 405
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETssvvirgsvayvpQVSWIFNATVR----------ENILFGSDFE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 406 SQ--WR----TAKHNDLMvrgmlgrlLFTADDSNK---KARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME-AIE 475
Cdd:PLN03232 707 SEryWRaidvTALQHDLD--------LLPGRDLTEigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 476 ALNNALKD-FQG-TLIFVSHDREFVsSLATRIIDIKDKqVIDFQGSFDEYLASCE 528
Cdd:PLN03232 779 VFDSCMKDeLKGkTRVLVTNQLHFL-PLMDRIILVSEG-MIKEEGTFAELSKSGS 831
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
339-526 |
6.13e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 339 DLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEG-------------EVKWSENATFGycpqdstkdfDNDL--TLFD 403
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvirgtvayvpQVSWIFNATVR----------DNILfgSPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 404 WMSQWR----TAKHNDLmvrgmlgRLLFTADDSNKKAR--NCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME-AIEA 476
Cdd:PLN03130 707 PERYERaidvTALQHDL-------DLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499648994 477 LNNALKD--FQGTLIFVSHDREFVSSLaTRIIDIKDKQVIDfQGSFDEYLAS 526
Cdd:PLN03130 780 FDKCIKDelRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE-EGTYEELSNN 829
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-209 |
7.08e-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: 7.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKCTMIIIS 209
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAkaeIYRLIRELAAEGKAVIVIS 451
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-211 |
7.76e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFE-----NISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAG-----NVSITPGLK----VGNLSQ 71
Cdd:PRK13645 11 NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgDYAIPANLKkikeVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 72 D---QFAFEEFSVVDAVIMGDVELWKVK--QERERIYSlpemseddgmKVAELESVFAEMDGYTAESRAEeilleagidk 146
Cdd:PRK13645 91 EiglVFQFPEYQLFQETIEKDIAFGPVNlgENKQEAYK----------KVPELLKLVQLPEDYVKRSPFE---------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 147 efhyglmanVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-------IHTITWLANELNKRkctMIIISHD 211
Cdd:PRK13645 151 ---------LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeedfINLFERLNKEYKKR---IIMVTHN 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
388-526 |
9.43e-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: 45.39 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 388 PQDSTKDFDNDLTLFDwmsqwRTAKHNDLMVRGMLGRLLFTAD------DSNKKARNCSGGEKNRL-LFGKLMMQDVNVL 460
Cdd:TIGR00630 437 SIREAHEFFNQLTLTP-----EEKKIAEEVLKEIRERLGFLIDvgldylSLSRAAGTLSGGEAQRIrLATQIGSGLTGVL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 461 -VMDEPT-------NHmdmEAIEALNNaLKDFQGTLIFVSHDREFVSSlATRIIDIKDK------QVIdFQGSFDEYLAS 526
Cdd:TIGR00630 512 yVLDEPSiglhqrdNR---RLINTLKR-LRDLGNTLIVVEHDEDTIRA-ADYVIDIGPGagehggEVV-ASGTPEEILAN 585
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
315-514 |
9.62e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 315 MYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCL--VDELKSLEGEVKWSENATFGYCPQDST 392
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 393 KD----FDNDLTLFDWMS---------QWRTAK--HNDLMVRG---MLGRLLFTAdDSNKKARNCSGGEKNRLLFGKLMM 454
Cdd:PRK13549 81 RAgiaiIHQELALVKELSvleniflgnEITPGGimDYDAMYLRaqkLLAQLKLDI-NPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 455 QDVNVLVMDEPTNHMDMEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
440-525 |
1.15e-04 |
|
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: 43.68 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM--EAI--EALNNALKDFqgTLIFVSHdRefVSSL--ATRIIDIKDKQV 513
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAesEKLvqEALDRAMKGR--TTIVIAH-R--LSTIrnADLIAVLQNGQV 215
|
90
....*....|..
gi 499648994 514 IDfQGSFDEYLA 525
Cdd:cd03249 216 VE-QGTHDELMA 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-187 |
1.25e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 5 ANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPS-------AGNVSIT-PGLK-VGNLSQDQFA 75
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftgtilANNRKPTkQILKrTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 76 FEEFSVVDAVIMgdVELWKvkqereriysLPE-MSEDDGMKVAEleSVFAEMdGYTaesRAEEILleagIDKEFHYGlma 154
Cdd:PLN03211 152 YPHLTVRETLVF--CSLLR----------LPKsLTKQEKILVAE--SVISEL-GLT---KCENTI----IGNSFIRG--- 206
|
170 180 190
....*....|....*....|....*....|...
gi 499648994 155 nVAPGWKLRVLLAQALFANPDILLLDEPTNNLD 187
Cdd:PLN03211 207 -ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-509 |
1.39e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.72 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 345 GAKLAVIGENGVGKTTFLRCLVDELKSLEGEV--------KWSENATFGYCPQDSTKDFD-----NDLTL---FDWMSQW 408
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQSEEVDWSfpvlvEDVVMmgrYGHMGWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 409 RTAK-HNDLMVRGMLGRLLFTaDDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEA---IEALNNALKDF 484
Cdd:PRK15056 113 RRAKkRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDE 191
|
170 180
....*....|....*....|....*
gi 499648994 485 QGTLIFVSHDREFVSSLATRIIDIK 509
Cdd:PRK15056 192 GKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-505 |
1.46e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 349 AVIGENGVGKTTFLRCLVDELKSLEG-------EVKWSENA---TFGYCPQDSTkdFDNDLT-----LFDWMSQWRTAKH 413
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGtvlvggkDIETNLDAvrqSLGMCPQHNI--LFHHLTvaehiLFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 414 NDLMVRGMLgrllftaDDS------NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG- 486
Cdd:TIGR01257 1038 AQLEMEAML-------EDTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSg 1110
|
170 180
....*....|....*....|
gi 499648994 487 -TLIFVSHDREFVSSLATRI 505
Cdd:TIGR01257 1111 rTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
438-514 |
1.50e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 438 NCSGGEKNRL-LFGKLMMqDVNVLVMDEPTNHMDMEAIEALNNALKDF--QG-TLIFVSHDREFVSSLATRIIDIKDKQV 513
Cdd:PRK13651 165 ELSGGQKRRVaLAGILAM-EPDFLVFDEPTAGLDPQGVKEILEIFDNLnkQGkTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
.
gi 499648994 514 I 514
Cdd:PRK13651 244 I 244
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-241 |
1.76e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 18 ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNV---------SITPGLKvGNLSQDQFAfeEFSVvdaVIMG 88
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrngevsviAISAGLS-GQLTGIENI--EFKM---LCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 89 dvelWKVKQERERiysLPEMSEddgmkvaelesvFAEMDgytaesraeeilleagidkEFHYGLMANVAPGWKLRVLLAQ 168
Cdd:PRK13546 115 ----FKRKEIKAM---TPKIIE------------FSELG-------------------EFIYQPVKKYSSGMRAKLGFSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 169 ALFANPDILLLDEPtnnLDIHTITWLANELNK------RKCTMIIISHDRHFLNSVCTHMADI------DYGELRIYPGN 236
Cdd:PRK13546 157 NITVNPDILVIDEA---LSVGDQTFAQKCLDKiyefkeQNKTIFFVSHNLGQVRQFCTKIAWIeggklkDYGELDDVLPK 233
|
....*
gi 499648994 237 YEKFL 241
Cdd:PRK13546 234 YEAFL 238
|
|
| 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 499648994 126 MDGYTAESRAEEILLEAGI-DKEFhyglMANVAP-----GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLAN 196
Cdd:COG4172 125 LSGAAARARALELLERVGIpDPER----RLDAYPhqlsgGQRQRVMIAMALANEPDLLIADEPTTALDVTVqaqILDLLK 200
|
90 100
....*....|....*....|....*....
gi 499648994 197 ELNKR-KCTMIIISHDrhfLNSVcTHMAD 224
Cdd:COG4172 201 DLQRElGMALLLITHD---LGVV-RRFAD 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
2.22e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.23 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 2 ISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILS--GALVPSAgnvsitpglkvgnLSQDQFAFEEF 79
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGF-------------RVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 80 SVVDavimGDVELWKVkqeRERI-------YSLPEMSEDDGMKVAELESVFAEMDGYTAESRAEEILLEAGIDKEFHYGL 152
Cdd:PRK14243 78 NLYA----PDVDPVEV---RRRIgmvfqkpNPFPKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSGL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 153 maNVAPGWKLRVLLAQALFANPDILLLDEPTNNLD-IHT--ITWLANELnKRKCTMIIISHD 211
Cdd:PRK14243 151 --SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTlrIEELMHEL-KEQYTIIIVTHN 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-505 |
2.26e-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: 42.99 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenaTFGycpqdstkdfDNDL 399
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI------LLD----------GKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 T-----------------LFDWMSQW-------RTAKHN----DLMVRGMLgRLLFTADDSNKKARNCSGGEKNRLLFGK 451
Cdd:cd03300 65 TnlpphkrpvntvfqnyaLFPHLTVFeniafglRLKKLPkaeiKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 452 LMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG----TLIFVSHDREFVSSLATRI 505
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
439-509 |
2.31e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 2.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499648994 439 CSGGEKNR----LLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDF---QGTLIFVSHDREFVsSLATRIIDIK 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 ... |
440-526 |
2.45e-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: 42.67 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQ----GTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
90
....*....|.
gi 499648994 516 FqGSFDEYLAS 526
Cdd:cd03295 217 V-GTPDEILRS 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
342-493 |
2.53e-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: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLvDELKSLEGEV--KWSENATFgYCPQ----------------DSTKDF-DNDLTLF 402
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRltKPAKGKLF-YVPQrpymtlgtlrdqiiypDSSEDMkRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 403 DWMSQWRTAKHNDLMVRGmlGRLLFTADDSNKkarnCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALK 482
Cdd:TIGR00954 553 DLEQILDNVQLTHILERE--GGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR 626
|
170
....*....|.
gi 499648994 483 DFQGTLIFVSH 493
Cdd:TIGR00954 627 EFGITLFSVSH 637
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-224 |
2.99e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.61 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 32 LIGANGCGKSTFMKILSGaLVPSAGNVSitpglkVGNLSQDQFAFEEFSVVDAvimgdvelWKVKQERErIYSLP----- 106
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIQ------FAGQPLEAWSAAELARHRA--------YLSQQQTP-PFAMPvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 107 EMSEDDGMKVAELESVFAEMdgytaesrAEEILLEagiDKefhYGLMANVAPG--WKlRVLLAQALF-----ANPD--IL 177
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEV--------AEALGLD---DK---LGRSVNQLSGgeWQ-RVRLAAVVLqvwpdINPAgqLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 178 LLDEPTNNLDIHTITWLaNELNKRKC----TMIIISHDrhfLNSVCTHmAD 224
Cdd:PRK03695 156 LLDEPMNSLDVAQQAAL-DRLLSELCqqgiAVVMSSHD---LNHTLRH-AD 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-207 |
3.04e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.39 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQFGAEPLFENISAKFGNGnRYGLI-GANGCGKSTFMKILSGALVPSAGNVsITPGLKVGNLSQDQFAFE-EFSVVD 83
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAG-EFKLItGPSGCGKSTLLKIVASLISPTSGTL-LFEGEDISTLKPEIYRQQvSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 84 AVIMGDVEL------WKVKQEReriyslPEMSE-DDGMKVAELesvfaemdgytaesraEEILLEAGIdkefhyglmANV 156
Cdd:PRK10247 90 PTLFGDTVYdnlifpWQIRNQQ------PDPAIfLDDLERFAL----------------PDTILTKNI---------AEL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499648994 157 APGWKLRVLLAQALFANPDILLLDEPTNNLDIHtitwlanelNKRKCTMII 207
Cdd:PRK10247 139 SGGEKQRISLIRNLQFMPKVLLLDEITSALDES---------NKHNVNEII 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-245 |
3.14e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 43.28 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 163 RVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELNKRKcTMIIISHDRHFLnsvcTHMADI---DYGELRIYpGN 236
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETerqILELLAEHAQNK-TVLMITHRLTGL----EQFDRIcvmDNGQIIEQ-GT 556
|
....*....
gi 499648994 237 YEKFLEAAG 245
Cdd:PRK11160 557 HQELLAQQG 565
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
315-510 |
3.21e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 315 MYRQALEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYCPQDSTKD 394
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 395 ----FDNDLTLFDWMSQWRTAKHNDLMVRGMLG--------------RLLFTAD---DSNKKARNCSGGEKNRLLFGKLM 453
Cdd:PRK09700 81 gigiIYQELSVIDELTVLENLYIGRHLTKKVCGvniidwremrvraaMMLLRVGlkvDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 454 MQDVNVLVMDEPTNHMDMEAIE---ALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKD 510
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDylfLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKD 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
440-516 |
3.57e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 42.31 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTLI---FVSHDREFVSSLATRIIDIKDKQVIDF 516
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
437-526 |
3.58e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.41 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 437 RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDfqgtlifVSHDR-EFV-----SSL--ATRIIDI 508
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGRtTFIiahrlSTVrnADRILVF 542
|
90
....*....|....*...
gi 499648994 509 KDKQVIDfQGSFDEYLAS 526
Cdd:PRK13657 543 DNGRVVE-SGSFDELVAR 559
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-210 |
3.76e-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: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 6 NITMQF--GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVSI------TPGL-----KVGNLSQD 72
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdisKIGLhdlrsRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 73 QFAFE-----------EFSvvdavimgDVELWKVKQE---RERIYSLPEMsedDGMKVAElesvfaemDGytaesraeei 138
Cdd:cd03244 87 PVLFSgtirsnldpfgEYS--------DEELWQALERvglKEFVESLPGG---LDTVVEE--------GG---------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 139 lleagidkefhyglmANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:cd03244 138 ---------------ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-58 |
3.96e-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: 41.89 E-value: 3.96e-04
10 20
....*....|....*....|....*...
gi 499648994 31 GLIGANGCGKSTFMKILSGALVPSAGNV 58
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSI 60
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
342-494 |
3.98e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 342 LEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSENATFGYcPQDSTKD--------FDN---------------- 397
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA-DPEAQKLlrqkiqivFQNpygslnprkkvgqile 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 398 -------DLTlfdwmSQWRTAKhndlmVRGMLGRLLFTADDSNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD 470
Cdd:PRK11308 117 epllintSLS-----AAERREK-----ALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180
....*....|....*....|....*....
gi 499648994 471 MeAIEA-LNNALKDFQGTL----IFVSHD 494
Cdd:PRK11308 187 V-SVQAqVLNLMMDLQQELglsyVFISHD 214
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-238 |
4.08e-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: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 27 GNRYGLIGANGCGKSTFMKILSGALVPSAGNVsitpglkvgnlsqdqfafeefsvvdAVIMGDVELWKVKQERERIYSLP 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------IYIDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 107 EMSEDDGMKvaelesvfaemdgytaesraeeilleagidkefhyglmanvapgwKLRVLLAQALFANPDILLLDEPTNNL 186
Cdd:smart00382 57 KKASGSGEL---------------------------------------------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499648994 187 DIHT---------ITWLANELNKRKCTMIIISHDRHFLNSvcthMADIDYGELRIYPGNYE 238
Cdd:smart00382 92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGP----ALLRRRFDRRIVLLLIL 148
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
440-525 |
4.35e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 41.92 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGK-LMMQDvNVLVMDEPTNHMDMEAIEALNNALKDFQGTLI---FVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK11124 143 SGGQQQRVAIARaLMMEP-QVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVE 221
|
90 100
....*....|....*....|.
gi 499648994 516 fQGS-----------FDEYLA 525
Cdd:PRK11124 222 -QGDascftqpqteaFKNYLS 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-210 |
4.87e-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: 41.38 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 12 GAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALvpsagnvsITPGLKvgnlsqdqfafeefsvvdavimGDVE 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR--------TGLGVS----------------------GEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 92 LWKVKQERERIYSLPEMSEDDGMKVAELeSVFaEMDGYTAESRaeeilleagidkefhyGLMAnvapGWKLRVLLAQALF 171
Cdd:cd03213 70 INGRPLDKRSFRKIIGYVPQDDILHPTL-TVR-ETLMFAAKLR----------------GLSG----GERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499648994 172 ANPDILLLDEPTNNLD-------IHTITWLANElnkrKCTMIIISH 210
Cdd:cd03213 128 SNPSLLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIH 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-524 |
5.21e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.84 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGFDGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVkwsenatfGYCPQDSTkdfdnDL 399
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQ-----LR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 400 TLFDwMSQ------WRTA---KHND------------------LMVRGM--LGRLLFTA--------------DDsnkKA 436
Cdd:PRK11701 74 DLYA-LSEaerrrlLRTEwgfVHQHprdglrmqvsaggnigerLMAVGArhYGDIRATAgdwlerveidaariDD---LP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 437 RNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMeAIEA-----LNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDK 511
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQArlldlLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250
....*....|...
gi 499648994 512 QVIDfQGSFDEYL 524
Cdd:PRK11701 229 RVVE-SGLTDQVL 240
|
|
| 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 499648994 32 LIGANGCGKSTFMKILSGALVPSAGNVSI 60
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-221 |
5.42e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.49 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 14 EPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGaLVPSA-GNVSITPGLKVGNLSQDQFafeefsvvdaVIMGDVel 92
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGsGRIARPAGARVLFLPQRPY----------LPLGTL-- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 93 wkvkqeRERI-YSLPEMSEDDgmkvAELESVFAEMD-GYTAEsRAEEillEAGIDKEFhyglmanvAPGWKLRVLLAQAL 170
Cdd:COG4178 443 ------REALlYPATAEAFSD----AELREALEAVGlGHLAE-RLDE---EADWDQVL--------SLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 171 FANPDILLLDEPTNNLDIHTITWLANELNKR--KCTMIIISHdRHFLNSVCTH 221
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDR 552
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
433-508 |
7.65e-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: 41.09 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 433 NKKARNCSGGEKNRL-LFGKLMMQDVNVL-VMDEPT----NHMDMEAIEALNNaLKDFQGTLIFVSHDREFVsSLATRII 506
Cdd:cd03270 132 SRSAPTLSGGEAQRIrLATQIGSGLTGVLyVLDEPSiglhPRDNDRLIETLKR-LRDLGNTVLVVEHDEDTI-RAADHVI 209
|
..
gi 499648994 507 DI 508
Cdd:cd03270 210 DI 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
154-209 |
7.76e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 7.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 154 ANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIIS 209
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakYEIYKLINQLVQQGVAIIVIS 462
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
153-228 |
8.94e-04 |
|
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: 40.38 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 153 MANVAPGWKLRVLLAQALFANPD--ILLLDEPTNNLDIHTITWLANELNK---RKCTMIIISHDRHFLNSvcthmAD--I 225
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlidLGNTVILIEHNLDVLSS-----ADwiI 159
|
...
gi 499648994 226 DYG 228
Cdd:cd03238 160 DFG 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-209 |
9.36e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 9.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499648994 164 VLLAQALFANPDILLLDEPTNNLD------IHTITwlaNELNKRKCTMIIIS 209
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDvgakyeIYTII---NELAAEGKGVIVIS 461
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
440-515 |
9.44e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.30 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQ----GTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
320-514 |
1.04e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 41.22 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 320 LEVNKIGHGF-DGEMLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEV-------KWSENA------TFG 385
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepiKYDKKSllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 386 YCPQDS-------TKDFD---NDLTLFDWMSQWRTAKHNDLMVRGMLGRllftaddSNKKARNCSGGEKNRLLFGKLMMQ 455
Cdd:PRK13639 82 IVFQNPddqlfapTVEEDvafGPLNLGLSKEEVEKRVKEALKAVGMEGF-------ENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 456 DVNVLVMDEPTNHMDMEAIEALNNALKDF--QG-TLIFVSHDREFVSSLATRIIDIKDKQVI 514
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
440-519 |
1.04e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGT----LIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
....
gi 499648994 516 fQGS 519
Cdd:PRK15134 507 -QGD 509
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
317-471 |
1.20e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.82 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 317 RQALEVNKIGHGFDGeMLFSGGDLL-----------LEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVKWSenATFG 385
Cdd:TIGR01271 414 KQNNKARKQPNGDDG-LFFSNFSLYvtpvlknisfkLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS--GRIS 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 386 YCPQDS------TKD---------------------FDNDLTLFdwmsqwrtaKHNDLMVRGMLGRLLftaddsnkkarn 438
Cdd:TIGR01271 491 FSPQTSwimpgtIKDniifglsydeyrytsvikacqLEEDIALF---------PEKDKTVLGEGGITL------------ 549
|
170 180 190
....*....|....*....|....*....|...
gi 499648994 439 cSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM 471
Cdd:TIGR01271 550 -SGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
440-500 |
1.22e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 440 SGGEKN------RLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNN----ALKDFQG--TLIFVSHDREFVSS 500
Cdd:PRK01156 803 SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSV 875
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-526 |
1.39e-03 |
|
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: 40.55 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG--TLIFVSHDREFVSSlATRIIDIKDKQVIDfQ 517
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-Q 217
|
....*....
gi 499648994 518 GSFDEYLAS 526
Cdd:cd03252 218 GSHDELLAE 226
|
|
| 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 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS 59
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
432-510 |
1.54e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.09 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 432 SNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQGTL----IFVSHDREFVSSLATRIID 507
Cdd:PRK09452 138 AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIVV 217
|
...
gi 499648994 508 IKD 510
Cdd:PRK09452 218 MRD 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-527 |
1.56e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 41.35 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 319 ALEVNKIGHGFDGE--MLFSGGDLLLEAGAKLAVIGENGVGKTTFLRCLVDELKSLEGEVK--------WSENA---TFG 385
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngqpiadYSEAAlrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 386 YCPQ------DSTKDfdnDLTLfdwmsqwrtAKHN-------DLMVRGMLGRLLftaddSNKKARNC---------SGGE 443
Cdd:PRK11160 418 VVSQrvhlfsATLRD---NLLL---------AAPNasdealiEVLQQVGLEKLL-----EDDKGLNAwlgeggrqlSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 444 KNRLLFGKLMMQDVNVLVMDEPTNHMDMEA-IEALNNALKDFQG-TLIFVSHDREFVSSLaTRIIDIKDKQVIDfQGSFD 521
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQIIE-QGTHQ 558
|
....*.
gi 499648994 522 EYLASC 527
Cdd:PRK11160 559 ELLAQQ 564
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
440-528 |
1.87e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVN--VLVMDEPT-------NHMDMEAIEALNNalkdfQG-TLIFVSHDREFVSsLATRIIDIK 509
Cdd:PRK00635 478 SGGEQERTALAKHLGAELIgiTYILDEPSiglhpqdTHKLINVIKKLRD-----QGnTVLLVEHDEQMIS-LADRIIDIG 551
|
90 100
....*....|....*....|....
gi 499648994 510 DKQVI-----DFQGSFDEYLASCE 528
Cdd:PRK00635 552 PGAGIfggevLFNGSPREFLAKSD 575
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.89e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.12 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 1 MISTANITMQFGAEPLF--ENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAG-----NVSITPGlkvgNLSQDQ 73
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynNQAITDD----NFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 74 ------FAFEEFSVVDAVIMGDV----ELWKVKQEreriyslpEMSEddgmKVAElesVFAEMDGYtaeSRAeeilleag 143
Cdd:PRK13648 83 khigivFQNPDNQFVGSIVKYDVafglENHAVPYD--------EMHR----RVSE---ALKQVDML---ERA-------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499648994 144 iDKEFHyglmaNVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIH---TITWLANELNKRK-CTMIIISHD 211
Cdd:PRK13648 137 -DYEPN-----ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDarqNLLDLVRKVKSEHnITIISITHD 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-255 |
1.95e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 40.98 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 13 AEPLFENISAkfgnGNRYGLIGANGCGKSTFMKILSGALvPSAGNVSITpGLKVGNLS------------QDQFAFEEfS 80
Cdd:PRK11174 366 AGPLNFTLPA----GQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKIN-GIELRELDpeswrkhlswvgQNPQLPHG-T 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 81 VVDAVIMGDvelwkvkqereriyslPEMSEDDGMKVAELesvfaemdgytaeSRAEEIL--LEAGIDKEFHYGlMANVAP 158
Cdd:PRK11174 439 LRDNVLLGN----------------PDASDEQLQQALEN-------------AWVSEFLplLPQGLDTPIGDQ-AAGLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISHDRHFLnsvcTHMADI---DYGELrIY 233
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQLEDL----AQWDQIwvmQDGQI-VQ 563
|
250 260
....*....|....*....|..
gi 499648994 234 PGNYEKFLEAAGLQREqLLAEN 255
Cdd:PRK11174 564 QGDYAELSQAGGLFAT-LLAHR 584
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
159-211 |
2.01e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 2.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKC-TMIIISHD 211
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVtiqAQIIELLLELQQKENmALVLITHD 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-218 |
2.21e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499648994 159 GWKLRVLLAQALFANPDILLLDEPTNNLDIHT---ITWLANELnKRKCTM--IIISHDrhfLNSV 218
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLREL-QQELNMglLFITHN---LSIV 220
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-216 |
2.44e-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: 40.80 E-value: 2.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499648994 162 LRVLLAQALFANPDILLLDEPTNNLDIHTITWLANEL--------NKRKCTMIIISHDRHFLN 216
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsQQRNFQLLVITHDEDFVE 1274
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
440-525 |
2.51e-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: 39.52 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME---AI-EALNNALKDfqGTLIFVSHDREFVSSlATRIIDIKDKQVID 515
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDTEserLVqAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
90
....*....|
gi 499648994 516 fQGSFDEYLA 525
Cdd:cd03251 217 -RGTHEELLA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
440-526 |
3.22e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.86 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDM----EAIEALNNALKDFQGTLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
90
....*....|.
gi 499648994 516 FqGSFDEYLAS 526
Cdd:PRK11144 210 F-GPLEEVWAS 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
433-493 |
3.22e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 39.51 E-value: 3.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 433 NKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDME---AIEALNNALKDfQGTLIFVSH 493
Cdd:PRK14247 141 DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEntaKIESLFLELKK-DMTIVLVTH 203
|
|
| 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 499648994 143 GIDKEFHYGlMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDIHTITWLANELNK--RKCTMIIISH 210
Cdd:PLN03232 1360 GLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAH 1428
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-49 |
3.77e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 3.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 499648994 6 NITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSG 49
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
422-506 |
4.05e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 39.63 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 422 LGRLLftaddsNKKARNCSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMD------MEA-IEALNnalKDFQGTLIFVSHD 494
Cdd:PRK11000 123 LAHLL------DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLH---KRLGRTMIYVTHD 193
|
90
....*....|..
gi 499648994 495 REFVSSLATRII 506
Cdd:PRK11000 194 QVEAMTLADKIV 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
435-510 |
4.25e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 38.70 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 435 KARN----CSGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG---TLIFVSHDREFVSSLATRIID 507
Cdd:PRK10908 130 KAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLT 209
|
...
gi 499648994 508 IKD 510
Cdd:PRK10908 210 LSD 212
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-58 |
4.74e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 4.74e-03
10 20
....*....|....*....|....*
gi 499648994 34 GANGCGKSTFMKILSGALVPSAGNV 58
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
440-522 |
5.75e-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: 38.47 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNALKDFQG----TLIFVSHDREFVSSLATRIIDIKDKQVID 515
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
....*..
gi 499648994 516 FqGSFDE 522
Cdd:cd03296 218 V-GTPDE 223
|
|
| 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 499648994 1 MISTANITMQFGAEPLFENISAKFGNGNRYGLIGANGCGKSTFMKILSGALVPSAGNVS 59
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL 59
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
440-504 |
7.89e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 38.22 E-value: 7.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499648994 440 SGGEKNRLLFGKLMMQDVNVLVMDEPTNHMDMEAIEALNNAL----KDFQGTLIFVSHDrefvSSLATR 504
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD----LQLAAR 212
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
162-211 |
8.36e-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: 37.34 E-value: 8.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499648994 162 LRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIISHD 211
Cdd:cd03227 88 LALILALASLKPRPLYILDEIDRGLDPrdgQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
149-209 |
8.44e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 8.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499648994 149 HYGLMANVAPGWKLRVLLAQALFANPDILLLDEPTNNLDI---HTITWLANELNKRKCTMIIIS 209
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVgakFEIYQLIAELAKKDKGIIIIS 448
|
|
| |
