|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-525 |
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: 718.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 4 TSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDYMVLD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 TVMMGNARLYEIMKEKEVIYAKEDFTDEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPEKVK 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 164 VLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFWYES 243
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 244 SQLLIRQMKEANKKKEEKIKELQEFISRFSANASKSKQATSRKRALEKIELDDIQPSSrKYPYIDFRPNREIGNEVLTVE 323
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRD-KTVEIRFPPPERLGKKVLELE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 324 GLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPLDSgSEFDNEYTIVE 403
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 404 WLTQYSDEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNGLVKF 483
Cdd:COG0488 399 ELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2124998340 484 PGVLLFSSRDHQIVQTTANRIMEIVPGGkLIDKITTYDEYLE 525
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGG-VREYPGGYDDYLE 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-530 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 665.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDYM 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEIMKEKEVIYAKEDFTDEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPE 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFW 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 241 YESSQLLIRQMKEANKKKEEKIKELQEFISRFSANASKSKQATSRKRALEKIELDDIQPSSRKYPYIDFRPNREIGNEVL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 321 TVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPLDSGSEFDNEYT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 401 IVEWLTQYSDEK-DVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNG 479
Cdd:PRK15064 401 LFDWMSQWRQEGdDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 480 LVKFPGVLLFSSRDHQIVQTTANRIMEIVPGGkLIDKITTYDEYLESDEMA 530
Cdd:PRK15064 481 LEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRSQGIE 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-493 |
2.29e-93 |
|
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: 295.69 E-value: 2.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDYMVLDTVMMGNAR 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 92 LYEIMKEKEVIYAKedFTDED------GIKASELEGEFAAMNGWEAESDAATLLNGLGIDAElhDKAMKDLNGPEKVKVL 165
Cdd:TIGR03719 96 IKDALDRFNEISAK--YAEPDadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFWYESSQ 245
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 246 LLIRQMKEANKKKEEKIKELQEFIsRFSAnasKSKQATSRKR--ALEKIELDDIQ-PSSRKYPYIDfrPNREIGNEVLTV 322
Cdd:TIGR03719 252 KRLEQEEKEESARQKTLKRELEWV-RQSP---KGRQAKSKARlaRYEELLSQEFQkRNETAEIYIP--PGPRLGDKVIEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 323 EGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYfpLD-SGSEFDNEYTI 401
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAY--VDqSRDALDPNKTV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 402 VEWLTQYSDEKDVTYV----RGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALN 477
Cdd:TIGR03719 404 WEEISGGLDIIKLGKReipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALE 483
|
490
....*....|....*.
gi 2124998340 478 NGLVKFPGVLLFSSRD 493
Cdd:TIGR03719 484 EALLNFAGCAVVISHD 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-493 |
2.39e-87 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 280.08 E-value: 2.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDYMVLDTVMMGNAR 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 92 LYEIMKEKEVIYAK--EDFTDEDGIKA--SELEGEFAAMNGWEAES------DAATLLNGlgidaelhDKAMKDLNGPEK 161
Cdd:PRK11819 98 VKAALDRFNEIYAAyaEPDADFDALAAeqGELQEIIDAADAWDLDSqleiamDALRCPPW--------DAKVTKLSGGER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFWY 241
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 242 ESSQLLIRQMKEANKKKEEKIKELQEFIsRFSANA--SKSK---------QATSRKRALEKIELdDIQPSSRkypyidfr 310
Cdd:PRK11819 250 EQKAKRLAQEEKQEAARQKALKRELEWV-RQSPKArqAKSKarlaryeelLSEEYQKRNETNEI-FIPPGPR-------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 311 pnreIGNEVLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYfpLD 390
Cdd:PRK11819 320 ----LGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAY--VD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 391 -SGSEFDNEYTIVEwltQYSDEKDVTYV-------RGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLD 462
Cdd:PRK11819 394 qSRDALDPNKTVWE---EISGGLDIIKVgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
490 500 510
....*....|....*....|....*....|.
gi 2124998340 463 EPTNHLDMESITALNNGLVKFPGVLLFSSRD 493
Cdd:PRK11819 471 EPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-501 |
1.86e-75 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 251.02 E-value: 1.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDYM 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEIMKEKEVIYAK--EDFTDEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAelhDKAMKDLNG 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLveTDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP---DAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 239 FWYESSQLLIRQMKEANKKKEEKIKELQEFIsRFSANASKSKQaTSRKRALE----------------KIELDDiqpSSR 302
Cdd:PRK11147 240 QYLLEKEEALRVEELQNAEFDRKLAQEEVWI-RQGIKARRTRN-EGRVRALKalrrerserrevmgtaKMQVEE---ASR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 303 KypyidfrpnreiGNEVLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTT 382
Cdd:PRK11147 315 S------------GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 383 SQAYFplDS-GSEFDNEYTIVEWLTQysDEKDVT------YVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISG 455
Cdd:PRK11147 383 EVAYF--DQhRAELDPEKTVMDNLAE--GKQEVMvngrprHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKP 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2124998340 456 ANVLLLDEPTNHLDMESITALNNGLVKFPGVLLFSSRDHQIVQTTA 501
Cdd:PRK11147 459 SNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTV 504
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-543 |
8.15e-75 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 249.32 E-value: 8.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDdYM 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP-QP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEImkEKEVIYAKEDftdEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPE 160
Cdd:PRK10636 80 ALEYVIDGDREYRQL--EAQLHDANER---NDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFW 240
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 241 YESSQLLIRQMKEANKKKEEKIKELQEFISRFSANASKSKQATSRKRALEKIELddIQPSSRKYPY-IDFRPNREIGNEV 319
Cdd:PRK10636 235 EVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLPNPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPLDSGSEFDNEY 399
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 TIVEWLTQYSDEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNG 479
Cdd:PRK10636 393 SPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 480 LVKFPGVLLFSSRDHQIVQTTANRIMEIVPG------GKLIDkittYDEYL--------ESDEMARKRQTYSIQSEED 543
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLLRSTTDDLYLVHDGkvepfdGDLED----YQQWLsdvqkqenQTDEAPKENNANSAQARKD 546
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-523 |
1.18e-64 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 223.58 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSgqLEPSKGdviITPGERLSFLQQDHFQyDDYMV 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG---IPKNCQILHVEQEVVG-DDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMMGNARLYEIMKEKEVIYAKEDFTDEDGIKA-------------------SELEGEFAAMNGWEAESDAATLLNGL 142
Cdd:PLN03073 252 LQCVLNTDIERTQLLEEEAQLVAQQRELEFETETGkgkgankdgvdkdavsqrlEEIYKRLELIDAYTAEARAASILAGL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 143 GIDAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQI 222
Cdd:PLN03073 332 SFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 223 ADIDYGKIKLYAGNYDFWYESSQLLIRQMKEANKKKEEKIKELQEFISRFSANASKSKQATSRKRALEKIELDDIQPSSR 302
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDP 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 303 KYPYIDFRPNREIGNEVLTVEGLSKTIDGEKIL-DDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVT 381
Cdd:PLN03073 492 DYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 382 TSQAYFPLDSGSEFDNEYTIVEWLTQYSDEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:PLN03073 572 VRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 462 DEPTNHLDMESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMeIVPGGKLIDKITTYDEY 523
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELW-VVSEGKVTPFHGTFHDY 712
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-242 |
1.12e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 187.19 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDym 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDP-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgNARLYEIMKEkeviyAKEDFTdedgikaselegefaamngweaESDAATLLNGLGIDAELHDKAMKDLNGPE 160
Cdd:COG0488 393 --------DKTVLDELRD-----GAPGGT----------------------EQEVRGYLGRFLFSGDDAFKPVGVLSGGE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFW 240
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
..
gi 2124998340 241 YE 242
Cdd:COG0488 518 LE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-511 |
1.14e-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: 167.63 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPldsgsefdney 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 tivewltQysdekdvtyvrgflgrmlfsgedgvkkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNG 479
Cdd:cd03221 70 -------Q------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 2124998340 480 LVKFPGVLLFSSRDHQIVQTTANRIMEIVPGG 511
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-229 |
2.85e-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: 166.86 E-value: 2.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQdhfqyddymv 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmmgnarlyeimkekeviyakedftdedgikaselegefaamngweaesdaatllnglgidaelhdkamkdLNGPEK 161
Cdd:cd03221 71 --------------------------------------------------------------------------LSGGEK 76
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:cd03221 77 MRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
2.17e-36 |
|
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: 135.94 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGE---RLSFL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQDHFQYDDYMVLDTVMMGnaRlyeimkekeviyakedftdedgikaselegeFAAMNGWEAESD-----AATLLNGLGI 144
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG--R-------------------------------YPHLGLFGRPSAedreaVEEALERTGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 145 dAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHDryfLN---K 217
Cdd:COG1120 128 -EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNlaaR 203
|
250
....*....|...
gi 2124998340 218 VCTQIADIDYGKI 230
Cdd:COG1120 204 YADRLVLLKDGRI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-534 |
1.89e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 139.04 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 322 VEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwgVTTSQ----AYFPLDSgsEFDN 397
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE----VSIPKglriGYLPQEP--PLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 398 EYTIVEW-------LTQYSDEKDVTY-------------------------------VRGFLGRMLFSGEDGVKKVKVLS 439
Cdd:COG0488 75 DLTVLDTvldgdaeLRALEAELEELEaklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 440 GGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMEIVPGgklidKITT 519
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRG-----KLTL 229
|
250
....*....|....*....
gi 2124998340 520 ----YDEYLESDEMARKRQ 534
Cdd:COG0488 230 ypgnYSAYLEQRAERLEQE 248
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-242 |
1.07e-34 |
|
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: 130.75 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflQQDHFQYDDYM 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI---------DGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLD--TVMMGNARLYEIMKEKEVIyakedftdedgikasELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAmKDLNG 158
Cdd:COG4555 72 ARRqiGVLPDERGLYDRLTVRENI---------------RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-GELST 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDRYFLNKVCTQIADIDYGKIkLYAG 235
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV-VAQG 214
|
....*..
gi 2124998340 236 NYDFWYE 242
Cdd:COG4555 215 SLDELRE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
4.40e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.25 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII----------TPGERLSFLQQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 72 DHFQYDDYMVLDTVMMgNARLYEimkekeviyakedftdedgikaselegefaaMNGWEAESDAATLLNGLGIDAELHDK 151
Cdd:COG1131 81 EPALYPDLTVRENLRF-FARLYG-------------------------------LPRKEARERIDELLELFGLTDAADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 152 AmKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKVCTQIADIDYG 228
Cdd:COG1131 129 V-GTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
..
gi 2124998340 229 KI 230
Cdd:COG1131 208 RI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
4.50e-30 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 115.96 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII---TPGERLSFLQQdHFQYdd 78
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkDIKKEPEEVKR-RIGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 ymvldtvMMGNARLYEimkekeviyakedftdedgikaselegefaAMNGWEaesdaatllnglgidaelhdkaMKDLNG 158
Cdd:cd03230 78 -------LPEEPSLYE------------------------------NLTVRE----------------------NLKLSG 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:cd03230 99 GMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
5.01e-30 |
|
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: 116.81 E-value: 5.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQyddym 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPIRDAREDYRR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgnarlyeimkekEVIYAkedfTDEDGIKAsELEGE-----FAAMNGWEA-ESDAATLLNGLGIdAELHDKAMK 154
Cdd:COG4133 76 -------------------RLAYL----GHADGLKP-ELTVRenlrfWAALYGLRAdREAIDEALEAVGL-AGLADLPVR 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 155 DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFL 215
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
3.80e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII------TPGERLSFLQQdHF 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 75 QYDDYM---VLDTVMMGNARLYEIMKekevIYAKEDftdedgikaselegefaamngWEAesdAATLLNGLGIdAELHDK 151
Cdd:COG1121 85 EVDWDFpitVRDVVLMGRYGRRGLFR----RPSRAD---------------------REA---VDEALERVGL-EDLADR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 152 AMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKVCTQIA 223
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-218 |
3.75e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 3 STSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITP------GERLSFLQQdHFQY 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 DDYM---VLDTVMMGNARLYEIMKekevIYAKEDFtdedgikaselegefaamngweaeSDAATLLNGLGIdAELHDKAM 153
Cdd:cd03235 80 DRDFpisVRDVVLMGLYGHKGLFR----RLSKADK------------------------AKVDEALERVGL-SELADRQI 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIawlEEFLINFDN------TVIVVSHDryfLNKV 218
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ---EDIYELLRElrregmTILVVTHD---LGLV 195
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-229 |
8.06e-28 |
|
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: 110.63 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 3 STSNITLRV--GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItPGERLSFLQQDH------- 73
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-DGKDLTKLSLKElrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 -FQY-DDYMVLDTVmmgnarlyeimkEKEVIYAKEDFtdedGIKASELEGEfaamngweaesdAATLLNGLGIDaELHDK 151
Cdd:cd03225 80 vFQNpDDQFFGPTV------------EEEVAFGLENL----GLPEEEIEER------------VEEALELVGLE-GLRDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 152 AMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDRYFLNKVCTQIADIDYG 228
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
.
gi 2124998340 229 K 229
Cdd:cd03225 211 K 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-237 |
1.17e-27 |
|
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: 116.96 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDD--- 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPnkt 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 -YMV----LDTVMMGNarlYEIMKEKEViyakedftdedgikaseleGEFaamngweaesdaatllNGLGIDAElhdKAM 153
Cdd:TIGR03719 403 vWEEisggLDIIKLGK---REIPSRAYV-------------------GRF----------------NFKGSDQQ---KKV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQI-ADIDYGKIKL 232
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHIlAFEGDSHVEW 521
|
....*
gi 2124998340 233 YAGNY 237
Cdd:TIGR03719 522 FEGNF 526
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-230 |
4.60e-27 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 108.96 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRV--GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII----TPGERLSFLQQdH-- 73
Cdd:COG1122 1 IELENLSFSYpgGTPAL-DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRR-Kvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 --FQY-DDYMVLDTVmmgnarlyeimkEKEVIYakedftdedGIKASELEGEfaamngwEAESDAATLLNGLGIdAELHD 150
Cdd:COG1122 79 lvFQNpDDQLFAPTV------------EEDVAF---------GPENLGLPRE-------EIRERVEEALELVGL-EHLAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 151 KAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDRYFLNKVCTQIADIDY 227
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
...
gi 2124998340 228 GKI 230
Cdd:COG1122 210 GRI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-230 |
1.11e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.37 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 3 STSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--TPGERLSFLQQdhfqyddym 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdgKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgnARLYEIMkekeviyakedftdedgikaselegefaamngweaesdaATLLNGLGIdAELHDKAMKDLNGPE 160
Cdd:cd03214 72 ---------ARKIAYV---------------------------------------PQALELLGL-AHLADRPFNELSGGE 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHDryfLN---KVCTQIADIDYGKI 230
Cdd:cd03214 103 RQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNlaaRYADRVILLKDGRI 176
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-230 |
2.36e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.44 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI--------ITPGE---RLSFLQ 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsaMPPPEwrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 71 QDHFqyddyMVLDTVmmgnarlyeimkekeviyaKEDFTDEDGIKASELEGEfaamngweaesDAATLLNGLGIDAELHD 150
Cdd:COG4619 81 QEPA-----LWGGTV-------------------RDNLPFPFQLRERKFDRE-----------RALELLERLGLPPDILD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 151 KAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADID 226
Cdd:COG4619 126 KPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLE 205
|
....
gi 2124998340 227 YGKI 230
Cdd:COG4619 206 AGRL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-231 |
2.39e-25 |
|
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: 103.49 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 3 STSNITLRVGKKA-LFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI-----ITPGERLS---FLQQDh 73
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpIKAKERRKsigYVMQD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 fqYDDYMVLDTVmmgnarlyeimkekeviyakedftdedgikASELegEFAAMNGWEAESDAATLLNGLGIdAELHDKAM 153
Cdd:cd03226 80 --VDYQLFTDSV------------------------------REEL--LLGLKELDAGNEQAETVLKDLDL-YALKERHP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD---LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
.
gi 2124998340 231 K 231
Cdd:cd03226 205 V 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-230 |
3.38e-25 |
|
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: 103.07 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIitpgerlsFLQQDHFQ-YDDYM 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT--------FDGKSYQKnIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNArLYEIMKekeviyAKEDFtdedGIKASELEGEfaamngweaESDAATLLNGLGIDAELHDKAmKDLNGPE 160
Cdd:cd03268 73 RIGALIEAPG-FYPNLT------ARENL----RLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKV-KGFSLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
5.54e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 101.17 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 5 SNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqdhfqyddymvldt 84
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 85 vmmgnarlyeimkekeviyakedftdeDGIKASELEGEfaamngweaesdaaTLLNGLGIdaelhdkaMKDLNGPEKVKV 164
Cdd:cd00267 59 ---------------------------DGKDIAKLPLE--------------ELRRRIGY--------VPQLSGGQRQRV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 165 LLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
1.19e-23 |
|
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: 98.80 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGnCYGLIGANGAGKSTFLRILSGQLEPSKG-------DVIITPGE---RLSFLQQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGtiridgqDVLKQPQKlrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 72 DHFQYDDYMV---LDTVmmgnARLYEIMKEKEviyakedftdedgikaselegefaamngwEAESDAATLLNGLGidaEL 148
Cdd:cd03264 80 EFGVYPNFTVrefLDYI----AWLKGIPSKEV-----------------------------KARVDEVLELVNLG---DR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 149 HDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDldaiawLEEfLINFDN---------TVIVVSHDRYFLNKVC 219
Cdd:cd03264 124 AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD------PEE-RIRFRNllselgedrIVILSTHIVEDVESLC 196
|
250
....*....|..
gi 2124998340 220 TQIADIDYGKIK 231
Cdd:cd03264 197 NQVAVLNKGKLV 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
1.69e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 96.56 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 17 FEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-----------TPGERLSFLQQDHFQYDDYMVLDTV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 MMGnARLYEIMKEkeviyakedftdedgikaselegefaamngwEAESDAATLLNGLGIDAELHDKA---MKDLNGPEKV 162
Cdd:pfam00005 81 RLG-LLLKGLSKR-------------------------------EKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQ 128
|
170 180
....*....|....*....|..
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTN 184
Cdd:pfam00005 129 RVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-230 |
1.58e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.02 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGK-----KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-------TPGERLSFL 69
Cdd:cd03255 1 IELKNLSKTYGGggekvQAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdiskLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQDH----FQydDYMVLDtvmmgnarlyeimkekeviyakeDFTDEDGIkasELEGEFAAMNGWEAESDAATLLNGLGID 145
Cdd:cd03255 80 RRRHigfvFQ--SFNLLP-----------------------DLTALENV---ELPLLLAGVPKKERRERAEELLERVGLG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 146 AELHDKAMKdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLINFDNTVIVVSHDRYFLNKvCTQ 221
Cdd:cd03255 132 DRLNHYPSE-LSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAEY-ADR 209
|
....*....
gi 2124998340 222 IADIDYGKI 230
Cdd:cd03255 210 IIELRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
1.60e-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: 96.35 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGK-KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH------- 73
Cdd:cd03219 1 LEVRGLTKRFGGlVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 --FQ----YDDYMVLDTVMMGnarlyeimkekeVIYAKEDFTDEDGIKASElegefaamngWEAESDAATLLNGLGIDAE 147
Cdd:cd03219 79 rtFQiprlFPELTVLENVMVA------------AQARTGSGLLLARARREE----------REARERAEELLERVGLADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 148 LHDKAmKDLNGPEKVKVLLAQALFGNPDILLLDEPT---NHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIAD 224
Cdd:cd03219 137 ADRPA-GELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTV 215
|
....*.
gi 2124998340 225 IDYGKI 230
Cdd:cd03219 216 LDQGRV 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-237 |
2.31e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 100.58 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDymv 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP--- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmmgnarlyeimkEKEVIyakEDFTD-EDGIKaselegefaaMNGWEAESDA-ATLLNGLGIDAElhdKAMKDLNGP 159
Cdd:PRK11819 402 ----------------NKTVW---EEISGgLDIIK----------VGNREIPSRAyVGRFNFKGGDQQ---KKVGVLSGG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIadIDY---GKIKLYAGN 236
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFegdSQVEWFEGN 527
|
.
gi 2124998340 237 Y 237
Cdd:PRK11819 528 F 528
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-230 |
2.16e-21 |
|
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: 93.73 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 5 SNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGE-----------RLSFLQQDH 73
Cdd:TIGR03873 5 SRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDlhglsrrararRVALVEQDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 FQYDDYMVLDTVMMGNArlyeimkEKEVIYAKEdfTDEDgikaSELEGEFAAMNGWEAesdaatllnglgidaeLHDKAM 153
Cdd:TIGR03873 85 DTAVPLTVRDVVALGRI-------PHRSLWAGD--SPHD----AAVVDRALARTELSH----------------LADRDM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEfLINFDNTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:TIGR03873 136 STLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqletLALVRE-LAATGVTVVAALHDLNLAASYCDHVVVLDGGR 214
|
.
gi 2124998340 230 I 230
Cdd:TIGR03873 215 V 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-211 |
5.20e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 16 LFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQdHFQYDDYM---VLDTVMMGnarl 92
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSLpltVRDLVAMG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 yeimkekeviyakedftdedgikaselegEFAAMNGW-----EAESDAATLLNGLGIdAELHDKAMKDLNGPEKVKVLLA 167
Cdd:NF040873 82 -----------------------------RWARRGLWrrltrDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2124998340 168 QALFGNPDILLLDEPTNHLDLDAIAWLEEfLINF----DNTVIVVSHD 211
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIA-LLAEeharGATVVVVTHD 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-471 |
6.11e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 96.42 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 26 EGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITP----------GERLsflqQDHF--------------QYDDY-- 79
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlkrfrGTEL----QNYFkklyngeikvvhkpQYVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 80 MVLDtvmmGNARlyEIMKEkeviyakedfTDEDGiKASELEGEfaamngweaesdaatllngLGIDAELhDKAMKDLNGP 159
Cdd:PRK13409 174 KVFK----GKVR--ELLKK----------VDERG-KLDEVVER-------------------LGLENIL-DRDISELSGG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLDL-------DAIAWLEEflinfDNTVIVVSHDRYFLNKVCTQIaDIDYGK--- 229
Cdd:PRK13409 217 ELQRVAIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDYLADNV-HIAYGEpga 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 230 -------------IKLYAGNYdfwYESSQLLIRQmkeankkkeekikELQEFisrfsanasKSKQATSRKRALEKIELDD 296
Cdd:PRK13409 291 ygvvskpkgvrvgINEYLKGY---LPEENMRIRP-------------EPIEF---------EERPPRDESERETLVEYPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 297 IqpsSRKYPyiDFRpnreignevLTVEGlsktidGEkildditftLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY 376
Cdd:PRK13409 346 L---TKKLG--DFS---------LEVEG------GE---------IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 377 KWGVTTSqaYFPLDSGSEFDNeyTIVEWLTQYSDEKDVTY-----VRGF-LGRMLfsgeDgvKKVKVLSGGEKVR----- 445
Cdd:PRK13409 397 DPELKIS--YKPQYIKPDYDG--TVEDLLRSITDDLGSSYykseiIKPLqLERLL----D--KNVKDLSGGELQRvaiaa 466
|
490 500
....*....|....*....|....*.
gi 2124998340 446 CLLSKmmisgANVLLLDEPTNHLDME 471
Cdd:PRK13409 467 CLSRD-----ADLYLLDEPSAHLDVE 487
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
9.65e-21 |
|
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: 91.64 E-value: 9.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGK-KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH------ 73
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRiarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 ---FQ----YDDYMVLDTVMMG-NARLYEimkekeviyakedftdedGIKASELEGEFAAMNGWEAESDAATLLNGLGID 145
Cdd:COG0411 82 artFQnprlFPELTVLENVLVAaHARLGR------------------GLLAALLRLPRARREEREARERAEELLERVGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 146 AELHDKAmKDLNGPEKVKVLLAQALFGNPDILLLDEPT---NHLDLDAIAWL-----EEFLInfdnTVIVVSHDRYFLNK 217
Cdd:COG0411 144 DRADEPA-GNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELirrlrDERGI----TILLIEHDMDLVMG 218
|
250
....*....|...
gi 2124998340 218 VCTQIADIDYGKI 230
Cdd:COG0411 219 LADRIVVLDFGRV 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-230 |
1.27e-20 |
|
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: 90.50 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKAL----FEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKG-------DVIITPGE---RL 66
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfatvdgfDVVKEPAEarrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 67 SFLQqdhfqyddymvldtvmmGNARLYEIMKEKEVIyakedftdedgikasELEGEFAAMNGWEAESDAATLLNGLGIdA 146
Cdd:cd03266 81 GFVS-----------------DSTGLYDRLTARENL---------------EYFAGLYGLKGDELTARLEELADRLGM-E 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 147 ELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKVCTQIA 223
Cdd:cd03266 128 ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVV 207
|
....*..
gi 2124998340 224 DIDYGKI 230
Cdd:cd03266 208 VLHRGRV 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-469 |
1.38e-20 |
|
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: 94.87 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSG--QLEPSKGDVIITPG--------ERLSFLQQ 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 72 ---------DHFQYDDYMVLDTVMMGNARLYEIMKEKEVIYAKEDFTDEDGIKASELEGefaaMNGWEAESDAATLLNGL 142
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIG----YEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 143 GIDAELHDKAmKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAI----AWLEEFLINFDNTVIVVSHDRYFLNKV 218
Cdd:TIGR03269 157 QLSHRITHIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 219 CTQIADIDYGKIKLyAGNYDfwyessqllirqmkeankkkeekikelqEFISRFSANASKSKQATsrkralekielddiq 298
Cdd:TIGR03269 236 SDKAIWLENGEIKE-EGTPD----------------------------EVVAVFMEGVSEVEKEC--------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 299 pssrkypyidfrpNREIGNEVLTVEGLSK---TIDGE--KILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDE 373
Cdd:TIGR03269 272 -------------EVEVGEPIIKVRNVSKryiSVDRGvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 374 GTY------KWGVTTSQAyfPLDSGSE------FDNEY------TIVEWLT-----QYSDEKDVTYVRGFLGRMLFSGED 430
Cdd:TIGR03269 339 GEVnvrvgdEWVDMTKPG--PDGRGRAkryigiLHQEYdlyphrTVLDNLTeaiglELPDELARMKAVITLKMVGFDEEK 416
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2124998340 431 GV----KKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:TIGR03269 417 AEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
1.77e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 90.91 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERL-------------- 66
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 67 --SFLQQdhfQYDDYM-VLDTVMMGnarLYEIMkekeVIYakEDFTDEDgikaselegefaamngweaESDAATLLNGLG 143
Cdd:COG1119 83 vsPALQL---RFPRDEtVLDVVLSG---FFDSI----GLY--REPTDEQ-------------------RERARELLELLG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 144 IdAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLINFDNTVIVVSH 210
Cdd:COG1119 132 L-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-471 |
9.61e-20 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 92.54 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 26 EGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPG--ERLSFLQ----QDHF--------------QYDDY--MVLD 83
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdEVLKRFRgtelQDYFkklangeikvahkpQYVDLipKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 tvmmGNARlyEIMKEkeviyakedfTDEDGiKASELEGEfaamngweaesdaatllngLGIDAELhDKAMKDLNGPEKVK 163
Cdd:COG1245 178 ----GTVR--ELLEK----------VDERG-KLDELAEK-------------------LGLENIL-DRDISELSGGELQR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 164 VLLAQALFGNPDILLLDEPTNHLDLD---AIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIAdIDYGK----------- 229
Cdd:COG1245 221 VAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYVH-ILYGEpgvygvvskpk 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 230 -----IKLYAGNYdfwYESSQLLIRQMKEankkkeekikelqefisRFSANASKSKQATSrkralEKIELDDIqpsSRKY 304
Cdd:COG1245 300 svrvgINQYLDGY---LPEENVRIRDEPI-----------------EFEVHAPRREKEEE-----TLVEYPDL---TKSY 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 305 PyiDFRpnreignevLTVEGlsktidGEkildditftLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSq 384
Cdd:COG1245 352 G--GFS---------LEVEG------GE---------IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIS- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 385 aYFPldsgsefdneytivewltQY-SDEKDVTyVRGFLGRMLFSGEDGV-----------------KKVKVLSGGEkvrc 446
Cdd:COG1245 405 -YKP------------------QYiSPDYDGT-VEEFLRSANTDDFGSSyykteiikplgleklldKNVKDLSGGE---- 460
|
490 500 510
....*....|....*....|....*....|
gi 2124998340 447 lLSKMMISG-----ANVLLLDEPTNHLDME 471
Cdd:COG1245 461 -LQRVAIAAclsrdADLYLLDEPSAHLDVE 489
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
1.27e-19 |
|
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: 87.62 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEpskgdviITPGERLS----FLQQDHFQYD 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLND-------LIPGAPDEgevlLDGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 78 DY---------MVLDTVMMGNARLYEimkekEVIYAKEDFtdedGIKASElegefaamngwEAESDAATLLNGLGIDAEL 148
Cdd:cd03260 74 VDvlelrrrvgMVFQKPNPFPGSIYD-----NVAYGLRLH----GIKLKE-----------ELDERVEEALRKAALWDEV 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 149 HDKAM-KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHD 211
Cdd:cd03260 134 KDRLHaLGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-230 |
1.56e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 92.20 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVG--KKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGE---RLSF 68
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqiDPASlrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 69 LQQDHFQYDDyMVLDTVMMGNarlyeimkekeviyakEDFTDEDGIKASELEGefaamngweAESDAATLLNGLgiDAEL 148
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGD----------------PDATDEEIIEAARLAG---------LHDFIEALPMGY--DTVV 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 149 HDKAmKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHDRYFLnKVCTQIADID 226
Cdd:COG2274 606 GEGG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLD 683
|
....
gi 2124998340 227 YGKI 230
Cdd:COG2274 684 KGRI 687
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
319-514 |
3.02e-19 |
|
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: 87.22 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT--------YKWGVTTSQAYFPLD 390
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgedvRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 391 SGSEFDNEYTIVEWLTQY------SDEKDVTYVRGFLGRMLFSgEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEP 464
Cdd:COG4555 81 DERGLYDRLTVRENIRYFaelyglFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 465 TNHLDMESITALNNGLVKF---PGVLLFSSRDHQIVQTTANRIMeIVPGGKLI 514
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV-ILHKGKVV 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-507 |
8.99e-19 |
|
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: 84.84 E-value: 8.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQ----------AYFP 388
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdaredyrrrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 389 LDSGseFDNEYTIVEWLT----QYSDEKDVTYVRGFLGRMLFSG-EDgvKKVKVLSGGEKVRCLLSKMMISGANVLLLDE 463
Cdd:COG4133 82 HADG--LKPELTVRENLRfwaaLYGLRADREAIDEALEAVGLAGlAD--LPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2124998340 464 PTNHLDMESITALNNGLVKFP---GVLLFSSrdHQIVQTTANRIMEI 507
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTT--HQPLELAAARVLDL 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
1.01e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 89.43 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLR-VGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQ----Y 76
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPASWRrqiaW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 ---DDYMVLDTVmMGNARLyeimkekeviyAKEDFTDEDGIKASELegefaamngweaeSDAATLLNGL--GIDAELHDK 151
Cdd:COG4988 416 vpqNPYLFAGTI-RENLRL-----------GRPDASDEELEAALEA-------------AGLDEFVAALpdGLDTPLGEG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 152 AMKdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSHDRYFLnKVCTQIADIDYGK 229
Cdd:COG4988 471 GRG-LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALL-AQADRILVLDDGR 548
|
.
gi 2124998340 230 I 230
Cdd:COG4988 549 I 549
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-507 |
1.04e-18 |
|
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: 83.60 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKwgvttsqaYFPLDSGSEFDNEY 399
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------VLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 TIVEWLTQYSdekdvtyvrGFLGRMlfSGEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNN- 478
Cdd:cd03230 73 RRIGYLPEEP---------SLYENL--TVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEl 137
|
170 180 190
....*....|....*....|....*....|.
gi 2124998340 479 --GLVKFPGVLLFSSRDHQIVQTTANRIMEI 507
Cdd:cd03230 138 lrELKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
1.39e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.59 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGE---RLSFL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwSPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQDH---FqydDYMVLDTVMMGNARLYEIMKEKEVIYAkedftdedgikaselegefAAMngweAESDAatllnglgidA 146
Cdd:PRK13548 82 PQHSslsF---PFTVEEVVAMGRAPHGLSRAEDDALVA-------------------AAL----AQVDL----------A 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 147 ELHDKAMKDLNGPEKVKVLLAQAL------FGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHDryfLN 216
Cdd:PRK13548 126 HLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---LN 202
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-188 |
2.46e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.78 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-------TPGERLSF----L 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLngrplaaWSPWELARrravL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQD---HFqydDYMVLDTVMMGNARlyeimkekeviYAKEDFTDEDGIKaselegefAAMngweaesdAATLLNGLGida 146
Cdd:COG4559 81 PQHsslAF---PFTVEEVVALGRAP-----------HGSSAAQDRQIVR--------EAL--------ALVGLAHLA--- 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124998340 147 elhDKAMKDLNGPEKVKVLLAQAL-------FGNPDILLLDEPTNHLDL 188
Cdd:COG4559 128 ---GRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
2.85e-18 |
|
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: 84.09 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH-------- 73
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAElyrlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 ---FQ----YDDYMVLDTVMMgnaRLYE--IMKEKEViyakedftdedgikaseleGEFAAMNgweaesdaatlLNGLGI 144
Cdd:cd03261 80 gmlFQsgalFDSLTVFENVAF---PLREhtRLSEEEI-------------------REIVLEK-----------LEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 145 DAElHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEfLIN-----FDNTVIVVSHDRYFLNKVC 219
Cdd:cd03261 127 RGA-EDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDD-LIRslkkeLGLTSIMVTHDLDTAFAIA 204
|
250
....*....|.
gi 2124998340 220 TQIADIDYGKI 230
Cdd:cd03261 205 DRIAVLYDGKI 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-233 |
3.32e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpgERLSFLqqdhfqyddym 80
Cdd:COG1134 27 LLLRRRRTRREEFWAL-KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN--GRVSAL----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vLDtVMMG-------------NARLYEiMKEKEvIYAKEDFtdedgIKA-SELeGEFaamngweaesdaatllnglgIDA 146
Cdd:COG1134 93 -LE-LGAGfhpeltgreniylNGRLLG-LSRKE-IDEKFDE-----IVEfAEL-GDF--------------------IDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 147 ELhdKA----MkdlngpeKVKVLLAQALFGNPDILLLDEPTNHLDLD----AIAWLEEFLINfDNTVIVVSHDRYFLNKV 218
Cdd:COG1134 143 PV--KTyssgM-------RARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRL 212
|
250
....*....|....*
gi 2124998340 219 CTQIADIDYGKIKLY 233
Cdd:COG1134 213 CDRAIWLEKGRLVMD 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-466 |
3.67e-18 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 81.54 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 335 LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQ-----------AYFPLDSGseFDNEYTIVE 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdderkslrkeiGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 404 WLTQYSDEKDVTY---------VRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTN 466
Cdd:pfam00005 79 NLRLGLLLKGLSKrekdaraeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-230 |
7.09e-18 |
|
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: 82.42 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqdhFQYDdymv 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV-------------AGHD---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmmgnarlyeIMKE----KEVI-YAKEDFTDEDGIKASE---LEGEFAAMNGWEAESDAATLLNGLGIdAELHDKAM 153
Cdd:cd03265 64 -------------VVREprevRRRIgIVFQDLSVDDELTGWEnlyIHARLYGVPGAERRERIDELLDFVGL-LEAADRLV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIA--W--LEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:cd03265 130 KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
.
gi 2124998340 230 I 230
Cdd:cd03265 210 I 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-233 |
8.84e-18 |
|
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: 81.94 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQYddymv 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-GKPLDIAARNRIGY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmMGNAR-LYEIMKEKEV-IYAkedftdedgikaseleGEFAAMNGWEAESDAATLLNGLGIdAELHDKAMKDLNGP 159
Cdd:cd03269 75 -----LPEERgLYPKMKVIDQlVYL----------------AQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEflinFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKL 232
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDpvnvellKDVIRELAR----AGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
.
gi 2124998340 233 Y 233
Cdd:cd03269 209 Y 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-210 |
1.27e-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: 80.72 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVG--KKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqdhfqyddy 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 80 mvldtvmmgnarlyeimkekeviyakedftdeDGIKASEL-EGEFAAMNGWEAEsdaatllnglgiDAELHDKAMKD--L 156
Cdd:cd03246 62 --------------------------------DGADISQWdPNELGDHVGYLPQ------------DDELFSGSIAEniL 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 157 NGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFD---NTVIVVSH 210
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-214 |
2.29e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 81.69 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 24 FTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDvIITPGERLSFLQQdhfqyddYMVLDTVMMGNARLYEIMKekeviy 103
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-IEIELDTVSYKPQ-------YIKADYEGTVRDLLSSITK------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 104 akedftdedgikaselegEFAAMNGWEAEsdaatLLNGLGIDaELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPT 183
Cdd:cd03237 88 ------------------DFYTHPYFKTE-----IAKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190
....*....|....*....|....*....|....*
gi 2124998340 184 NHLD----LDAIAWLEEFLINFDNTVIVVSHDRYF 214
Cdd:cd03237 144 AYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIM 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-230 |
2.50e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 81.10 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI--------ITPGE---RLSFLQQDhfqyddymvldtVM 86
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqLDPADlrrNIGYVPQD------------VT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 87 MGNARLYEimkekEVIYAKEDFTDEDGIKASELEG--EFAAmngweaesdaatlLNGLGIDAELHDKAMkDLNGPEKVKV 164
Cdd:cd03245 89 LFYGTLRD-----NITLGAPLADDERILRAAELAGvtDFVN-------------KHPNGLDLQIGERGR-GLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 165 LLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSHdRYFLNKVCTQIADIDYGKI 230
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-230 |
3.90e-17 |
|
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: 84.47 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGErlsflqqdhfQYDDYMVLDTVMMGNARLY-EIM 96
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGD----------EWVDMTKPGPDGRGRAKRYiGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 97 KEKEVIYAK----EDFTDEDGIkasELEGEFAAMNgweaesdAATLLNGLGID----AELHDKAMKDLNGPEKVKVLLAQ 168
Cdd:TIGR03269 371 HQEYDLYPHrtvlDNLTEAIGL---ELPDELARMK-------AVITLKMVGFDeekaEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 169 ALFGNPDILLLDEPTNHLD-LDAIAWLEEFL---INFDNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDpITKVDVTHSILkarEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
4.13e-17 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 76.07 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 223 ADIDYGKIKLYAGNYDFWYESSQLLIRQMKEANKKKEEKIKELQEFISRFSANASKSKQATSRKRALEKIEldDIQPSSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKME--RIEKPER 78
|
....*..
gi 2124998340 303 KYPYIDF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-233 |
4.36e-17 |
|
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: 80.27 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 9 LRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQYDDYMVLDTVMMg 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR-GRVSSLLGLGGGFNPELTGRENIYL- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 89 NARLYEiMKEKEvIYAKEDFTdedgIKASELeGEFAamngweaesdaatllnglgidaelhDKAMKDLNGPEKVKVLLAQ 168
Cdd:cd03220 108 NGRLLG-LSRKE-IDEKIDEI----IEFSEL-GDFI-------------------------DLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 169 ALFGNPDILLLDEPT----NHLDLDAIAWLEEFLINfDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLY 233
Cdd:cd03220 156 ATALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
4.69e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-----------TPGERLSFL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQDHFQYDDYMVLDTVMMGN----ARLyeimkekeviyakeDFTDEDGIKASElegefAAMNGWEAesdaatllnglgid 145
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRtphrSRF--------------DTWTETDRAAVE-----RAMERTGV-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 146 AELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLD-AIAWLE--EFLINFDNTVIVVSHDRYFLNKVCTQI 222
Cdd:PRK09536 130 AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHDLDLAARYCDEL 209
|
....*...
gi 2124998340 223 ADIDYGKI 230
Cdd:PRK09536 210 VLLADGRV 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
4.90e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDhfqyddyM 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEIMKEkeviyakedftdedGIKASELEGEFAAMNGweaesdaatllnglgidAELHDKAMKDLNGPE 160
Cdd:PRK09544 77 YLDTTLPLTVNRFLRLRP--------------GTKKEDILPALKRVQA-----------------GHLIDAPMQKLSGGE 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEfLIN-----FDNTVIVVSHD 211
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD-LIDqlrreLDCAVLMVSHD 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-230 |
6.67e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRV--GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH----- 73
Cdd:COG2884 1 MIRFENVSKRYpgGREAL-SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 ------FQY----DDYMVLDTVMMgnarlyeIMkekEVIYAKEDftdedgikaselegefaamngwEAESDAATLLNGLG 143
Cdd:COG2884 79 rrigvvFQDfrllPDRTVYENVAL-------PL---RVTGKSRK----------------------EIRRRVREVLDLVG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 144 idaeLHDKAMK---DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDlDAIAW-----LEEFlinfdN----TVIVVSHD 211
Cdd:COG2884 127 ----LSDKAKAlphELSGGEQQRVAIARALVNRPELLLADEPTGNLD-PETSWeimelLEEI-----NrrgtTVLIATHD 196
|
250
....*....|....*....
gi 2124998340 212 RYFLNKVCTQIADIDYGKI 230
Cdd:COG2884 197 LELVDRMPKRVLELEDGRL 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-231 |
6.95e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 79.86 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 19 DVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII----------TPGERLSFLQQDHFQYDDYMVLDTVmmg 88
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirtdrkAARQSLGYCPQFDALFDELTVREHL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 89 naRLYEIMKekeviyakedftdedGIkaselegefaamNGWEAESDAATLLNGLGIDAELHDKAmKDLNGPEKVKVLLAQ 168
Cdd:cd03263 97 --RFYARLK---------------GL------------PKSEIKEEVELLLRVLGLTDKANKRA-RTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 169 ALFGNPDILLLDEPTNHLD-------LDAIAWLEEflinfDNTVIVVSHDRYFLNKVCTQIADIDYGKIK 231
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDpasrraiWDLILEVRK-----GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-233 |
8.44e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.92 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVG-KKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQYddy 79
Cdd:COG4152 1 MLELKGLTKRFGdKTAV-DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLDPEDRRRIGY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 80 mvldtvmMGNAR-LYEIMKEKEVIYAkedftdedgikaselegeFAAMNGW---EAESDAATLLNGLGIdAELHDKAMKD 155
Cdd:COG4152 76 -------LPEERgLYPKMKVGEQLVY------------------LARLKGLskaEAKRRADEWLERLGL-GDRANKKVEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF-DN--TVIVVSHDryfLNKV---CTQIADIDYGK 229
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaAKgtTVIFSSHQ---MELVeelCDRIVIINKGR 206
|
....
gi 2124998340 230 IKLY 233
Cdd:COG4152 207 KVLS 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-230 |
8.91e-17 |
|
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: 79.47 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGK---KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDH--------- 73
Cdd:cd03257 8 SVSFPTGGgsvKAL-DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkeiqm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 -FQyDDYMVLDTVMmgnaRLYEIMKEkeVIYAKEDFTDEDGIKASELEgefaamngweaesdaatLLNGLGIDAELHDKA 152
Cdd:cd03257 87 vFQ-DPMSSLNPRM----TIGEQIAE--PLRIHGKLSKKEARKEAVLL-----------------LLVGVGLPEEVLNRY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 153 MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEfliNFDNTVIVVSHDRYFLNKVCTQIADI 225
Cdd:cd03257 143 PHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQE---ELGLTLLFITHDLGVVAKIADRVAVM 219
|
....*
gi 2124998340 226 DYGKI 230
Cdd:cd03257 220 YAGKI 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
9.03e-17 |
|
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: 79.55 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNIT----LRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGqLE-PSKGDVIITpGERLSFL---QQD 72
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVD-GTDLTLLsgkELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 73 HFQYDDYMVLDTvmmgnarlYEIMKEKEVIyakedftdeDGIkasELEGEFAAMNGWEAESDAATLLNGLGIdAELHDKA 152
Cdd:cd03258 79 KARRRIGMIFQH--------FNLLSSRTVF---------ENV---ALPLEIAGVPKAEIEERVLELLELVGL-EDKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 153 MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL--IN--FDNTVIVVSHDRYFLNKVCTQIADIDYG 228
Cdd:cd03258 138 PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLrdINreLGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
..
gi 2124998340 229 KI 230
Cdd:cd03258 218 EV 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-237 |
1.01e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.46 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpGERLSFLQQDHFQYD---DYMVL 82
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC--GTKLEVAYFDQHRAEldpEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 83 DTVMMGNArlyEIM---KEKEVIYAKEDFTdedgikaselegeFAAMngweaesdaatllnglgidaelhdKAM---KDL 156
Cdd:PRK11147 402 DNLAEGKQ---EVMvngRPRHVLGYLQDFL-------------FHPK------------------------RAMtpvKAL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 157 NGPEKVKVLLAQaLFGNP-DILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQ--IADIDyGKIKLY 233
Cdd:PRK11147 442 SGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFEGN-GKIGRY 519
|
....
gi 2124998340 234 AGNY 237
Cdd:PRK11147 520 VGGY 523
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-230 |
2.06e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 82.12 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-----------TPGERLSFLQQDHFqyddym 80
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldedDLRRRIAVVPQRPH------ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLyeimkekeviyAKEDFTDEdgikasELegefaamngWEAESDA--ATLLNGL--GIDAELHDKAMKdL 156
Cdd:COG4987 420 LFDTTLRENLRL-----------ARPDATDE------EL---------WAALERVglGDWLAALpdGLDTWLGEGGRR-L 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 157 NGPEKVKVLLAQALFGNPDILLLDEPTNHLD-LDAIAWLEEFLINFDN-TVIVVSHDRYFLNKVcTQIADIDYGKI 230
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGrTVLLITHRLAGLERM-DRILVLEDGRI 547
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
2.37e-16 |
|
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: 82.02 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH------FQYDDYMVLDTV 85
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEvrrrvsVCAQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 MMGNARLyeimkekeviyAKEDFTDEDGIKASELEGefaamngweAESDAATLLNGLgiDAELHDKAmKDLNGPEKVKVL 165
Cdd:TIGR02868 425 VRENLRL-----------ARPDATDEELWAALERVG---------LADWLRALPDGL--DTVLGEGG-ARLSGGERQRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHD 211
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-235 |
2.39e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.53 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 19 DVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII---TPGER---------LSFLQQDHFQYdDYMVLDTVM 86
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglVPWKRrkkflrrigVVFGQKTQLWW-DLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 87 MgNARLYEImkekeviyakedftdEDGIKASELEgEFAAMngweaesdaatllngLGIDAELhDKAMKDLNGPEKVKVLL 166
Cdd:cd03267 118 L-LAAIYDL---------------PPARFKKRLD-ELSEL---------------LDLEELL-DTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 167 AQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF----DNTVIVVSHDRYFLNKVCTQIADIDYGKIkLYAG 235
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-505 |
4.20e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 81.10 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGqLEPSKGDViitpGERLSFLQQDHFQYDDYMVLDTV 85
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRI----SGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 MMgnarlyeIMKEKEViyAKEDFTDEDGIkaselegEFAAMNGW----EAESDAATLLNGLGIdAELHDKAMKDLNGPEK 161
Cdd:COG1123 86 GM-------VFQDPMT--QLNPVTVGDQI-------AEALENLGlsraEARARVLELLEAVGL-ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAgny 237
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 238 dfwyessqllirqmkeankkkeekikelqefisrfsanasKSKQATSRKRALEKIELDDIQPSSRkypyidfRPNREIGN 317
Cdd:COG1123 226 ----------------------------------------PPEEILAAPQALAAVPRLGAARGRA-------APAAAAAE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 318 EVLTVEGLSKT-----IDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQAY----- 386
Cdd:COG1123 259 PLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKLSrrslr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 387 ---------F--PLDSgseFDNEYTIVEWLTqysdekdvtyvRGFLGRMLFSGEDGVKKV-----KV------------- 437
Cdd:COG1123 339 elrrrvqmvFqdPYSS---LNPRMTVGDIIA-----------EPLRLHGLLSRAERRERVaelleRVglppdladryphe 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 438 LSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMeSITA--LN--NGLVKFPGV-LLFSSRDHQIVQTTANRIM 505
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqiLNllRDLQRELGLtYLFISHDLAVVRYIADRVA 476
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-510 |
4.71e-16 |
|
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: 75.74 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 321 TVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwgvttsqayfpldsgsefdneyt 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 401 iVEWLTQYSDEKDVTYVRGFLGrMLFSgedgvkkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNGL 480
Cdd:cd00267 56 -ILIDGKDIAKLPLEELRRRIG-YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|...
gi 2124998340 481 VKF--PGV-LLFSSRDHQIVQTTANRIMEIVPG 510
Cdd:cd00267 124 RELaeEGRtVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-232 |
5.15e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIIT------PGERLSFLQQD---HFQYDDYmvld 83
Cdd:PRK13637 20 KKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdKKVKLSDIRKKvglVFQYPEY---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 tvmmgnaRLYEIMKEKEVIYAKEDFtdedGIKASELEGE-FAAMngweaesdaatllNGLGIDAE-LHDKAMKDLNGPEK 161
Cdd:PRK13637 95 -------QLFEETIEKDIAFGPINL----GLSEEEIENRvKRAM-------------NIVGLDYEdYKDKSPFELSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEfliNFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKL 232
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
6.02e-16 |
|
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: 76.79 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGER-LSFLQQDHFQY 76
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvPPERRnIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 DDYMVLDTVMMGnarlyeiMKEKEViyakedftDEDGIKASELEgefaamngweaesdaatLLNGLGIDAELHDKAmKDL 156
Cdd:cd03259 85 PHLTVAENIAFG-------LKLRGV--------PKAEIRARVRE-----------------LLELVGLEGLLNRYP-HEL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 157 NGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLINFDNTVIVVSHDR 212
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-528 |
7.65e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 334 ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEG--TYKWGVTTS--QAYFPLD-SGSEFDneYT------IV 402
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGriIYEQDLIVArlQQDPPRNvEGTVYD--FVaegieeQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 403 EWLTQY---SDEKDVTYVRGFLGRM--------------LFS---------GEDGVKKVKVLSGGEKVRCLLSKMMISGA 456
Cdd:PRK11147 96 EYLKRYhdiSHLVETDPSEKNLNELaklqeqldhhnlwqLENrinevlaqlGLDPDAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 457 NVLLLDEPTNHLDMESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMEIvPGGKLIDKITTYDEYLESDE 528
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGKLVSYPGNYDQYLLEKE 246
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-229 |
9.77e-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: 75.30 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 5 SNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-------------TPGERLSFLQQ 71
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 72 DHFQYDDYMVLDTVMMGnarlyeimkekeviyakedftdedgikaselegefaamngweaesdaatllnglgidaelhdk 151
Cdd:cd03229 84 DFALFPHLTVLENIALG--------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 152 amkdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLI----NFDNTVIVVSHDRYFLNKVCTQIADIDY 227
Cdd:cd03229 101 ----LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
..
gi 2124998340 228 GK 229
Cdd:cd03229 177 GK 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
1.76e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGE---RLSFL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdkpismlSSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQDHFQYDDYMVLDTVMMGNA-------RLyeimkekeviyakedfTDEDgikaselegefaamngwEAESDAAtlLNGL 142
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSpwlslwgRL----------------SAED-----------------NARVNQA--MEQT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 143 GIDaELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDryfLNKVC 219
Cdd:PRK11231 127 RIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD---LNQAS 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-515 |
2.15e-15 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 74.95 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYK-WGVTTSQAYFPLD------SG 392
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRrigaliEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 393 SEFDNEYTIVEWLTQYSDEKDVTY--VRGFLGRMLFSGEDGvKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDM 470
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKkrIDEVLDVVGLKDSAK-KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2124998340 471 ESITALNN---GLVKFPGVLLFSSrdHQI--VQTTANRIMeIVPGGKLID 515
Cdd:cd03268 160 DGIKELRElilSLRDQGITVLISS--HLLseIQKVADRIG-IINKGKLIE 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-211 |
2.57e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 75.02 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFT-EGNCYGLIGANGAGKSTFLRILSGQLEPSKG-----DVIITPGERLSFL--QQDHFQYd 77
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlnGTVLFDSRKKINLppQQRKIGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 78 dymvldtvMMGNARLYEIMKEKEVIY--AKEDFTDEDGIKASElegefaamngweaesdaatLLNGLGIDaELHDKAMKD 155
Cdd:cd03297 80 --------VFQQYALFPHLNVRENLAfgLKRKRNREDRISVDE-------------------LLDLLGLD-HLLNRYPAQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHD 211
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHD 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-216 |
2.80e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 31 GLIGANGAGKSTFLRILSGQLEPSKGDVIITPgeRLSFLQQdhfqyddYMVLDTVMMGNARLYEImkekeviyaKEDFTD 110
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--KISYKPQ-------YIKPDYDGTVEDLLRSI---------TDDLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 111 edgikaselegefaamNGWEAEsdaatLLNGLGIDaELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLD- 189
Cdd:PRK13409 431 ----------------SYYKSE-----IIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEq 488
|
170 180 190
....*....|....*....|....*....|...
gi 2124998340 190 ------AIAWLEEfliNFDNTVIVVSHDRYFLN 216
Cdd:PRK13409 489 rlavakAIRRIAE---EREATALVVDHDIYMID 518
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
5.70e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-------TPGE----RLSFL 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldvatTPSRelakRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 70 QQD-HFqyddymvldtvmmgNARLyeimKEKEVI------YAKEDFTDEDgikaselegefaamngWEAESDAATLLNgL 142
Cdd:COG4604 81 RQEnHI--------------NSRL----TVRELVafgrfpYSKGRLTAED----------------REIIDEAIAYLD-L 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 143 GidaELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHD 211
Cdd:COG4604 126 E---DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-230 |
6.70e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 4 TSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--TPGERLSFLQQDHFQYDDYMV 81
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgEPLAKLNRAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 L-DTVMMGNAR--LYEIMKEkeviyAKEDFTDedgikaselegefaaMNGWEAESDAATLLNGLGIDAELHDKAMKDLNG 158
Cdd:PRK10419 95 FqDSISAVNPRktVREIIRE-----PLRHLLS---------------LDKAERLARASEMLRAVDLDDSVLDKRPPQLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-230 |
8.06e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.87 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-------TPGERLSFLQQdHFQY---DDYMV 81
Cdd:COG1123 277 GVRAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgkdltkLSRRSLRELRR-RVQMvfqDPYSS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMmgnaRLYEIMKEkeviyakedftdedGIKAselegeFAAMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPEK 161
Cdd:COG1123 355 LNPRM----TVGDIIAE--------------PLRL------HGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLIN----FDNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqreLGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.06e-14 |
|
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: 71.69 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGK-KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLqqdhfqyddym 80
Cdd:cd03216 1 LELRGITKRFGGvKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-GKEVSFA----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgnarlyeimkekeviyakedftdedgikaselegefaamNGWEAESdaatllngLGIdaelhdkAM-KDLNGP 159
Cdd:cd03216 68 ----------------------------------------------SPRDARR--------AGI-------AMvYQLSVG 86
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSH 210
Cdd:cd03216 87 ERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISH 140
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
1.08e-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: 76.56 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRV-GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQYD--- 77
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLADADADSWRDQiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 78 ----DYMVLDTVMmGNARLyeimkekeviyAKEDFTDEDGIKASELEGefaamngweaesdAATLLNGL--GIDAELhDK 151
Cdd:TIGR02857 401 vpqhPFLFAGTIA-ENIRL-----------ARPDASDAEIREALERAG-------------LDEFVAALpqGLDTPI-GE 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 152 AMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHDR 212
Cdd:TIGR02857 455 GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-504 |
1.30e-14 |
|
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: 71.65 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGE--KILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTtsqayfPLDSGSEFDN 397
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV------DLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 398 EYTIVeWLTQysdekDVtyvrgflgrMLFSGedgvkKVK--VLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITA 475
Cdd:cd03228 75 RKNIA-YVPQ-----DP---------FLFSG-----TIRenILSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|..
gi 2124998340 476 LNNGLVKFPG---VLLFSSRDHQIVQttANRI 504
Cdd:cd03228 135 ILEALRALAKgktVIVIAHRLSTIRD--ADRI 164
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-230 |
1.43e-14 |
|
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: 72.83 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIIT-------PGERLSFLQQD---HFQyddymv 81
Cdd:cd03292 13 GTAAL-DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKigvVFQ------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 lDTVMMGNARLYE-IMKEKEVIYAKedftdedgikaselegefaamnGWEAESDAATLLNGLGIDAELHDKAMKdLNGPE 160
Cdd:cd03292 86 -DFRLLPDRNVYEnVAFALEVTGVP----------------------PREIRKRVPAALELVGLSHKHRALPAE-LSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-187 |
2.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALFeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDV-----IITPGER---LSFLQQD---HFQYDDymv 81
Cdd:PRK13634 20 RRALY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKnkkLKPLRKKvgiVFQFPE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmmgnARLYEIMKEKEVIYAKEDFtdedGIKASelegefaamngwEAESDAATLLNGLGIDAELHDKAMKDLNGPEK 161
Cdd:PRK13634 96 --------HQLFEETVEKDICFGPMNF----GVSEE------------DAKQKAREMIELVGLPEELLARSPFELSGGQM 151
|
170 180
....*....|....*....|....*.
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
2.12e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 72.75 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI-----ITP----GERLSFLQQDHFQYDDYMVLDTVMMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkdITNlppeKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 89 nARLYEIMK---EKEVIyakedftdedgikaselegEFAAMngweaesdaatllngLGIDAELHDKAmKDLNGPEKVKVL 165
Cdd:cd03299 96 -LKKRKVDKkeiERKVL-------------------EIAEM---------------LGIDHLLNRKP-ETLSGGEQQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHD 211
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-230 |
2.45e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 72.29 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHfqYDDYMVLDtv 85
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDLPPKD--RDIAMVFQ-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 mmgNARLYEIMKEKEVIY--AKEDFTDEDGIKaselegefaamngwEAESDAATLlngLGIDAELHDKAmKDLNGPEKVK 163
Cdd:cd03301 80 ---NYALYPHMTVYDNIAfgLKLRKVPKDEID--------------ERVREVAEL---LQIEHLLDRKP-KQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 164 VLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-230 |
2.58e-14 |
|
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: 72.60 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQ---------------QDHFQY 76
Cdd:cd03256 13 GKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLKgkalrqlrrqigmifQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 DDYMVLDTVMMGnaRLyeimkekeviyakedftdedGIKASelegeFAAMNGWEAESD---AATLLNGLGIdAELHDKAM 153
Cdd:cd03256 91 ERLSVLENVLSG--RL--------------------GRRST-----WRSLFGLFPKEEkqrALAALERVGL-LDKAYQRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDpassRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
.
gi 2124998340 230 I 230
Cdd:cd03256 223 I 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-198 |
3.97e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.67 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 21 NIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI--ITPGERLSFLQQDHFQYDDYMVLDTVMMGNARLYEIMKE 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFSHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 99 KEVIyakedftdEDGIKASELEGEFAAMngweaesdaatllngLGIDAeLHDKAMKDLNGPEKVKVLLAQALFGNPDILL 178
Cdd:PRK10938 103 AEII--------QDEVKDPARCEQLAQQ---------------FGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180
....*....|....*....|
gi 2124998340 179 LDEPTNHLDLDAIAWLEEFL 198
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELL 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-216 |
4.18e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.82 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 31 GLIGANGAGKSTFLRILSGQLEPSKGDViiTPGERLSFLQQdhfqyddYMVLDTvmmgNARLYEIMKEKeviyAKEDFTD 110
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQ-------YISPDY----DGTVEEFLRSA----NTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 111 edgikaselegefaamNGWEAEsdaatLLNGLGIDaELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLD- 189
Cdd:COG1245 433 ----------------SYYKTE-----IIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEq 490
|
170 180 190
....*....|....*....|....*....|...
gi 2124998340 190 ------AIAWLEEfliNFDNTVIVVSHDRYFLN 216
Cdd:COG1245 491 rlavakAIRRFAE---NRGKTAMVVDHDIYLID 520
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-531 |
4.22e-14 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQ------AYFPLDSg 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrriGYVPQRA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 393 sEFDNEYTI-VEwltqysdekDV-----TYVRGFLGRmlFSGEDgvkKVKV-------------------LSGGEKVRCL 447
Cdd:COG1121 85 -EVDWDFPItVR---------DVvlmgrYGRRGLFRR--PSRAD---REAVdealervgledladrpigeLSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 448 LSKMMISGANVLLLDEPTNHLDMES---ITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMEIvpGGKLIdKITTYDEYL 524
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATeeaLYELLRELRREGKTILVVTHDLGAVREYFDRVLLL--NRGLV-AHGPPEEVL 226
|
....*..
gi 2124998340 525 ESDEMAR 531
Cdd:COG1121 227 TPENLSR 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-510 |
4.57e-14 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 71.39 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVG----GnelaKTTLFQILTGEMEPDEGTYKWG---VTTSQ-------- 384
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGpsgsG----KSTLLRALADLDPPTSGEIYLDgkpLSAMPppewrrqv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 385 AYFPLDSGSeFDNeyTIVEWLT---QYSDEK-DVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVR-CLLSKMMIsGANVL 459
Cdd:COG4619 77 AYVPQEPAL-WGG--TVRDNLPfpfQLRERKfDRERALELLERLGLPPDILDKPVERLSGGERQRlALIRALLL-QPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 460 LLDEPTNHLDMES---ITALNNGLVKFPGV-LLFSSRDHQIVQTTANRIMEIVPG 510
Cdd:COG4619 153 LLDEPTSALDPENtrrVEELLREYLAEEGRaVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-231 |
5.46e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGE----------------- 64
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 65 -------RLSFLQQdHFQYDDYM-VLDTVMMGNARLYEIMKEkeviyakedftdedgikaselegefaamngwEAESDAA 136
Cdd:PRK10619 86 qlrllrtRLTMVFQ-HFNLWSHMtVLENVMEAPIQVLGLSKQ-------------------------------EARERAV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 137 TLLNGLGIDAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIA---WLEEFLINFDNTVIVVSHDRY 213
Cdd:PRK10619 134 KYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMG 213
|
250
....*....|....*...
gi 2124998340 214 FLNKVCTQIADIDYGKIK 231
Cdd:PRK10619 214 FARHVSSHVIFLHQGKIE 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-470 |
9.53e-14 |
|
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: 69.39 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 321 TVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwgVTtsqayfpLDSGSefDNEYT 400
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE----IL-------LDGKD--LASLS 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 401 IVE------WLTQYSDEKDVTYvrgFLGRMLFSgedgvkkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDM 470
Cdd:cd03214 68 PKElarkiaYVPQALELLGLAH---LADRPFNE----------LSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-465 |
1.15e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQ----QDH-----FQ----YDDYM 80
Cdd:COG1129 18 KAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-GEPVRFRSprdaQAAgiaiiHQelnlVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNarlyEIMKEKeviyakedFTDedgikaselegeFAAMNgweaeSDAATLLNGLGIDAELHDKaMKDLNGPE 160
Cdd:COG1129 96 VAENIFLGR----EPRRGG--------LID------------WRAMR-----RRARELLARLGLDIDPDTP-VGDLSVAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLeeflinFDN---------TVIVVSHdryFLNKVcTQIAD------- 224
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREVERL------FRIirrlkaqgvAIIYISH---RLDEV-FEIADrvtvlrd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 225 ---IDYGKIKlyagnyDFwyeSSQLLIRQMkeankkkeekikelqefISRfsanaskskqatsrkralekiELDDIQPss 301
Cdd:COG1129 216 grlVGTGPVA------EL---TEDELVRLM-----------------VGR---------------------ELEDLFP-- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 302 rkypyidfRPNREIGNEVLTVEGLSktidGEKILDDITFTLNHDDKVAFVGgneLA---KTTLFQILTGEMEPDEGT-YK 377
Cdd:COG1129 247 --------KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAG---LVgagRTELARALFGADPADSGEiRL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 378 WGV-----TTSQA------YFPLDSGSE--------FDNeyTIVEWLTQYS------DEKDVTYVRGFLGRMlfsgedGV 432
Cdd:COG1129 312 DGKpvrirSPRDAiragiaYVPEDRKGEglvldlsiREN--ITLASLDRLSrgglldRRRERALAEEYIKRL------RI 383
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2124998340 433 K------KVKVLSGG--EKVrcLLSKMMISGANVLLLDEPT 465
Cdd:COG1129 384 KtpspeqPVGNLSGGnqQKV--VLAKWLATDPKVLILDEPT 422
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-525 |
1.19e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.48 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT--------YKWGVTTSQ--AYFPL 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedvARDPAEVRRriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 390 DSGseFDNEYTIVEWLTQYSD---------EKDVTYVRGFLGrmLFSGEDgvKKVKVLSGGEKVRCLLSKMMISGANVLL 460
Cdd:COG1131 81 EPA--LYPDLTVRENLRFFARlyglprkeaRERIDELLELFG--LTDAAD--RKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 461 LDEPTNHLDMESITALNNGLVKF--PGV-LLFSSrdHQI--VQTTANRIMeIVPGGKLIDKITTYD---EYLE 525
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELaaEGKtVLLST--HYLeeAERLCDRVA-IIDKGRIVADGTPDElkaRLLE 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
319-534 |
1.27e-13 |
|
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: 73.43 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEK-ILDDITFTLNHDDKVAFVGGNELAKTTLFQIL-------TGEMEPDEGtYKWGvttsqaYFPLD 390
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfNGEARPQPG-IKVG------YLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 391 SgsEFDNEYTIVEwltqySDEKDVTYVRGFLGR-----MLFSGED----------------------------------- 430
Cdd:TIGR03719 77 P--QLDPTKTVRE-----NVEEGVAEIKDALDRfneisAKYAEPDadfdklaaeqaelqeiidaadawdldsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 431 -----GVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIM 505
Cdd:TIGR03719 150 lrcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWIL 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 2124998340 506 EIvPGGKLIDKITTYDEYLE----------SDEMARKRQ 534
Cdd:TIGR03719 230 EL-DRGRGIPWEGNYSSWLEqkqkrleqeeKEESARQKT 267
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-210 |
1.49e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALFeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQYDDYMVLDTVMMGNARLY 93
Cdd:PRK13643 20 RALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 94 EIMKEKEVIYAKEDFtdedGIKASElegefaamngweAESDAATLLNGLGIDAELHDKAMKDLNGPEKVKVLLAQALFGN 173
Cdd:PRK13643 99 EETVLKDVAFGPQNF----GIPKEK------------AEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAME 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2124998340 174 PDILLLDEPTNHLDLDA---IAWLEEFLINFDNTVIVVSH 210
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-230 |
1.57e-13 |
|
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: 69.87 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII------TPGERLSFLQQD--- 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkltDDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 73 ---HFQYDDYM-VLDTVMMGnarlyeIMKEKeviyakedftdedgikaselegefaAMNGWEAESDAATLLNGLGIDael 148
Cdd:cd03262 81 vfqQFNLFPHLtVLENITLA------PIKVK-------------------------GMSKAEAEERALELLEKVGLA--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 149 hDKAMK---DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEFLInfdnTVIVVSHDRYFLNKV 218
Cdd:cd03262 127 -DKADAypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvgevLDVMKDLAEEGM----TMVVVTHEMGFAREV 201
|
250
....*....|..
gi 2124998340 219 CTQIADIDYGKI 230
Cdd:cd03262 202 ADRVIFMDDGRI 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
1.73e-13 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 69.81 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVG-----KKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII------TPGERLSFLQ 70
Cdd:cd03293 1 LEVRNVSKTYGggggaVTAL-EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 71 QDH--FQYddYMVLDTVMMGnarlyeimkekeviyakedftdedgikaseLEGEFAAMNGWEAESDAATLLNGLGiDAEl 148
Cdd:cd03293 80 QQDalLPW--LTVLDNVALG------------------------------LELQGVPKAEARERAEELLELVGLS-GFE- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 149 hDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHD 211
Cdd:cd03293 126 -NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-229 |
2.56e-13 |
|
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: 68.18 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGE---RLSFLQQDHFQYDdym 80
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdlrdlDLESlrkNIAYVPQDPFLFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vlDTVmmgnarlyeimkeKEVIyakedftdedgikaselegefaamngweaesdaatllnglgidaelhdkamkdLNGPE 160
Cdd:cd03228 90 --GTI-------------RENI-----------------------------------------------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLD-AIAWLEEFLINFDN-TVIVVSHdRYFLNKVCTQIADIDYGK 229
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPEtEALILEALRALAKGkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-470 |
2.81e-13 |
|
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: 69.69 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQ----------AYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLASlsrrelarriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 388 PLDSGSEFDneYTIVE-----------WLTQYSDEkDVTYVRGFLGRMlfsgedGV-----KKVKVLSGGEKVRCLLSKM 451
Cdd:COG1120 81 PQEPPAPFG--LTVRElvalgryphlgLFGRPSAE-DREAVEEALERT------GLehladRPVDELSGGERQRVLIARA 151
|
170
....*....|....*....
gi 2124998340 452 MISGANVLLLDEPTNHLDM 470
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDL 170
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
2.90e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDViitpgerlsflqqdhfqyddyMV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---------------------TV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMMGNARLYEimKEKEVIYAKEDFTDEDGIKASELE-GEFAAMNGWEAESDAATLLNGlgidAELHDKA---MKDLN 157
Cdd:PRK13536 101 LGVPVPARARLAR--ARIGVVPQFDNLDLEFTVRENLLVfGRYFGMSTREIEAVIPSLLEF----ARLESKAdarVSDLS 174
|
170 180 190
....*....|....*....|....*....|
gi 2124998340 158 GPEKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
320-527 |
3.21e-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: 72.10 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEK-ILDDITFTLNHDDKVAFVG----GnelaKTTLFQILTGEMEPDEGTYKWGVTtsqayfPLDSGSE 394
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGpsgaG----KSTLLNLLLGFLPPYSGSILINGV------DLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 395 FD----------NEY----TIVEWLT----QYSDEK-----DVTYVRGFLGR-------MLfsGEDGVKkvkvLSGGEKV 444
Cdd:COG4988 407 ASwrrqiawvpqNPYlfagTIRENLRlgrpDASDEEleaalEAAGLDEFVAAlpdgldtPL--GEGGRG----LSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 445 RCLLSKMMISGANVLLLDEPTNHLDMESITALNNGLVKFPG---VLLFSSRDHQIVQttANRI--MEivpGGKLIDkITT 519
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrtVILITHRLALLAQ--ADRIlvLD---DGRIVE-QGT 554
|
....*...
gi 2124998340 520 YDEYLESD 527
Cdd:COG4988 555 HEELLAKN 562
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-230 |
3.44e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.35 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGERL------ 66
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkvndpKVDERLirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 67 SFLQQDHFqYDDYMVLDTVMMGNARLYEIMKEkeviyakedftdedgikaselegefaamngwEAESDAATLLNGLGIDA 146
Cdd:PRK09493 81 MVFQQFYL-FPHLTALENVMFGPLRVRGASKE-------------------------------EAEKQARELLAKVGLAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 147 ELHDKAmKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----------LDAIAwlEEFLinfdnTVIVVSHDRYFLN 216
Cdd:PRK09493 129 RAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpelrhevlkvMQDLA--EEGM-----TMVIVTHEIGFAE 200
|
250
....*....|....
gi 2124998340 217 KVCTQIADIDYGKI 230
Cdd:PRK09493 201 KVASRLIFIDKGRI 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-226 |
4.02e-13 |
|
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: 69.00 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 17 FEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpgerlsflqqdhfqyDDYMVLDtvmMGNArlyeim 96
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR---------------HDGGWVD---LAQA------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 97 KEKEVIYAKEDftdEDG-----------IKASELEGEFAAMNGW---EAESDAATLLNGLGIDAELHDKAMKDLNGPEKV 162
Cdd:COG4778 83 SPREILALRRR---TIGyvsqflrviprVSALDVVAEPLLERGVdreEARARARELLARLNLPERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLDLD----AIAWLEEFLINfDNTVIVVSHDRYFLNKVCTQIADID 226
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAAnravVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
5.58e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.35 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGE---RLSFLQQDHFQYDdym 80
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdlTLESlrrQIGVVPQDTFLFS--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vlDTVmMGNarlyeimkekeVIYAKEDFTDEDGIKASElegefAAmngwEAESDAATLLNGLgiDAELHDKAMKdLNGPE 160
Cdd:COG1132 428 --GTI-REN-----------IRYGRPDATDEEVEEAAK-----AA----QAHEFIEALPDGY--DTVVGERGVN-LSGGQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAiawleEFLI--NFDN-----TVIVVSH 210
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTET-----EALIqeALERlmkgrTTIVIAH 533
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
9.27e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.04 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 19 DVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKG-----DVIITPGERLSFLQQDH------FQYDDymvldtvmm 87
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdDITITHKTKDKYIRPVRkrigmvFQFPE--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 88 gnARLYEIMKEKEVIYAKEDFtdedgikaselegefaAMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPEKVKVLLA 167
Cdd:PRK13646 96 --SQLFEDTVEREIIFGPKNF----------------KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2124998340 168 QALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHD 211
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
9.64e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 19 DVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDhfqyddymvlDTVMMGNARLYEIMKE 98
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN-GQPMSKLSSA----------AKAELRNQKLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 99 KEVIyakEDFTDEDGIKASELEGefaAMNGWEAESDAATLLNGLGIDAELHDKAmKDLNGPEKVKVLLAQALFGNPDILL 178
Cdd:PRK11629 96 HHLL---PDFTALENVAMPLLIG---KKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124998340 179 LDEPTNHLDL---DAI-AWLEEFLINFDNTVIVVSHD 211
Cdd:PRK11629 169 ADEPTGNLDArnaDSIfQLLGELNRLQGTAFLVVTHD 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
2.19e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 66.98 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLS----------FLQQ 71
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-GEDATdvpvqernvgFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 72 DHFQYDDYMVLDTVMMGnarlyeiMKEKEviyaKEDFTDEDGIKASELEgefaamngweaesdaatLLNGLGIDAeLHDK 151
Cdd:cd03296 82 HYALFRHMTVFDNVAFG-------LRVKP----RSERPPEAEIRAKVHE-----------------LLKLVQLDW-LADR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 152 AMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHD 211
Cdd:cd03296 133 YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
2.97e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 32 LIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH----------FQYDDYMVLDTVmmgNArlyeimkekev 101
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQMDEEAraklrakhvgFVFQSFMLIPTL---NA----------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 102 iyakedftdedgIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKdLNGPEKVKVLLAQALFGNPDILLLDE 181
Cdd:PRK10584 106 ------------LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2124998340 182 PTNHLDL---DAIAWLeEFLIN--FDNTVIVVSHD 211
Cdd:PRK10584 173 PTGNLDRqtgDKIADL-LFSLNreHGTTLILVTHD 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-230 |
3.58e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDViitpgerlsFLQQDHFQYddymvldtv 85
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDGEHIQH--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 mmgnarlyeiMKEKEV-----IYAKEDFTDEDgIKASEL--EGEF---AAMNGWEAESDAAT--LLNGLGIdAELHDKAM 153
Cdd:PRK10253 74 ----------YASKEVarrigLLAQNATTPGD-ITVQELvaRGRYphqPLFTRWRKEDEEAVtkAMQATGI-THLADQSV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDryfLNKVC---TQIADID 226
Cdd:PRK10253 142 DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQACryaSHLIALR 218
|
....
gi 2124998340 227 YGKI 230
Cdd:PRK10253 219 EGKI 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
4.54e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILS--GQLEPS---------KGDVIITPGER---- 65
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtitgsivyNGHNIYSPRTDtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 66 -----LSFLQQDHFQYDDYmvlDTVMMGnARLYEImKEKEVIyakeDFTDEDGIKASELegefaamngWEAESDaatlln 140
Cdd:PRK14239 85 rkeigMVFQQPNPFPMSIY---ENVVYG-LRLKGI-KDKQVL----DEAVEKSLKGASI---------WDEVKD------ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 141 glgidaELHDKAMkDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSH 210
Cdd:PRK14239 141 ------RLHDSAL-GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTR 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-229 |
4.97e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSflQQDHF------- 74
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLC-GEPVP--SRARHarqrvgv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 75 --QYDDymvLDTvmmgnarlyeimkekeviyakeDFTDEDGIKaseLEGEFAAMNGWEAESDAATLLNGlgidAELHDKA 152
Cdd:PRK13537 85 vpQFDN---LDP----------------------DFTVRENLL---VFGRYFGLSAAAARALVPPLLEF----AKLENKA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 153 ---MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA--IAWlEEF--LINFDNTVIVVSHDRYFLNKVCTQIADI 225
Cdd:PRK13537 133 dakVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMW-ERLrsLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
....
gi 2124998340 226 DYGK 229
Cdd:PRK13537 212 EEGR 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
322-476 |
5.48e-12 |
|
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: 65.25 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 322 VEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKwgvttsqaYFpldsGSEFDNEYTI 401
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR--------VF----GKPLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 402 VEWLTQYSdEKDVTY---VRGF--LGRMLFSG-------------EDGVKKVKV----------LSGGEKVRCLLSKMMI 453
Cdd:cd03235 70 IGYVPQRR-SIDRDFpisVRDVvlMGLYGHKGlfrrlskadkakvDEALERVGLseladrqigeLSGGQQQRVLLARALV 148
|
170 180
....*....|....*....|...
gi 2124998340 454 SGANVLLLDEPTNHLDMESITAL 476
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDI 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-223 |
5.54e-12 |
|
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: 68.89 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 27 GNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHF------QYDdymVLDTVMMGNARLYeimkeke 100
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQnmgycpQFD---AIDDLLTGREHLY------- 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 101 vIYAKedftdEDGIKASELEgefaAMNGWEAESdaatllNGLGIDAelhDKAMKDLNGPEKVKVLLAQALFGNPDILLLD 180
Cdd:TIGR01257 2035 -LYAR-----LRGVPAEEIE----KVANWSIQS------LGLSLYA---DRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2124998340 181 EPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKVCTQIA 223
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRLA 2141
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-476 |
6.34e-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: 67.77 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDG-EKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwgVTTSQAyfPLDSGSEfDNE 398
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE----VTLDGV--PVSSLDQ-DEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 399 YTIVEWLTQ-------------------YSDEkDVTYV--RGFLGRMLFSGEDGVKKV-----KVLSGGEKVRCLLSKMM 452
Cdd:TIGR02868 408 RRRVSVCAQdahlfdttvrenlrlarpdATDE-ELWAAleRVGLADWLRALPDGLDTVlgeggARLSGGERQRLALARAL 486
|
170 180
....*....|....*....|....
gi 2124998340 453 ISGANVLLLDEPTNHLDMESITAL 476
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-196 |
6.37e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.82 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 4 TSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPgerlsflQQDHFQYDDYmvld 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-------GPLDFQRDSI---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 tvmmgnarlyeimkEKEVIYAKEdftdEDGIKA--SELEGE--FAAMNG----WEAESDAAtlLNGLGidaelhDKAMKD 155
Cdd:cd03231 72 --------------ARGLLYLGH----APGIKTtlSVLENLrfWHADHSdeqvEEALARVG--LNGFE------DRPVAQ 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEE 196
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-211 |
7.49e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpgerlsflqqdhfqydDYMVldTVMMGNARL 92
Cdd:PRK13641 20 KKGL-DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA----------------GYHI--TPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 YEIMKEKEVIYakeDFTDEDGIKASELEG-EFAAMN-GW---EAESDAATLLNGLGIDAELHDKAMKDLNGPEKVKVLLA 167
Cdd:PRK13641 81 KKLRKKVSLVF---QFPEAQLFENTVLKDvEFGPKNfGFsedEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2124998340 168 QALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFD---NTVIVVSHD 211
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHN 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-505 |
8.28e-12 |
|
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: 64.59 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 321 TVEGLSKTI-DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGV--------TTSQAYFPLDS 391
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 392 GSEFDNEyTIVEWLTQYSDE--KDVTYVRGFLGRM-LFSGEDgvKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHL 468
Cdd:cd03226 81 DYQLFTD-SVREELLLGLKEldAGNEQAETVLKDLdLYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2124998340 469 D---MESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIM 505
Cdd:cd03226 158 DyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-187 |
1.02e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALFeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKG-----DVIITPGERLSFLQQDH------FQYDDYMVL 82
Cdd:PRK13649 21 RALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvdDTLITSTSKNKDIKQIRkkvglvFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 83 D-TVMmgnarlyeimkeKEVIYAKEDFtdedGIKASelegefaamngwEAESDAATLLNGLGIDAELHDKAMKDLNGPEK 161
Cdd:PRK13649 100 EeTVL------------KDVAFGPQNF----GVSQE------------EAEALAREKLALVGISESLFEKNPFELSGGQM 151
|
170 180
....*....|....*....|....*.
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-211 |
1.14e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFqyddymvldtv 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAF----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 mmgnARlyeimkekEVIYAKEDFTDEDGIKASELE-----------GEFAAMNGWEAEsDAATLLnGLgidAELHDKAMK 154
Cdd:PRK10575 84 ----AR--------KVAYLPQQLPAAEGMTVRELVaigrypwhgalGRFGAADREKVE-EAISLV-GL---KPLAHRLVD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 155 DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHD 211
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-514 |
2.16e-11 |
|
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: 63.37 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLnhDDKV-AFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQ---------AYFP 388
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL--GPGMyGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKqpqklrrriGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 389 LDSGseFDNEYTIVE------WLTQYSDEKDVTYVRGFLGRM-LFSGEDgvKKVKVLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:cd03264 79 QEFG--VYPNFTVREfldyiaWLKGIPSKEVKARVDEVLELVnLGDRAK--KKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 462 DEPTNHLDMESITALNNGLVKFPG--VLLFSSrdHQI--VQTTANRIMeIVPGGKLI 514
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEdrIVILST--HIVedVESLCNQVA-VLNKGKLV 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-210 |
2.58e-11 |
|
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: 63.79 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQYDDYMV-LDTVMMGNARL 92
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLRRAIGVVpQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 YEIMkekeviYAKEDFTDEDGIKASELegefaamngweaesdaatllnglgidAELHDKAMK--------------DLNG 158
Cdd:cd03253 93 YNIR------YGRPDATDEEVIEAAKA--------------------------AQIHDKIMRfpdgydtivgerglKLSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEflinfDNTVIVVSH 210
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDthtereiQAALRDVSK-----GRTTIVIAH 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-236 |
2.81e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII---TP-GERLSFLQQdhfqyddymvlDTVMMG 88
Cdd:COG4586 35 VEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyVPfKRRKEFARR-----------IGVVFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 89 N-ARL---------YEIMKEkevIYakedftdedGIKASELE---GEFAAMngweaesdaatllngLGIDaELHDKAMKD 155
Cdd:COG4586 103 QrSQLwwdlpaidsFRLLKA---IY---------RIPDAEYKkrlDELVEL---------------LDLG-ELLDTPVRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL--IN--FDNTVIVVSHDryfLN---KVCTQIADIDYG 228
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeYNreRGTTILLTSHD---MDdieALCDRVIVIDHG 231
|
....*...
gi 2124998340 229 KIkLYAGN 236
Cdd:COG4586 232 RI-IYDGS 238
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-187 |
2.81e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIitpGER-LSFLQQDHFqyddymVLDTVMMGNARL 92
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---AERsIAYVPQQAW------IMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 YEimkekeviyaKEDFTD-EDGIKASELEGEFAAMNGweaesdaatllnglGIDAELHDKAMkDLNGPEKVKVLLAQALF 171
Cdd:PTZ00243 744 FD----------EEDAARlADAVRVSQLEADLAQLGG--------------GLETEIGEKGV-NLSGGQKARVSLARAVY 798
|
170
....*....|....*.
gi 2124998340 172 GNPDILLLDEPTNHLD 187
Cdd:PTZ00243 799 ANRDVYLLDDPLSALD 814
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-182 |
3.12e-11 |
|
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: 63.33 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqdhfqyDDYMV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL----------------DGQDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMMGNARLyeimkekEVIY-AKE-----DFTDEDGIKASElegEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKd 155
Cdd:cd03218 65 TKLPMHKRARL-------GIGYlPQEasifrKLTVEENILAVL---EIRGLSKKEREEKLEELLEEFHITHLRKSKASS- 133
|
170 180
....*....|....*....|....*..
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEP 182
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-470 |
3.27e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.25 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG---------VTTSQ--AYFP 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaRAASRrvASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 389 LDSGSEFD-NEYTIVEW-----LTQYS--DEKDVTYVRGFLGRM---LFSGEDgvkkVKVLSGGEKVRCLLSKMMISGAN 457
Cdd:PRK09536 84 QDTSLSFEfDVRQVVEMgrtphRSRFDtwTETDRAAVERAMERTgvaQFADRP----VTSLSGGERQRVLLARALAQATP 159
|
170
....*....|...
gi 2124998340 458 VLLLDEPTNHLDM 470
Cdd:PRK09536 160 VLLLDEPTASLDI 172
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-230 |
4.52e-11 |
|
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: 63.01 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--TPG---------ERLSFLQQdhfqyDDYM 80
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgIDIrdisrkslrSMIGVVLQ-----DTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMmgnarlyeimkeKEVIYAKEDFTDEDGIKASELEGefaamngweaesdAATLLNGL--GIDAELHDKAmKDLNG 158
Cdd:cd03254 89 FSGTIM------------ENIRLGRPNATDEEVIEAAKEAG-------------AHDFIMKLpnGYDTVLGENG-GNLSQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL--INFDNTVIVVSHdRYFLNKVCTQIADIDYGKI 230
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH-RLSTIKNADKILVLDDGKI 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-187 |
5.06e-11 |
|
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: 62.67 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSK---GDVIITPGERLSFLQQDHFQY---DDYMV--LdT 84
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKCVAYvrqDDILLpgL-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 85 V-----MMGNARLYEIMKEKEviyakedftdedgikaselegefaamngwEAESDAATLLNGLGiDAELHDKAMKDLNGP 159
Cdd:cd03234 98 VretltYTAILRLPRKSSDAI-----------------------------RKKRVEDVLLRDLA-LTRIGGNLVKGISGG 147
|
170 180
....*....|....*....|....*...
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:cd03234 148 ERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
7.80e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDhfqyddym 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ-GKPLDYSKRG-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgnarLYEIMKEKEVIYAKED----FTDEDGIKASELEGEFAAmngwEAE-----SDAATLlnglgIDAE-LHD 150
Cdd:PRK13638 72 -----------LLALRQQVATVFQDPEqqifYTDIDSDIAFSLRNLGVP----EAEitrrvDEALTL-----VDAQhFRH 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 151 KAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEfLINFDNTVIVVSHD 211
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRR-IVAQGNHVIISSHD 195
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
322-542 |
1.08e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 322 VEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLF---------------QILTGEME---------------- 370
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamhaidgipkncQILHVEQEvvgddttalqcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 371 --------------PDEGTYKWGVTTSQAYFPLDSGSEFD-------NEYTIVEWLTQYSDEKDVTYVrgfLGRMLFSGE 429
Cdd:PLN03073 260 iertqlleeeaqlvAQQRELEFETETGKGKGANKDGVDKDavsqrleEIYKRLELIDAYTAEARAASI---LAGLSFTPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 430 DGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMEIvP 509
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL-H 415
|
250 260 270
....*....|....*....|....*....|...
gi 2124998340 510 GGKLIDKITTYDEYLESDEMARKRQTYSIQSEE 542
Cdd:PLN03073 416 GQKLVTYKGDYDTFERTREEQLKNQQKAFESNE 448
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
322-476 |
1.09e-10 |
|
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: 61.33 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 322 VEGLSKTIDG--EKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG----VTTSQAYFPLDSGSEF 395
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 396 dneytivewltQYSD--------EKDVTYVrgfLGRMLFSGEDGVKKVKV-----------------LSGGEKVRCLLSK 450
Cdd:cd03225 82 -----------QNPDdqffgptvEEEVAFG---LENLGLPEEEIEERVEEalelvgleglrdrspftLSGGQKQRVAIAG 147
|
170 180
....*....|....*....|....*.
gi 2124998340 451 MMISGANVLLLDEPTNHLDMESITAL 476
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRREL 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
320-469 |
1.22e-10 |
|
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: 64.02 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEK--ILDDITFTLNHDDKVAFVG----GnelaKTTLFQILTGEMEPDEGTYKWG-------------- 379
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGpsgsG----KSTLLALLLRFLDPQSGSITLGgvdlrdldeddlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 380 ---VTTSQAYFpldsgseFDNeyTIVEWLT----QYSDE------KDV---TYVRGF---LGRMLfsGEDGVKkvkvLSG 440
Cdd:COG4987 410 riaVVPQRPHL-------FDT--TLRENLRlarpDATDEelwaalERVglgDWLAALpdgLDTWL--GEGGRR----LSG 474
|
170 180
....*....|....*....|....*....
gi 2124998340 441 GEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLD 503
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-187 |
1.85e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLE--PSKGDVIItpgerlsflQQDHFqYDDYMVLD 83
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV---------PDNQF-GREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 TvmmgnarlyeimkekevIYAKEDFTdedgikaselegefaamngweaesDAATLLNGLGI-DAELHDKAMKDLNGPEKV 162
Cdd:COG2401 105 A-----------------IGRKGDFK------------------------DAVELLNAVGLsDAVLWLRRFKELSTGQKF 143
|
170 180
....*....|....*....|....*
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-482 |
2.03e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGK-KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGqLEPS---KGDVIITpGERLSFlqqdhfqyddYMV 81
Cdd:PRK13549 10 NITKTFGGvKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFE-GEELQA----------SNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMMGNARLY-EIMKEKEVIYAKEDFTDEDGIKASELegEFAAMNgweaeSDAATLLNGLGIDAELHDKAMkDLNGPE 160
Cdd:PRK13549 77 RDTERAGIAIIHqELALVKELSVLENIFLGNEITPGGIM--DYDAMY-----LRAQKLLAQLKLDINPATPVG-NLGLGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDryfLNKV---CTQIADIDYGKiklYA 234
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHK---LNEVkaiSDTICVIRDGR---HI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 235 GNYDFWYESSQLLIRQMkeankkkeekikelqefISRfsanaskskqatsrkralekiELddiqpsSRKYPYIdfrpNRE 314
Cdd:PRK13549 223 GTRPAAGMTEDDIITMM-----------------VGR---------------------EL------TALYPRE----PHT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 315 IGNEVLTVEGLS---KTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMepdEGTYKWGV----------T 381
Cdd:PRK13549 255 IGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY---PGRWEGEIfidgkpvkirN 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 382 TSQAyfpLDSG----SEFDNEYTIV-----------EWLTQYS------DEKDVTYVRGFLGRMLFSGEDGVKKVKVLSG 440
Cdd:PRK13549 332 PQQA---IAQGiamvPEDRKRDGIVpvmgvgknitlAALDRFTggsridDAAELKTILESIQRLKVKTASPELAIARLSG 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2124998340 441 GEKVRCLLSKMMISGANVLLLDEPTNHLDMES---ITALNNGLVK 482
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAkyeIYKLINQLVQ 453
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
2.19e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGErlsflqqdhfqyddym 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgnarlYEIMKEKEVI-YA------KEDFTDEDGIkaselegEF-AAMNGwEAESDAATLLNGLGIDAELHDKA 152
Cdd:PRK13539 66 ------------IDDPDVAEAChYLghrnamKPALTVAENL-------EFwAAFLG-GEELDIAAALEAVGLAPLAHLPF 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124998340 153 mKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEE 196
Cdd:PRK13539 126 -GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-473 |
2.21e-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: 60.20 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQAYFPLDSGSEF--- 395
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYlgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 396 ----DNEYTIVEWLTQYSDEKDVTYVRGFLGRMLFSG-EDgvKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDM 470
Cdd:cd03231 81 apgiKTTLSVLENLRFWHADHSDEQVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
...
gi 2124998340 471 ESI 473
Cdd:cd03231 159 AGV 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-469 |
2.26e-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: 59.36 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGvttsqayfpldsGSEFdney 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------GKEV---- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 tivewltQYSDEKDvtyvrgflgrmlfSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:cd03216 65 -------SFASPRD-------------ARRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-211 |
2.56e-10 |
|
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: 61.23 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 26 EGNCYGLIGANGAGKSTFLRILSGQLEPSKG--------DVIITP--GERLsflqQDHF--------------QYDDymV 81
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwDEILDEfrGSEL----QNYFtkllegdvkvivkpQYVD--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMMGNARlyEIMKEKEVIYAKEDFtdedgIKASELEGefaamngweaesdaatllnglgidaeLHDKAMKDLNGPEK 161
Cdd:cd03236 99 IPKAVKGKVG--ELLKKKDERGKLDEL-----VDQLELRH--------------------------VLDRNIDQLSGGEL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 162 VKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEfLINFDNTVIVVSHD 211
Cdd:cd03236 146 QRVAIAAALARDADFYFFDEPSSYLDikqrLNAARLIRE-LAEDDNYVLVVEHD 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
330-532 |
2.73e-10 |
|
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: 62.93 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQ----------AYFPLD----SGSE 394
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDLRQidpaslrrqiGVVLQDvflfSGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 395 FDNeytIVEWLTQYSDEK-----DVTYVRGFLGRM-----LFSGEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLLDEP 464
Cdd:COG2274 566 REN---ITLGDPDATDEEiieaaRLAGLHDFIEALpmgydTVVGEGGSN----LSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 465 TNHLDMESITALNNGLVKFPG---VLLFSSRDHQIVQttANRI--MEivpGGKLIDkITTYDEYLESDEMARK 532
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKgrtVIIIAHRLSTIRL--ADRIivLD---KGRIVE-DGTHEELLARKGLYAE 705
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
3.07e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKG-----DVIItpGERLSFLQQDHFQY 76
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLL--GGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 DDYM-------------VLDTVMMGnARLYEIMKEKEVIYAKEDFTDEDGIkaselegefaamngWEAESDaatllnglg 143
Cdd:PRK14271 100 RRRVgmlfqrpnpfpmsIMDNVLAG-VRAHKLVPRKEFRGVAQARLTEVGL--------------WDAVKD--------- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 144 idaELHDKAMKdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHD 211
Cdd:PRK14271 156 ---RLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
3.20e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.16 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLR--VGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqdhfqydd 78
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 ymvlDTVMMGNARLYEIMKEKEVIYAKED-----FTDEDGIkASELEGE---FAAMngWEAESDAATllnGLGIDAELhD 150
Cdd:PRK13632 69 ----DGITISKENLKEIRKKIGIIFQNPDnqfigATVEDDI-AFGLENKkvpPKKM--KDIIDDLAK---KVGMEDYL-D 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 151 KAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF----DNTVIVVSHD 211
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD 202
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-470 |
3.34e-10 |
|
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: 60.60 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG---VTTSQA------YFPLD 390
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgvdLHGLSRrararrVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 391 SGSEFDNEYTIVE------------WLTQYSDekDVTYVRGFLGRMLFSgEDGVKKVKVLSGGEKVRCLLSKMMISGANV 458
Cdd:TIGR03873 82 QDSDTAVPLTVRDvvalgriphrslWAGDSPH--DAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKL 158
|
170
....*....|..
gi 2124998340 459 LLLDEPTNHLDM 470
Cdd:TIGR03873 159 LLLDEPTNHLDV 170
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
3.88e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.63 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPS-----KGDVIITpGERLSFLQQDH--- 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLF-GRNIYSPDVDPiev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 -------FQYDD----YMVLDTVMMGnARLYEIMKEKEVIyakeDFTDEDGIKASELegefaamngWEAESDaatllngl 142
Cdd:PRK14267 84 rrevgmvFQYPNpfphLTIYDNVAIG-VKLNGLVKSKKEL----DERVEWALKKAAL---------WDEVKD-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 143 gidaELHDKAmKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSHDRYFLNKVCT 220
Cdd:PRK14267 142 ----RLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSD 216
|
250
....*....|
gi 2124998340 221 QIADIDYGKI 230
Cdd:PRK14267 217 YVAFLYLGKL 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-211 |
4.52e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--TPgerLSFLQQDhfqyddymvld 83
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtAP---LAEARED----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 TVMM-GNARLyeiMKEKEVIyakedftDEDGIKaseLEGEfaamngWEAESDAAtlLNGLGidaeLHDKAMK---DLNGP 159
Cdd:PRK11247 83 TRLMfQDARL---LPWKKVI-------DNVGLG---LKGQ------WRDAALQA--LAAVG----LADRANEwpaALSGG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHldLDAIAWLE-EFLI-------NFdnTVIVVSHD 211
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGA--LDALTRIEmQDLIeslwqqhGF--TVLLVTHD 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-188 |
4.90e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 5 SNITLRVgkKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDviITPGERLSFLQQDHFqyddymvldt 84
Cdd:TIGR01271 432 SNFSLYV--TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK--IKHSGRISFSPQTSW---------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 85 VMMGNARlyeimkeKEVIY--AKEDFTDEDGIKASELEGEFAAMngweAESDAATLLNGlGIdaelhdkamkDLNGPEKV 162
Cdd:TIGR01271 498 IMPGTIK-------DNIIFglSYDEYRYTSVIKACQLEEDIALF----PEKDKTVLGEG-GI----------TLSGGQRA 555
|
170 180
....*....|....*....|....*.
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLDL 188
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
5.59e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNI--TLRVGKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSflqqdhfqydd 78
Cdd:PRK13652 3 LIETRDLcySYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-GEPIT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 ymvldtvmmgNARLYEIMKEKEVIYAKEDftdeDGIKASELEGE--FAAMN-GWEAESDA---ATLLNGLGIDaELHDKA 152
Cdd:PRK13652 70 ----------KENIREVRKFVGLVFQNPD----DQIFSPTVEQDiaFGPINlGLDEETVAhrvSSALHMLGLE-ELRDRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 153 MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYG 228
Cdd:PRK13652 135 PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
..
gi 2124998340 229 KI 230
Cdd:PRK13652 215 RI 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
6.36e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsFLQQDHFQ---YDDYMVLDTVMMGNA 90
Cdd:PRK13651 21 KAL-DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW-------IFKDEKNKkktKEKEKVLEKLVIQKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 91 RLYEIMKEKEV--------IYAK----EDFTDEDGIkaselegeFAAMN----GWEAESDAATLLNGLGIDAELHDKAMK 154
Cdd:PRK13651 93 RFKKIKKIKEIrrrvgvvfQFAEyqlfEQTIEKDII--------FGPVSmgvsKEEAKKRAAKYIELVGLDESYLQRSPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 155 DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIawlEEFLINFDN------TVIVVSHD 211
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGV---KEILEIFDNlnkqgkTIILVTHD 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-218 |
6.49e-10 |
|
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: 58.69 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILsgqlepskgdviitpgerlsflqqdhfqyddymvldtv 85
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI-------------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 mMGNARlYEIMkEKEVIYAKEDFTDedgIKASE--LEGEFAAMNgWEAESDAATLLNGLgidaelhdkamKDLN----GP 159
Cdd:cd03217 47 -MGHPK-YEVT-EGEILFKGEDITD---LPPEEraRLGIFLAFQ-YPPEIPGVKNADFL-----------RYVNegfsGG 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEF---LINFDNTVIVVSHDRYFLNKV 218
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-472 |
7.06e-10 |
|
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: 59.06 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKT--IDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT---YKWGVTTSQAYFPLDSGS- 393
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayiNGYSIRTDRKAARQSLGYc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 394 -EFDN---EYTIVEWLTQYS-----DEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEP 464
Cdd:cd03263 81 pQFDAlfdELTVREHLRFYArlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
....*...
gi 2124998340 465 TNHLDMES 472
Cdd:cd03263 161 TSGLDPAS 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
324-469 |
9.55e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 324 GLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQayfpldsgseFDNEYTIVE 403
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ----------FGREASLID 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 404 WLTQYSDEKDVTYVrgfLGRMLFSgeDGV---KKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:COG2401 105 AIGRKGDFKDAVEL---LNAVGLS--DAVlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-230 |
1.20e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.43 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPgerlsflqqdhfqyddymv 81
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 LDTVMMGNARLYEImKEKEVIYAKEDFT---DEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAmKDLNG 158
Cdd:PRK10070 90 VDIAKISDAELREV-RRKKIAMVFQSFAlmpHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP-DELSG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF----DNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-480 |
1.44e-09 |
|
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: 57.23 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEK--ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPLDSGSefdn 397
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 398 eytIVEWLTQysdekDVtyvrgflgrMLFSG---EDgvkkvkVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESIT 474
Cdd:cd03246 77 ---HVGYLPQ-----DD---------ELFSGsiaEN------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
....*.
gi 2124998340 475 ALNNGL 480
Cdd:cd03246 134 ALNQAI 139
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-210 |
1.45e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.40 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKK--ALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpG------------ERLS 67
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-GhdvrdytlaslrRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 68 FLQQDHFQYDDymvldTVMmgnarlyeimkeKEVIYAKEDFTDEDGIKASELegefaamngweaeSDAATLLNGL--GID 145
Cdd:cd03251 80 LVSQDVFLFND-----TVA------------ENIAYGRPGATREEVEEAARA-------------ANAHEFIMELpeGYD 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 146 AELHDKAMKdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL-------DAIAWLEEflinfDNTVIVVSH 210
Cdd:cd03251 130 TVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALDTeserlvqAALERLMK-----NRTTFVIAH 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-230 |
1.73e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVG-KKALFeDVNIKFTEGNCYGLIGANGAGKSTFLRIL-------SGQLE--PSKGDVIITPGER-LSFLQ 70
Cdd:PRK11124 3 IQLNGINCFYGaHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiaGNHFDFSKTPSDKaIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 71 QD---HF-QYDDYMVLdTVMmgnarlyeimkekeviyakEDFTdEDGIKASELEGEfaamngwEAESDAATLLNGLgida 146
Cdd:PRK11124 82 RNvgmVFqQYNLWPHL-TVQ-------------------QNLI-EAPCRVLGLSKD-------QALARAEKLLERL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 147 ELHDKAMK---DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEFLInfdnTVIVVSHDRYFLN 216
Cdd:PRK11124 130 RLKPYADRfplHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI----TQVIVTHEVEVAR 205
|
250
....*....|....
gi 2124998340 217 KVCTQIADIDYGKI 230
Cdd:PRK11124 206 KTASRVVYMENGHI 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.81e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRV--GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSflqqdhfqYDd 78
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEPIK--------YD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 ymvldtvmmgNARLYEIMKEKEVIYAKEDftdeDGIKASELEGE--FAAMN----GWEAESDAATLLNGLGIDAeLHDKA 152
Cdd:PRK13639 70 ----------KKSLLEVRKTVGIVFQNPD----DQLFAPTVEEDvaFGPLNlglsKEEVEKRVKEALKAVGMEG-FENKP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 153 MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHD 211
Cdd:PRK13639 135 PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
2.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSkgDVIITPGERLSFLQQDHFQYDdym 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIY--DSKIKVDGKVLYFGKDIFQID--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vldtvmmgnarLYEIMKEKEVIYAKED----FTDEDGIkASELEGEfAAMNGWEAESDAATLLNGLGIDAELHDK---AM 153
Cdd:PRK14246 85 -----------AIKLRKEVGMVFQQPNpfphLSIYDNI-AYPLKSH-GIKEKREIKKIVEECLRKVGLWKEVYDRlnsPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 154 KDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-198 |
2.45e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.98 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGErlSFLQQDHFQyddymv 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP--LAEQRDEPH------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmmgnarlyeimkeKEVIYAKEdftdEDGIKA--SELEG-EFAAMNGWEAESDAATLLNGLGIDAeLHDKAMKDLNG 158
Cdd:TIGR01189 73 -----------------ENILYLGH----LPGLKPelSALENlHFWAAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2124998340 159 PEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL 198
Cdd:TIGR01189 131 GQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
2.74e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.04 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNI--TLRVGKK---ALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDH-- 73
Cdd:PRK11153 1 MIELKNIskVFPQGGRtihAL-NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQDLTALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 ---------FQYDDYMVLDTVmMGNARLyeimkekeviyakedftdedgikASELEGEFAAmngwEAESDAATLLNGLGI 144
Cdd:PRK11153 79 karrqigmiFQHFNLLSSRTV-FDNVAL-----------------------PLELAGTPKA----EIKARVTELLELVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 145 dAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD---LDAI-AWLEEflIN--FDNTVIVVSHDRYFLNKV 218
Cdd:PRK11153 131 -SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSIlELLKD--INreLGLTIVLITHEMDVVKRI 207
|
250
....*....|..
gi 2124998340 219 CTQIADIDYGKI 230
Cdd:PRK11153 208 CDRVAVIDAGRL 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-210 |
3.14e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 57.55 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 17 FEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQ----QDHFQY--DDYMVLDTVMMGNa 90
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLNlrwlRSQIGLvsQEPVLFDGTIAEN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 91 rlyeimkekeVIYAKEDFTDEDGIKASELEgefaamngwEAESDAATLLNGLgiDAELHDKAMKdLNGPEKVKVLLAQAL 170
Cdd:cd03249 97 ----------IRYGKPDATDEEVEEAAKKA---------NIHDFIMSLPDGY--DTLVGERGSQ-LSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2124998340 171 FGNPDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSH 210
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-211 |
3.18e-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: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGK-KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGErlsflqqdhfqydDYM 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-GE-------------DIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEIMKekevIYAKEDFTDEDGIkaseleGEFAAMNGWEAE---SDAATLLNGLGID-AELHDKAMKDL 156
Cdd:cd03295 67 EQDPVELRRKIGYVIQQ----IGLFPHMTVEENI------ALVPKLLKWPKEkirERADELLALVGLDpAEFADRYPHEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 157 NGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN----TVIVVSHD 211
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelgkTIVFVTHD 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-229 |
3.20e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpgerlsflQQDHFQYDDYMVLDTV 85
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--------GVDLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 MMGNARLYEIMK-EKEVIYakedftdedGIKASELEGEfaamngwEAESDAATLLnGLGIDAELHDKAMKDLNGPEKVKV 164
Cdd:PRK11607 96 MFQSYALFPHMTvEQNIAF---------GLKQDKLPKA-------EIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 165 LLAQALFGNPDILLLDEPTNHLD--------LDAIAWLEEFLInfdnTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERVGV----TCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-225 |
3.22e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqDHFQYDDYM 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-----------NNINYNKLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEimkEKEVIyakedftDEDGIKASELEGEFAAMNGW--------EAESDAATLLNGLGIDAELHDKa 152
Cdd:PRK09700 74 HKLAAQLGIGIIYQ---ELSVI-------DELTVLENLYIGRHLTKKVCgvniidwrEMRVRAAMMLLRVGLKVDLDEK- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 153 MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLeeFLI-----NFDNTVIVVSH---------DRYFLNK- 217
Cdd:PRK09700 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLImnqlrKEGTAIVYISHklaeirricDRYTVMKd 220
|
250
....*....|..
gi 2124998340 218 ---VCT-QIADI 225
Cdd:PRK09700 221 gssVCSgMVSDV 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-476 |
3.81e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGvttsqayfplDSGSEFDNE 398
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD----------GGDIDDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 399 YTIVEWLTQYSDEKDVTYV-------RGFLGRMLFSGEDGVKKV----------KVLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:PRK13539 72 AEACHYLGHRNAMKPALTVaenlefwAAFLGGEELDIAAALEAVglaplahlpfGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170
....*....|....*
gi 2124998340 462 DEPTNHLDMESITAL 476
Cdd:PRK13539 152 DEPTAALDAAAVALF 166
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
334-463 |
4.50e-09 |
|
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: 56.77 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 334 ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKwgvTTSQAYFPLDSGSEFDNEYTIVEwltqysdekd 413
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT---VRGRVSSLLGLGGGFNPELTGRE---------- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 414 vtYVRgFLGRML----------------FS--GEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDE 463
Cdd:cd03220 104 --NIY-LNGRLLglsrkeidekideiieFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
320-494 |
5.09e-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: 58.84 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGE-KILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQ----------AYF 387
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADadadswrdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 388 P----LDSGSEFDN---------EYTIVEWLTQ-YSDEKDVTYVRGfLGRMLfsGEDGVKkvkvLSGGEKVRCLLSKMMI 453
Cdd:TIGR02857 402 PqhpfLFAGTIAENirlarpdasDAEIREALERaGLDEFVAALPQG-LDTPI--GEGGAG----LSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124998340 454 SGANVLLLDEPTNHLDMESITALNNGLVKFPG---VLLFSSRDH 494
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrtVLLVTHRLA 518
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-505 |
5.15e-09 |
|
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: 55.66 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGvttsqayfpldsGSEFDNEY 399
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID------------GEDLTDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 TIVEWLtqysdEKDVTYVrgFLGRMLFSGEDGVKKVK-VLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDME---SITA 475
Cdd:cd03229 69 DELPPL-----RRRIGMV--FQDFALFPHLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRA 141
|
170 180 190
....*....|....*....|....*....|.
gi 2124998340 476 LNNGLVKFPGV-LLFSSRDHQIVQTTANRIM 505
Cdd:cd03229 142 LLKSLQAQLGItVVLVTHDLDEAARLADRVV 172
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
6.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLE--PS---KGDVIITpgerlsflQQDHFQY 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLD--------GQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 DDYMVLDTVMMgnarLYEIMKEKEVIYAKEDFTDedGIKASEL---EGEFAAMNGWEAESdaatllnglgidAELHDKAM 153
Cdd:PRK14247 76 DVIELRRRVQM----VFQIPNPIPNLSIFENVAL--GLKLNRLvksKKELQERVRWALEK------------AQLWDEVK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 154 KDLNGP-------EKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSH 210
Cdd:PRK14247 138 DRLDAPagklsggQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-188 |
7.09e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.17 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGkkALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGdvIITPGERLSFLQQDHFqyddymv 81
Cdd:cd03291 40 LFFSNLCLVGA--PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHSGRISFSSQFSW------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtVMMGNARlyeimkeKEVIY--AKEDFTDEDGIKASELEGEFAAMngweAESDAATLLNGlGIdaelhdkamkDLNGP 159
Cdd:cd03291 109 ---IMPGTIK-------ENIIFgvSYDEYRYKSVVKACQLEEDITKF----PEKDNTVLGEG-GI----------TLSGG 163
|
170 180
....*....|....*....|....*....
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLDL 188
Cdd:cd03291 164 QRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-187 |
1.05e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 16 LFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLS------------FLQQD----------H 73
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinlkwwrskigVVSQDpllfsnsiknN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 FQYDDYMVLDTVMMGN------ARLYEIMKEKEVIYAKEDFTDEDGIKASELEGEFAAMNGWEAESDAATLlnGLGIDAE 147
Cdd:PTZ00265 480 IKYSLYSLKDLEALSNyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVV--DVSKKVL 557
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 148 LHD--KAMKD------------LNGPEKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:PTZ00265 558 IHDfvSALPDkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-230 |
1.05e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.81 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSflQQDHFQYDDYMVL---DTVMMGN 89
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLV--QYDHHYLHRQVALvgqEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 90 ARlyeimkeKEVIYAKEDFTDEDGIKAselegefAAMngweaESDAATLLNGL--GIDAELHDKAMKdLNGPEKVKVLLA 167
Cdd:TIGR00958 570 SV-------RENIAYGLTDTPDEEIMA-------AAK-----AANAHDFIMEFpnGYDTEVGEKGSQ-LSGGQKQRIAIA 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 168 QALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSHdRYFLNKVCTQIADIDYGKI 230
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSV 691
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
1.37e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.53 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKftEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGER-LSFLQQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalPPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 72 DHFQYDDYMVLDTVMMG---NARLyeimkekeviyakedfTDEDgikaselegefaamngweaESDAATLLNGLGIdAEL 148
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlrpGLKL----------------TAEQ-------------------RAQVEQALERVGL-AGL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 149 HDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHD 211
Cdd:COG3840 123 LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-235 |
1.44e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.01 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqdhfqydDYMVLDTVMMGnar 91
Cdd:PRK13636 18 GTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF-----------------DGKPIDYSRKG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 92 lyeIMKEKEVIYAKEDFTDEDGIKASELEG-EFAAMN----GWEAESDAATLLNGLGIdAELHDKAMKDLNGPEKVKVLL 166
Cdd:PRK13636 77 ---LMKLRESVGMVFQDPDNQLFSASVYQDvSFGAVNlklpEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 167 AQALFGNPDILLLDEPTNHLDLDAIAWLEEFLIN----FDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAG 235
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqkeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-187 |
1.63e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 54.48 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRV------GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPS--KGDVII--------TPGER 65
Cdd:cd03213 4 LSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLIngrpldkrSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 66 LSFLQQDHFQYDDYMVLDTVMmgnarlyeimkekeviyakedftdedgikaselegeFAAmngweaesdaatllnglgid 145
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLM------------------------------------FAA-------------------- 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2124998340 146 aelhdkAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:cd03213 108 ------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-476 |
1.86e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.55 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPldSGSEFDNEY--TIVE---- 403
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVP--QRSEVPDSLplTVRDlvam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 404 ----------WLTQySDEKDVTY------VRGFLGRMLfsGEdgvkkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNH 467
Cdd:NF040873 81 grwarrglwrRLTR-DDRAAVDDalervgLADLAGRQL--GE--------LSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
....*....
gi 2124998340 468 LDMESITAL 476
Cdd:NF040873 150 LDAESRERI 158
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-183 |
2.07e-08 |
|
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: 54.75 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGK-KALFeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI-----IT---PGER----LSF 68
Cdd:cd03224 1 LEVENLNAGYGKsQILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrdITglpPHERaragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 69 LQQDHFQYDDYMVLDTVMMGnarlyeimkekevIYAKEDFTDEDGIKasELEGEFAAMngweaesdaatllnglgidAEL 148
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLG-------------AYARRRAKRKARLE--RVYELFPRL-------------------KER 125
|
170 180 190
....*....|....*....|....*....|....*
gi 2124998340 149 HDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPT 183
Cdd:cd03224 126 RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-187 |
2.53e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.09 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGK-----KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLqQDH-- 73
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-GKDVTKL-PEYkr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 -------FQyddymvlDTvMMGNArlyeimkekeviyakEDFTDED----------------GIKASELEgEFAAMngwe 130
Cdd:COG1101 79 akyigrvFQ-------DP-MMGTA---------------PSMTIEEnlalayrrgkrrglrrGLTKKRRE-LFREL---- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 131 aesdAATLlnGLGIDAELHDKaMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:COG1101 131 ----LATL--GLGLENRLDTK-VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-515 |
2.71e-08 |
|
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: 54.65 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 335 LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGvttsqAYFPLDSGSEFDNEYTIV------------ 402
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPWKRRKKFLRRIGVVfgqktqlwwdlp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 403 -----EWLTQYSDEKDVTYVRGF--LGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMESITA 475
Cdd:cd03267 112 vidsfYLLAAIYDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2124998340 476 LNNGLVKF-----PGVLLfSSRDHQIVQTTANRIMEIVPGGKLID 515
Cdd:cd03267 192 IRNFLKEYnrergTTVLL-TSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-211 |
3.23e-08 |
|
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: 54.96 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 19 DVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-------TPGERLSFLQQDH----FQYDDYM----VLD 83
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdgqdiaaMSRKELRELRRKKismvFQSFALLphrtVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 TVMMGnarlyeimkekeviyakedftdedgikaSELEGEFAAmngwEAESDAATLLNGLGIDAELHDKAmKDLNGPEKVK 163
Cdd:cd03294 122 NVAFG----------------------------LEVQGVPRA----EREERAAEALELVGLEGWEHKYP-DELSGGMQQR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 164 VLLAQALFGNPDILLLDEPTNHLD-LDAIAWLEEFL---INFDNTVIVVSHD 211
Cdd:cd03294 169 VGLARALAVDPDILLMDEAFSALDpLIRREMQDELLrlqAELQKTIVFITHD 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-230 |
3.57e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKG-----DVIITPGERLS-------- 67
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSqqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 68 FLQQDHFQYDDY------MVLDTVMmgnarlyeimkEKEVIYAKEDFTdedgikaselegefaamngwEAESDAATLLNG 141
Cdd:PRK11264 83 LRQHVGFVFQNFnlfphrTVLENII-----------EGPVIVKGEPKE--------------------EATARARELLAK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 142 LGIDAElHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEflinFDNTVIVVSHDRYF 214
Cdd:PRK11264 132 VGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQ----EKRTMVIVTHEMSF 206
|
250
....*....|....*.
gi 2124998340 215 LNKVCTQIADIDYGKI 230
Cdd:PRK11264 207 ARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-211 |
3.79e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.74 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSflqqdhfqyddymvLDTVmmgnarlYEIMK 97
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-GDLLT--------------EENV-------WDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 98 EKEVIYAKED-----FTDEDGIkASELEGEFAAMNGWEAESDAATLLNGLgidAELHDKAMKDLNGPEKVKVLLAQALFG 172
Cdd:PRK13650 82 KIGMVFQNPDnqfvgATVEDDV-AFGLENKGIPHEEMKERVNEALELVGM---QDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2124998340 173 NPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHD 211
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
332-469 |
4.01e-08 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 53.09 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 332 EKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwgVTTSQayFPLDSGSEFDNEYTIVewLTQYSDE 411
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE----ITLDG--VPVSDLEKALSSLISV--LNQRPYL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 412 KDVTyVRGFLGRMLfsgedgvkkvkvlSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:cd03247 87 FDTT-LRNNLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-230 |
4.49e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.01 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSflQQDHfqydDYMVLDTVMMGnarlyeimk 97
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD-GKPIS--QYEH----KYLHSKVSLVG--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 98 EKEVIYAKEdFTDE--DGIKASELEGEFAAMNGWEAESDAATLlnGLGIDAELHDKAMKdLNGPEKVKVLLAQALFGNPD 175
Cdd:cd03248 95 QEPVLFARS-LQDNiaYGLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 176 ILLLDEPTNHLDLDAIAWLEEFLI--NFDNTVIVVSHdRYFLNKVCTQIADIDYGKI 230
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYdwPERRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-482 |
4.49e-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: 53.77 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 331 GEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQ----------AYFPLD----SGSEF 395
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRDisrkslrsmiGVVLQDtflfSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 396 DNeytiVEWLTQYSDEKDVTYVRGFLGRMLF--SGEDGVKKV-----KVLSGGEKVRCLLSKMMISGANVLLLDEPTNHL 468
Cdd:cd03254 95 EN----IRLGRPNATDEEVIEAAKEAGAHDFimKLPNGYDTVlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170
....*....|....
gi 2124998340 469 DMESITALNNGLVK 482
Cdd:cd03254 171 DTETEKLIQEALEK 184
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
4.68e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqQDHFQYDDYMVLDTVMMGNARLYEIMK 97
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV----------GDIYIGDKKNNHELITNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 98 E-KEVIYAKEDFTD----EDGIKASELEGEFA-AMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPEKVKVLLAQALF 171
Cdd:PRK13631 113 ElRRRVSMVFQFPEyqlfKDTIEKDIMFGPVAlGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 172 GNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-59 |
5.39e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 53.83 E-value: 5.39e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGK-KALFeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI 59
Cdd:COG0410 3 MLEVENLHAGYGGiHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR 61
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-230 |
5.88e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.70 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKK-----ALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII-----T--PGERLSF 68
Cdd:COG1135 1 MIELENLSKTFPTKggpvtAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdlTalSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 69 LQQD------HFQyddymVLD--TVmMGN-ARLYEIMK-EKEVIYAKedftdedgikaselegefaamngweaesdAATL 138
Cdd:COG1135 80 ARRKigmifqHFN-----LLSsrTV-AENvALPLEIAGvPKAEIRKR-----------------------------VAEL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 139 LN--GLGidaelhDKAMK---DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL---DAI-AWLEEflIN--FDNTVIV 207
Cdd:COG1135 125 LElvGLS------DKADAypsQLSGGQKQRVGIARALANNPKVLLCDEATSALDPettRSIlDLLKD--INreLGLTIVL 196
|
250 260
....*....|....*....|....*..
gi 2124998340 208 VSHD----RyflnKVCTQIADIDYGKI 230
Cdd:COG1135 197 ITHEmdvvR----RICDRVAVLENGRI 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
330-472 |
6.92e-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: 53.55 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY---------KW---------GVTTS--QAYFPL 389
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerrgGEdvwelrkriGLVSPalQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 390 D--------SGSeFDneyTIVEWlTQYSDEkDVTYVRGFLGRMlfsgedGV-----KKVKVLSGGEKVRCLLSKMMISGA 456
Cdd:COG1119 94 DetvldvvlSGF-FD---SIGLY-REPTDE-QRERARELLELL------GLahladRPFGTLSQGEQRRVLIARALVKDP 161
|
170
....*....|....*.
gi 2124998340 457 NVLLLDEPTNHLDMES 472
Cdd:COG1119 162 ELLILDEPTAGLDLGA 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-230 |
8.38e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpGERlsflqqdhfqyDDYMVLDTVM--MGN 89
Cdd:TIGR01257 942 GRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV--GGK-----------DIETNLDAVRqsLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 90 ARLYEIM------KEKEVIYAkedftdedgikasELEGEfaamnGW-EAESDAATLLNGLGIDAELHDKAmKDLNGPEKV 162
Cdd:TIGR01257 1008 CPQHNILfhhltvAEHILFYA-------------QLKGR-----SWeEAQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQR 1068
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN--TVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
9.19e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGErlsflqqdhfqyddymvldtvmMGNAR 91
Cdd:PRK13647 17 GTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------------------VNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 92 LYEIMKEKEVIYAKEDftdeDGIKASELEGEFA------AMNGWEAESDAATLLNGLGIDaELHDKAMKDLNGPEKVKVL 165
Cdd:PRK13647 74 EKWVRSKVGLVFQDPD----DQVFSSTVWDDVAfgpvnmGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHD 211
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHD 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-469 |
1.12e-07 |
|
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: 52.67 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW---GVTTSQ----AYFPLDSG 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkPLDIAArnriGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 393 seFDNEYTIVEWLTQYSDEKDVT------YVRGFLGRmLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTN 466
Cdd:cd03269 81 --LYPKMKVIDQLVYLAQLKGLKkeearrRIDEWLER-LELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
...
gi 2124998340 467 HLD 469
Cdd:cd03269 158 GLD 160
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-226 |
1.13e-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: 51.77 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGK-KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGqLEPS-KGDVIITPGERLSFLQQdhfqyDDY 79
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLLFLPQ-----RPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 80 MVLDTvmmgnarLYEImkekeVIYAkedftdedgikaselegefaamngWEAEsdaatllnglgidaelhdkamkdLNGP 159
Cdd:cd03223 75 LPLGT-------LREQ-----LIYP------------------------WDDV-----------------------LSGG 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 160 EKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLInfdnTVIVVSHdRYFLNKVCTQIADID 226
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSALDEESedrlYQLLKELGI----TVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
1.20e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSgQLEPSKGDVIITpgERLSFLQQDHFQYddymv 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVE--GRVEFFNQNIYER----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 82 ldtvmmgNARLYEIMKEKEVIYAKEDFTDED-------GIKaselegefaaMNGWEAESDAATLLNGLGIDAELHD---- 150
Cdd:PRK14258 80 -------RVNLNRLRRQVSMVHPKPNLFPMSvydnvayGVK----------IVGWRPKLEIDDIVESALKDADLWDeikh 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 151 ---KAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF----DNTVIVVSHD 211
Cdd:PRK14258 143 kihKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-230 |
1.26e-07 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 52.50 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALfeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIIT--------PGER-LSFLQQD 72
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaapPADRpVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 73 HFQYDDYMVLDTVMMG---NARLYEIMKEK-EVIYAKedftdedgikaselegefaamngweaesdaatllngLGIdAEL 148
Cdd:cd03298 79 NNLFAHLTVEQNVGLGlspGLKLTAEDRQAiEVALAR------------------------------------VGL-AGL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 149 HDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIAD 224
Cdd:cd03298 122 EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVF 201
|
....*.
gi 2124998340 225 IDYGKI 230
Cdd:cd03298 202 LDNGRI 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-187 |
1.38e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPG--------ER----LSFLQQDHFQYDDYMVLDTV 85
Cdd:PRK10895 20 EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhARarrgIGYLPQEASIFRRLSVYDNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 MmgnarlyeimkekEVIYAKEDFTDED-GIKASELEGEFaamngweaesDAATLLNGLGidaelhdkamKDLNGPEKVKV 164
Cdd:PRK10895 100 M-------------AVLQIRDDLSAEQrEDRANELMEEF----------HIEHLRDSMG----------QSLSGGERRRV 146
|
170 180
....*....|....*....|...
gi 2124998340 165 LLAQALFGNPDILLLDEPTNHLD 187
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-186 |
1.43e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQqdhfqyddymVLDTVMMGNAR 91
Cdd:PRK11288 16 GVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-GQEMRFAS----------TTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 92 LYEimkekEVIYAKEdFTDEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKaMKDLNGPEKVKVLLAQALF 171
Cdd:PRK11288 84 IYQ-----ELHLVPE-MTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTP-LKYLSIGQRQMVEIAKALA 156
|
170
....*....|....*
gi 2124998340 172 GNPDILLLDEPTNHL 186
Cdd:PRK11288 157 RNARVIAFDEPTSSL 171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-216 |
1.46e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.54 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 32 LIGANGAGKSTFLRILSGqLEPSKGDVIIT-------PGERLS----FL--QQDH------FQYddymvLDTVMMGNARl 92
Cdd:COG4138 27 LIGPNGAGKSTLLARMAG-LLPGQGEILLNgrplsdwSAAELArhraYLsqQQSPpfampvFQY-----LALHQPAGAS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 yeimkekeviyakedftdedgikASELEGEFAAmngweaesdaatLLNGLGIDAELHdKAMKDLNGPEKVKVLLAQALF- 171
Cdd:COG4138 100 -----------------------SEAVEQLLAQ------------LAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVLLq 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 172 ----GNPD--ILLLDEPTNHLD------LDaiAWLEEFL---InfdnTVIVVSHDryfLN 216
Cdd:COG4138 144 vwptINPEgqLLLLDEPMNSLDvaqqaaLD--RLLRELCqqgI----TVVMSSHD---LN 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-464 |
1.48e-07 |
|
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: 52.55 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG---VTTSQ---------AYF 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdITKLPmhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 388 PLDSgSEF------DNEYTIVEwLTQYSDEKDVTYVRGFLGrmlfsgEDGVKKVK-----VLSGGEKVRCLLSKMMISGA 456
Cdd:cd03218 81 PQEA-SIFrkltveENILAVLE-IRGLSKKEREEKLEELLE------EFHITHLRkskasSLSGGERRRVEIARALATNP 152
|
....*...
gi 2124998340 457 NVLLLDEP 464
Cdd:cd03218 153 KFLLLDEP 160
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-513 |
1.53e-07 |
|
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: 52.11 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEK----ILDDITFTLNHDDKVAFVG----GnelaKTTLFQILTGEMEPDEGTYKW-GVTTS------- 383
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGpsgsG----KSTLLNILGGLDRPTSGEVRVdGTDISklsekel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 384 ------------QAYFPLDSGSEFDNeytiVEW---LTQYSDEKDVTYVRGFLGRMlfsGEDGVKKVKV--LSGGEKVRC 446
Cdd:cd03255 77 aafrrrhigfvfQSFNLLPDLTALEN----VELpllLAGVPKKERRERAEELLERV---GLGDRLNHYPseLSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 447 LLSKMMISGANVLLLDEPTNHLDMES---ITALNNGLVKFPGV-LLFSSRDHQIVQtTANRIMEIVpGGKL 513
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETgkeVMELLRELNKEAGTtIVVVTHDPELAE-YADRIIELR-DGKI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-469 |
2.19e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.02 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 317 NEVLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT---------------YKWGVT 381
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTllfegedistlkpeiYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 382 TSQAYFPLDSGSEFDNeyTIVEWLTQySDEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:PRK10247 85 YCAQTPTLFGDTVYDN--LIFPWQIR-NQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
....*...
gi 2124998340 462 DEPTNHLD 469
Cdd:PRK10247 162 DEITSALD 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-198 |
2.57e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSfLQQDHFQYddym 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIR-RQRDEYHQ---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 vlDTVMMGNArlyeimkekeviyakedftdeDGIKaSELEGE-----FAAMNGWEAESDAATLLNGLGIdAELHDKAMKD 155
Cdd:PRK13538 75 --DLLYLGHQ---------------------PGIK-TELTALenlrfYQRLHGPGDDEALWEALAQVGL-AGFEDVPVRQ 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL 198
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
2.63e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGK-KALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSF----------- 68
Cdd:COG3845 5 ALELRGITKRFGGvVAN-DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-GKPVRIrsprdaialgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 69 --LQQdHFQ-YDDYMVLDTVMMGNARLyeimkekeviyaKEDFTDEDGIKA--SELEGEFaamngweaesdaatllnGLG 143
Cdd:COG3845 83 gmVHQ-HFMlVPNLTVAENIVLGLEPT------------KGGRLDRKAARAriRELSERY-----------------GLD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 144 IDAelhDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSH 210
Cdd:COG3845 133 VDP---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaeGKSIIFITH 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
319-477 |
2.71e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG---VTTSQ-----AYFPLD 390
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgktATRGDrsrfmAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 391 SGSEFDneytivewltqYSDEKDVTYVRGFLGRM-------------LFSGEDGVkkVKVLSGGEKVRCLLSKMMISGAN 457
Cdd:PRK13543 91 PGLKAD-----------LSTLENLHFLCGLHGRRakqmpgsalaivgLAGYEDTL--VRQLSAGQKKRLALARLWLSPAP 157
|
170 180
....*....|....*....|
gi 2124998340 458 VLLLDEPTNHLDMESITALN 477
Cdd:PRK13543 158 LWLLDEPYANLDLEGITLVN 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
2.99e-07 |
|
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: 51.47 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI--------ITPGER-LSFLQQD 72
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldgkditnLPPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 73 HFQYDDYMVLDTVMMGnarlyeiMKEKEViyakedftDEDGIKaselegefaamngweAESDAATLLNGLGidaELHDKA 152
Cdd:cd03300 81 YALFPHLTVFENIAFG-------LRLKKL--------PKAEIK---------------ERVAEALDLVQLE---GYANRK 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 153 MKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN----TVIVVSHD 211
Cdd:cd03300 128 PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-469 |
3.03e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSK--TIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQIL------TGEMEPDEGTY------KW----GVT 381
Cdd:TIGR01271 1218 MDVQGLTAkyTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstEGEIQIDGVSWnsvtlqTWrkafGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 382 tSQAYFPLdSGSEFDNeytiVEWLTQYSDEK------DV---TYVRGFLGRMLFSGEDGVKkvkVLSGGEKVRCLLSKMM 452
Cdd:TIGR01271 1298 -PQKVFIF-SGTFRKN----LDPYEQWSDEEiwkvaeEVglkSVIEQFPDKLDFVLVDGGY---VLSNGHKQLMCLARSI 1368
|
170
....*....|....*..
gi 2124998340 453 ISGANVLLLDEPTNHLD 469
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLD 1385
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-483 |
3.50e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.99 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEpdegtYKwgVTTSQAYFpldsgsefdney 399
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK-----YE--VTEGEILF------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 tivewltqysDEKDVT----YVRGFLGRMLFSGE----DGVKKVKVL-------SGGEKVRCLLSKMMISGANVLLLDEP 464
Cdd:cd03217 62 ----------KGEDITdlppEERARLGIFLAFQYppeiPGVKNADFLryvnegfSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170
....*....|....*....
gi 2124998340 465 TNHLDMESITALNNGLVKF 483
Cdd:cd03217 132 DSGLDIDALRLVAEVINKL 150
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-515 |
4.16e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 50.83 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEK----ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQAyfPLDS--- 391
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKE--PAEArrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 392 -GSEFDNEyTIVEWLTQysdEKDVTYVRGFLG--------------RMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGA 456
Cdd:cd03266 80 lGFVSDST-GLYDRLTA---RENLEYFAGLYGlkgdeltarleelaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 457 NVLLLDEPTNHLDMESITALNNGL--VKFPG-VLLFSSRDHQIVQTTANRIMeIVPGGKLID 515
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIrqLRALGkCILFSTHIMQEVERLCDRVV-VLHRGRVVY 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-229 |
4.30e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 50.55 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 16 LFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII------TPGErlSFLQQDhfqyddyMVLDTVMMGN 89
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVpgsiayVSQE--PWIQNG-------TIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 90 ArlYEIMKEKEViyakedftdedgIKASELEGEFAAMNGweaesdaatllnglGIDAELHDKAMkDLNGPEKVKVLLAQA 169
Cdd:cd03250 91 P--FDEERYEKV------------IKACALEPDLEILPD--------------GDLTEIGEKGI-NLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 170 LFGNPDILLLDEPTNHLDLDAIAWLEEFLIN----FDNTVIVVSHDRYFLNKvCTQIADIDYGK 229
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFENCILglllNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-375 |
4.35e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.31 E-value: 4.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 318 EVLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT 375
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE 58
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-211 |
4.37e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDV--------------IITPGERL 66
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipamsrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 67 SFLQQDHFQYDDYMVLDTV---MMGNARLYEIMKEKEVIYAKEdftdedgikASELEGefaamngweaesdAATLLNGlg 143
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVaypLREHTQLPAPLLHSTVMMKLE---------AVGLRG-------------AAKLMPS-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 144 idaelhdkamkDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEfLINFDN-----TVIVVSHD 211
Cdd:PRK11831 143 -----------ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK-LISELNsalgvTCVVVSHD 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-526 |
5.37e-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: 52.13 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGqLEPS---KGDVIITPGErlsfLQQDHfqyd 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSP----LKASN---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 78 dymVLDTVMMGNARLY-EIMKEKEVIYAKEDFTdedgikASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKDL 156
Cdd:TIGR02633 72 ---IRDTERAGIVIIHqELTLVPELSVAENIFL------GNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 157 NGPEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEFLInfdnTVIVVSHDRYFLNKVCTQIADIDYGK 229
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTeketeilLDIIRDLKAHGV----ACVYISHKLNEVKAVCDTICVIRDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 230 iklYAGNYDFWYESSQLLIRQMkeankkkeekikelqefISRfsanaskskqatsrkralekiELDDIQPssrkypyidf 309
Cdd:TIGR02633 219 ---HVATKDMSTMSEDDIITMM-----------------VGR---------------------EITSLYP---------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 310 RPNREIGNEVLTVEGLSK-TIDGEKI--LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMepdEGTYKWGVTTSQAy 386
Cdd:TIGR02633 248 HEPHEIGDVILEARNLTCwDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY---PGKFEGNVFINGK- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 387 fPLDSGS-------------EFDNEYTIVewlTQYSDEKDVTY--VRGFLGRMLFSGE-------DGVKKVKV------- 437
Cdd:TIGR02633 324 -PVDIRNpaqairagiamvpEDRKRHGIV---PILGVGKNITLsvLKSFCFKMRIDAAaelqiigSAIQRLKVktaspfl 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 438 ----LSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMES---ITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMEIVPG 510
Cdd:TIGR02633 400 pigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
570
....*....|....*....
gi 2124998340 511 ---GKLIDKITTYDEYLES 526
Cdd:TIGR02633 480 klkGDFVNHALTQEQVLAA 498
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
292-400 |
5.42e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.85 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 292 IELDDIqpsSRKYPyIDFRPNREIGNEVLtveGLSKTIDGEK-ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEME 370
Cdd:COG1134 5 IEVENV---SKSYR-LYHEPSRSLKELLL---RRRRTRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110
....*....|....*....|....*....|
gi 2124998340 371 PDEGTYKWGVTTSqayFPLDSGSEFDNEYT 400
Cdd:COG1134 78 PTSGRVEVNGRVS---ALLELGAGFHPELT 104
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
320-472 |
6.91e-07 |
|
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: 50.28 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKI--LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPLD------- 390
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrrnigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 391 --------SGSEFDNeytivewLT---QYSDEKDV----------TYVRGF---LGRMLfsGEDGVKkvkvLSGGEKVRC 446
Cdd:cd03245 83 vpqdvtlfYGTLRDN-------ITlgaPLADDERIlraaelagvtDFVNKHpngLDLQI--GERGRG----LSGGQRQAV 149
|
170 180
....*....|....*....|....*.
gi 2124998340 447 LLSKMMISGANVLLLDEPTNHLDMES 472
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNS 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-187 |
7.42e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDV------IITPGERLSFLQQDHF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkpVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 75 QYDDYMVLDTVMMGNarlyeimkekeviyakedftdedgikaselegEFAAMNGWEAESDAATLLNGLGIdAELHDKAMK 154
Cdd:PRK11248 81 LLPWRNVQDNVAFGL--------------------------------QLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIW 127
|
170 180 190
....*....|....*....|....*....|...
gi 2124998340 155 DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:PRK11248 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-242 |
9.30e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.24 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGdviitpgeRLSFLQQD--------- 72
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG--------HIRFHGTDvsrlhardr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 73 -------HFQYDDYM-VLDTVMMGNARLyeimkekeviyAKEDFTDEDGIKaselegefaamngweaeSDAATLLNGLGI 144
Cdd:PRK10851 75 kvgfvfqHYALFRHMtVFDNIAFGLTVL-----------PRRERPNAAAIK-----------------AKVTQLLEMVQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 145 dAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCT 220
Cdd:PRK10851 127 -AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDaqvrKELRRWLRQLHEELKFTSVFVTHDQEEAMEVAD 205
|
250 260
....*....|....*....|..
gi 2124998340 221 QIADIDYGKIKLYAGNYDFWYE 242
Cdd:PRK10851 206 RVVVMSQGNIEQAGTPDQVWRE 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
326-477 |
1.01e-06 |
|
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: 49.57 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 326 SKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGtykwgVTTSQAYfpldSGSEFDNEYTIVEWL 405
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-----VEGDIHY----NGIPYKEFAEKYPGE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 406 TQYSDEKDVTY----VRGFLGrmlFSGE-DGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDmeSITALN 477
Cdd:cd03233 85 IIYVSEEDVHFptltVRETLD---FALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTALE 156
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
322-528 |
1.07e-06 |
|
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: 49.81 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 322 VEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT--------------------YKWGVT 381
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgedisglseaelyrlrRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 382 -TSQAYFplDSGSEFDNeytIVEWLTQYSDEKDVTY---VRGFLGRM-LFSGEDgvKKVKVLSGGEKVRCLLSKMMISGA 456
Cdd:cd03261 83 fQSGALF--DSLTVFEN---VAFPLREHTRLSEEEIreiVLEKLEAVgLRGAED--LYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 457 NVLLLDEPTNHLD---MESITALNNGLVKFPGV-LLFSSRDHQIVQTTANRIMEIVPGGKLIDkiTTYDEYLESDE 528
Cdd:cd03261 156 ELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGKIVAE--GTPEELRASDD 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
1.17e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.37 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRV--GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFlqqdhfqydd 78
Cdd:PRK13644 1 MIRLENVSYSYpdGTPAL-ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 ymvldtvmmgnARLYEIMKEKEVIYAKEDfTDEDGiKASELEGEFAAMN----GWEAESDAATLLNGLGIDAELHdKAMK 154
Cdd:PRK13644 70 -----------SKLQGIRKLVGIVFQNPE-TQFVG-RTVEEDLAFGPENlclpPIEIRKRVDRALAEIGLEKYRH-RSPK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 155 DLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA-IAWLEEF--LINFDNTVIVVSHDRYFLNkVCTQIADIDYGKIK 231
Cdd:PRK13644 136 TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIV 214
|
.
gi 2124998340 232 L 232
Cdd:PRK13644 215 L 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-465 |
1.24e-06 |
|
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: 49.74 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG---VTTSQAY---------- 386
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgedITGLPPHeiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 387 F----PLDSGSEFDN---------EYTIVEWLTQYSDEKDVTYVRGFLGRMlfsGEDGVKKVKV--LSGGEKVRCLLSKM 451
Cdd:cd03219 81 FqiprLFPELTVLENvmvaaqartGSGLLLARARREEREARERAEELLERV---GLADLADRPAgeLSYGQQRRLEIARA 157
|
170
....*....|....
gi 2124998340 452 MISGANVLLLDEPT 465
Cdd:cd03219 158 LATDPKLLLLDEPA 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-470 |
1.52e-06 |
|
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: 49.54 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT-------------YKWGVTT---S 383
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEilldgkditnlppHKRPVNTvfqN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 384 QAYFPldSGSEFDNeytIVEWLT-QYSDEKDV-TYVRGFLgRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:cd03300 81 YALFP--HLTVFEN---IAFGLRlKKLPKAEIkERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
....*....
gi 2124998340 462 DEPTNHLDM 470
Cdd:cd03300 155 DEPLGALDL 163
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-183 |
1.62e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.49 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIitpgerlsFLQQDHFQYDDYM 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV--------FDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMmgnarlyEIMKEKEVIYAKedFTDEDGIkaselegefaAMNGWEAESD--AATLLNGLGIDAELHDKAMK---D 155
Cdd:PRK11614 77 IMREAV-------AIVPEGRRVFSR--MTVEENL----------AMGGFFAERDqfQERIKWVYELFPRLHERRIQragT 137
|
170 180
....*....|....*....|....*...
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPT 183
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-212 |
1.77e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.10 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 6 NITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERL--SFLQQDhfqyDDYMVLD 83
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-GEDVthRSIQQR----DICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 84 TVMmgnarLYEIMKEKE-VIYakedftdedGIKaselegefaaMNGWEAESDAATLLNGLG-ID-AELHDKAMKDLNGPE 160
Cdd:PRK11432 86 SYA-----LFPHMSLGEnVGY---------GLK----------MLGVPKEERKQRVKEALElVDlAGFEDRYVDQISGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 161 KVKVLLAQALFGNPDILLLDEPTNHLDL-------DAIAWLEEfliNFDNTVIVVSHDR 212
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQ---QFNITSLYVTHDQ 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
1.91e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDViitpgerlsflqqdHFQYDDYM 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------------HYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 81 VLDTVMMGNARLYEIMKekeviyakedfTD--------EDGIK----ASELEGEFAAMNGW----EAESDAATLLNGLGI 144
Cdd:PRK11701 72 LRDLYALSEAERRRLLR-----------TEwgfvhqhpRDGLRmqvsAGGNIGERLMAVGArhygDIRATAGDWLERVEI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 145 DAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL----INFDNTVIVVSHD 211
Cdd:PRK11701 141 DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrglvRELGLAVVIVTHD 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
298-469 |
2.03e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.22 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 298 QPSSRKYpyidFRPNREIGNevltvegLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT-- 375
Cdd:PRK11607 9 QAKTRKA----LTPLLEIRN-------LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQim 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 376 -----------YKWGVTT---SQAYFPldsgsEFDNEYTIVEWLTQYSDEKDVTYVRgfLGRML---FSGEDGVKKVKVL 438
Cdd:PRK11607 78 ldgvdlshvppYQRPINMmfqSYALFP-----HMTVEQNIAFGLKQDKLPKAEIASR--VNEMLglvHMQEFAKRKPHQL 150
|
170 180 190
....*....|....*....|....*....|.
gi 2124998340 439 SGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
319-477 |
2.39e-06 |
|
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: 48.32 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDG------EKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTG--EMEPDEGTYKW-GVTTSQAYFPL 389
Cdd:cd03213 3 TLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLInGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 390 DSGsefdneytivewltqYSDEKDVTY----VRGFLgrmLFSGedgvkKVKVLSGGEKVRCLLSKMMISGANVLLLDEPT 465
Cdd:cd03213 83 IIG---------------YVPQDDILHptltVRETL---MFAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170
....*....|..
gi 2124998340 466 NHLDmeSITALN 477
Cdd:cd03213 140 SGLD--SSSALQ 149
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-232 |
2.44e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.32 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGK------KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgERLSFLQQDH- 73
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV---DGLDTSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 ----------FQYDDYMVLDTVMmgnarlyeimkEKEVIYAKEDFtdedGIKASEL----EGEFAAMNGWEAESDAATLl 139
Cdd:PRK13633 81 wdirnkagmvFQNPDNQIVATIV-----------EEDVAFGPENL----GIPPEEIrervDESLKKVGMYEYRRHAPHL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 140 nglgidaelhdkamkdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD----LDAIAWLEEFLINFDNTVIVVSHdryFL 215
Cdd:PRK13633 145 ----------------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YM 205
|
250
....*....|....*....
gi 2124998340 216 NKV--CTQIADIDYGKIKL 232
Cdd:PRK13633 206 EEAveADRIIVMDSGKVVM 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
86-210 |
2.53e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 MMGNARLYEIMKekeviYAKEDFTDEDGIKASElegeFAAMNGWeaesdAATLLNGLGIDAELHDKAmkdLNGPEKVKVL 165
Cdd:PTZ00265 1306 MLFNMSIYENIK-----FGKEDATREDVKRACK----FAAIDEF-----IESLPNKYDTNVGPYGKS---LSGGQKQRIA 1368
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINF----DNTVIVVSH 210
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-210 |
2.58e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 16 LFEDVNIKFTEGNCYGLIGANGAGKSTFLRILsGQLEPSKGDVIITPGE-RLSFLQQdhfqyDDYMVLDTVmmgnarlye 94
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPAKgKLFYVPQ-----RPYMTLGTL--------- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 95 imkEKEVIY--AKEDFTDEdGIKASEL---------------EGEFAAMNGWeaesdaatllnglgidaelhdkaMKDLN 157
Cdd:TIGR00954 532 ---RDQIIYpdSSEDMKRR-GLSDKDLeqildnvqlthilerEGGWSAVQDW-----------------------MDVLS 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 158 GPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNTVIVVSH 210
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-222 |
2.71e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 20 VNIKFTEGNCYGLIGANGAGKSTFLRILSGQlepSKGDVIITPgerlsflqqDHFQYDDYMVLDtvMMGNARLYEIMKEK 99
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTA---------DRMRFDDIDLLR--LSPRERRKLVGHNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 100 EVIYAKE----DFTDEDG------IKASELEGEFAAMNGWEaESDAATLLNGLGIDAelHDKAMK----DLNGPEKVKVL 165
Cdd:PRK15093 92 SMIFQEPqsclDPSERVGrqlmqnIPGWTYKGRWWQRFGWR-KRRAIELLHRVGIKD--HKDAMRsfpyELTEGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL--INFDN--TVIVVSHDRYFLNKVCTQI 222
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNntTILLISHDLQMLSQWADKI 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
2.92e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.86 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLR---VGKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIItpgerlsflqqDHFQYDD 78
Cdd:PRK13635 6 IRVEHISFRypdAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-----------GGMVLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 79 ymvlDTVmmgnarlYEIMKEKEVIYAKED--F---TDEDGIkASELEGefaamNGWEAES-----DAAtlLNGLGIDAEL 148
Cdd:PRK13635 74 ----ETV-------WDVRRQVGMVFQNPDnqFvgaTVQDDV-AFGLEN-----IGVPREEmvervDQA--LRQVGMEDFL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 149 HDKAMKdLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD-------LDAIAWLEEfliNFDNTVIVVSHD 211
Cdd:PRK13635 135 NREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-531 |
3.08e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 22 IKFT--EGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQ--QDHfQYDDYMVLDTVMmgnarLYEIMK 97
Cdd:PRK15439 30 IDFTlhAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-GNPCARLTpaKAH-QLGIYLVPQEPL-----LFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 98 EKEVIYakedftdedgikaselegeFAAMNGWEAESDAATLLNGLGIDAELHDKAmKDLNGPEKVKVLLAQALFGNPDIL 177
Cdd:PRK15439 103 VKENIL-------------------FGLPKRQASMQKMKQLLAALGCQLDLDSSA-GSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 178 LLDEPTNHL---DLDAIAWLEEFLINFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLYAGNYDFwyeSSQLLIRQMkea 254
Cdd:PRK15439 163 ILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL---STDDIIQAI--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 255 nkkkeekikelqefisrfsANASKSKQAT-SRKRALEkielddiQPSSRKYPYIDFrpnreignEVLTVEGLSktidGEK 333
Cdd:PRK15439 237 -------------------TPAAREKSLSaSQKLWLE-------LPGNRRQQAAGA--------PVLTVEDLT----GEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 334 ILdDITFTLNHDDKVAFV-----GGNELAKTT--LFQILTGEMEPDEGTYKwGVTTSQA------YFPLD---SGSEFD- 396
Cdd:PRK15439 279 FR-NISLEVRAGEILGLAgvvgaGRTELAETLygLRPARGGRIMLNGKEIN-ALSTAQRlarglvYLPEDrqsSGLYLDa 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 397 ----NEYTIVE-----WLTQYSDEKDVTYVRGFLGrMLFSGEDgvKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNH 467
Cdd:PRK15439 357 plawNVCALTHnrrgfWIKPARENAVLERYRRALN-IKFNHAE--QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 468 LD----------MESITALNnglvkfPGVLLFSSRDHQIVQtTANRImEIVPGGKLIDKITTydEYLESDEMAR 531
Cdd:PRK15439 434 VDvsarndiyqlIRSIAAQN------VAVLFISSDLEEIEQ-MADRV-LVMHQGEISGALTG--AAINVDTIMR 497
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
330-472 |
4.81e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.39 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVG----GnelaKTTLFQILTGEMEPDEGTYKW-GVTTSQayFPLDS------------- 391
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGpsgsG----KSTLVNLLLRFYDPTSGRILIdGVDIRD--LTLESlrrqigvvpqdtf 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 392 ---GSEFDNeytIVEWLTQYSDEK-----DVTYVRGFLGRM-------LfsGEDGVKkvkvLSGGEKVRCLLSKMMISGA 456
Cdd:COG1132 425 lfsGTIREN---IRYGRPDATDEEveeaaKAAQAHEFIEALpdgydtvV--GERGVN----LSGGQRQRIAIARALLKDP 495
|
170
....*....|....*.
gi 2124998340 457 NVLLLDEPTNHLDMES 472
Cdd:COG1132 496 PILILDEATSALDTET 511
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-378 |
4.98e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.57 E-value: 4.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW 378
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW 60
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
319-476 |
5.00e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.19 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFP----LDSgse 394
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPqklyLDT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 395 fdneyTIVewLTqysdekdvtyVRGFLgrMLfsgEDGVKKVKV-------------------LSGGEKVRCLLSKMMISG 455
Cdd:PRK09544 81 -----TLP--LT----------VNRFL--RL---RPGTKKEDIlpalkrvqaghlidapmqkLSGGETQRVLLARALLNR 138
|
170 180
....*....|....*....|.
gi 2124998340 456 ANVLLLDEPTNHLDMESITAL 476
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVAL 159
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-232 |
5.15e-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: 46.92 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 14 KALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQdhfQYDDYMvldTVMMGNARLY 93
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-GVPVSDLEK---ALSSLI---SVLNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 94 eimkekeviyakedftdedgikaselegefaamngweaesdAATLLNGLGidaelhdkamKDLNGPEKVKVLLAQALFGN 173
Cdd:cd03247 88 -----------------------------------------DTTLRNNLG----------RRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 174 PDILLLDEPTNHLDLDAIAWLEEFLINF--DNTVIVVSHDRYFLNKVcTQIADIDYGKIKL 232
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
329-504 |
5.32e-06 |
|
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: 47.67 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 329 IDGEKILDDitFTLNHD-----DKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTsqaYFplDSGSEFD------- 396
Cdd:cd03297 4 VDIEKRLPD--FTLKIDfdlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LF--DSRKKINlppqqrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 397 -----NEYTIVEWLTQY----------SDEKDVTYVRGFLGRMlfsGEDGVKKVKV--LSGGEKVRCLLSKMMISGANVL 459
Cdd:cd03297 77 iglvfQQYALFPHLNVRenlafglkrkRNREDRISVDELLDLL---GLDHLLNRYPaqLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124998340 460 LLDEPTNHLDMESITALNNGLVK----FPGVLLFSSRDHQIVQTTANRI 504
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLADRI 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-68 |
9.41e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 9.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2124998340 21 NIKFT--EGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSF 68
Cdd:PRK15112 31 PLSFTlrEGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID-DHPLHF 79
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-211 |
9.76e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.49 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 13 KKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDviitpgerlsflqqdhfqyDDYMVLDTVMMGNARL 92
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP-------------------NSKITVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 YEIMKEKEVIYAKED-----FTDEDGIkASELEGEFAAMNgwEAESDAATLLNGLGIdAELHDKAMKDLNGPEKVKVLLA 167
Cdd:PRK13640 80 WDIREKVGIVFQNPDnqfvgATVGDDV-AFGLENRAVPRP--EMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 168 QALFGNPDILLLDEPTNHLD-------LDAIAWLEEflinfDN--TVIVVSHD 211
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDpagkeqiLKLIRKLKK-----KNnlTVISITHD 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
334-513 |
9.87e-06 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 47.08 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 334 ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT--------------YKWGVTTSQAYFP-LDSGSEFDNe 398
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlldgkpisqyehkYLHSKVSLVGQEPvLFARSLQDN- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 399 ytIVEWLTQYSDEK-----DVTYVRGFLGRMLFSGEDGV-KKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLDMES 472
Cdd:cd03248 108 --IAYGLQSCSFECvkeaaQKAHAHSFISELASGYDTEVgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124998340 473 ITALNNGLVKFP---GVLLFSSRDHQIVQttANRIMeIVPGGKL 513
Cdd:cd03248 186 EQQVQQALYDWPerrTVLVIAHRLSTVER--ADQIL-VLDGGRI 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-469 |
1.15e-05 |
|
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: 46.36 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQAYFPL--DSGSEFDN 397
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 398 eYTIVEWLTQYsdeKDVTYVrgfLGRMLFSGEDGVKKVKV-----------------LSGGEKVRCLLSKMMISGANVLL 460
Cdd:cd03259 81 -YALFPHLTVA---ENIAFG---LKLRGVPKAEIRARVREllelvglegllnrypheLSGGQQQRVALARALAREPSLLL 153
|
....*....
gi 2124998340 461 LDEPTNHLD 469
Cdd:cd03259 154 LDEPLSALD 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
320-469 |
1.15e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG---VTTSQAyfplDSGSEFD 396
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpVEGPGA----ERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 397 NEyTIVEW------------LTQYSDEKDVTYVRGFLGRMLFSGEdGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEP 464
Cdd:PRK11248 78 NE-GLLPWrnvqdnvafglqLAGVEKMQRLEIAHQMLKKVGLEGA-EKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
....*
gi 2124998340 465 TNHLD 469
Cdd:PRK11248 156 FGALD 160
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
319-531 |
1.28e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.81 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY----------------KWGVtt 382
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplharaRRGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 383 sqAYFPLDSG-----SEFDNEYTIVEWLTQYSDEK------------DVTYVRGFLGrmlfsgedgvkkvKVLSGGEKVR 445
Cdd:PRK10895 81 --GYLPQEASifrrlSVYDNLMAVLQIRDDLSAEQredranelmeefHIEHLRDSMG-------------QSLSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 446 CLLSKMMISGANVLLLDEPTNHLDMESITAL--------NNGLvkfpGVLLfssRDHQIVQTTAnrIME---IVPGGKLI 514
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIkriiehlrDSGL----GVLI---TDHNVRETLA--VCErayIVSQGHLI 216
|
250
....*....|....*..
gi 2124998340 515 DKiTTYDEYLESDEMAR 531
Cdd:PRK10895 217 AH-GTPTEILQDEHVKR 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-229 |
1.43e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 150 DKAMKDLNGPEKVKVLLAQALFGNPD--ILLLDEPTNHLDLDAI-AWLEEF--LINFDNTVIVVSHDRYFLnkvctQIAD 224
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDInQLLEVIkgLIDLGNTVILIEHNLDVL-----SSAD 156
|
....*..
gi 2124998340 225 --IDYGK 229
Cdd:cd03238 157 wiIDFGP 163
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-60 |
1.64e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 1.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFeDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII 60
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY 59
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-469 |
1.81e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.77 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSK--TIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQIL------TGEMEPDEGTY------KW----GVT 381
Cdd:cd03289 3 MTVKDLTAkyTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntEGDIQIDGVSWnsvplqKWrkafGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 382 TSQAYfpLDSGSEFDNEYTIVEW----LTQYSDEKDV-TYVRGFLGRMLFSGEDGVKkvkVLSGGEKVRCLLSKMMISGA 456
Cdd:cd03289 83 PQKVF--IFSGTFRKNLDPYGKWsdeeIWKVAEEVGLkSVIEQFPGQLDFVLVDGGC---VLSHGHKQLMCLARSVLSKA 157
|
170
....*....|...
gi 2124998340 457 NVLLLDEPTNHLD 469
Cdd:cd03289 158 KILLLDEPSAHLD 170
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
331-470 |
2.32e-05 |
|
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: 47.04 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 331 GEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTTSQ-----------AYFPLD----SGSEF 395
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrhtlrqfiNYLPQEpyifSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 396 DN----------EYTIVEWLTQYSDEKDVTYV-RGFLGRMLFSGEDgvkkvkvLSGGEKVRCLLSKMMISGANVLLLDEP 464
Cdd:TIGR01193 566 ENlllgakenvsQDEIWAACEIAEIKDDIENMpLGYQTELSEEGSS-------ISGGQKQRIALARALLTDSKVLILDES 638
|
....*.
gi 2124998340 465 TNHLDM 470
Cdd:TIGR01193 639 TSNLDT 644
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-75 |
2.57e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 20 VNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLQQDHFQ 75
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD-GKPVTAEQPEDYR 396
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-47 |
2.88e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.80 E-value: 2.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRIL 47
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-516 |
3.07e-05 |
|
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: 45.40 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIdGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG----------------VTTS 383
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppekrdisyVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 384 QAYFPldSGSEFDN-EYTI-VEWLTQYSDEKDVTYVRGFLG-RMLFSgedgvKKVKVLSGGEKVRCLLSKMMISGANVLL 460
Cdd:cd03299 80 YALFP--HMTVYKNiAYGLkKRKVDKKEIERKVLEIAEMLGiDHLLN-----RKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 461 LDEPTNHLDM---ESITALNNGLVKFPGV-LLFSSRDHQIVQTTANRIMeIVPGGKLIDK 516
Cdd:cd03299 153 LDEPFSALDVrtkEKLREELKKIRKEFGVtVLHVTHDFEEAWALADKVA-IMLNGKLIQV 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-469 |
3.51e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.95 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVT----TSQAYFPLDSGS 393
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPvpsrARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 394 EFDN---EYTIVEWLTQY------SDEKDVTYVRGFLG-RMLFSGEDGvkKVKVLSGGEKVRCLLSKMMISGANVLLLDE 463
Cdd:PRK13537 87 QFDNldpDFTVRENLLVFgryfglSAAAARALVPPLLEfAKLENKADA--KVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
....*.
gi 2124998340 464 PTNHLD 469
Cdd:PRK13537 165 PTTGLD 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
335-469 |
3.55e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 335 LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEgTYKWGVTTSQAYFPLDS-------------GSEFDNEyti 401
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVVIRGSVAYVPQVSwifnatvrenilfGSDFESE--- 708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 402 vewltQYSDEKDVTYVRGFLGrmLFSGED----GVKKVKVlSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:PLN03232 709 -----RYWRAIDVTALQHDLD--LLPGRDlteiGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-49 |
3.80e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 3.80e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSG 49
Cdd:NF040905 13 GVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-233 |
3.88e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDV---------IITPG--ERLSFLQQDHFQyddymvldTVM 86
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrngevsviAISAGlsGQLTGIENIEFK--------MLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 87 MGnarlyeiMKEKEViyakEDFTDEDgIKASELeGEFAAmngweaesdaatllnglgidaelhdKAMKDLNGPEKVKVLL 166
Cdd:PRK13546 113 MG-------FKRKEI----KAMTPKI-IEFSEL-GEFIY-------------------------QPVKKYSSGMRAKLGF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 167 AQALFGNPDILLLDEPTNHLD-------LDAIAWLEEflinFDNTVIVVSHDRYFLNKVCTQIADIDYGKIKLY 233
Cdd:PRK13546 155 SINITVNPDILVIDEALSVGDqtfaqkcLDKIYEFKE----QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-211 |
3.98e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.64 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLSFLQQDHFQY----- 76
Cdd:PRK15056 9 VNDVTVTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpqse 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 77 -DDY----MVLDTVMMGNarlYEIMkekeviyakedftdedgikaselegefaamnGW---EAESDAATLLNGLG-ID-A 146
Cdd:PRK15056 88 eVDWsfpvLVEDVVMMGR---YGHM-------------------------------GWlrrAKKRDRQIVTAALArVDmV 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 147 ELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEfLINFDNTVIVVSHD 211
Cdd:PRK15056 134 EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTeariISLLRE-LRDEGKTMLVSTHN 201
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-218 |
4.00e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 17 FEDVNIKFTEG-NCygLIGANGAGKSTFLRILsgqlepskgDVIITPGERLSFLQQDHFQYDDYMVLDTVMMG--NARLY 93
Cdd:COG3593 14 IKDLSIELSDDlTV--LVGENNSGKSSILEAL---------RLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELtfGSLLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 94 EIMKEKEVIYAKEDFTDEDGIKASELEGEFAAMNGwEAESDAATLLNGLGIDAELHDKAMKDLNGPEKVKV--------- 164
Cdd:COG3593 83 RLLRLLLKEEDKEELEEALEELNEELKEALKALNE-LLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIedgkelpld 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 165 ------------LLAQALF-----GNPDILLLDEPTNHLDLDAIAWLEEFLINF---DNTVIVVSHDRYFLNKV 218
Cdd:COG3593 162 rlgsgfqrlillALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELsekPNQVIITTHSPHLLSEV 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-215 |
4.20e-05 |
|
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: 43.90 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 27 GNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITPGERLsflqqdhfqyddymvldtvmmgnarLYEIMKEKEVIYAKE 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDI-------------------------LEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 107 DFTDEDGIKaselegefaamngweaesdaatllnglgidaelhdkamkdlngpeKVKVLLAQALFGNPDILLLDEPTNHL 186
Cdd:smart00382 57 KKASGSGEL---------------------------------------------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190
....*....|....*....|....*....|....*...
gi 2124998340 187 D---------LDAIAWLEEFLINFDNTVIVVSHDRYFL 215
Cdd:smart00382 92 DaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-470 |
4.53e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.00 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVTtsqayfPLDSGSefDNEY 399
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK------PISMLS--SRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 T-IVEWLTQY-------SDEKDVTYVRG----FLGRMlfSGED----------------GVKKVKVLSGGEKVRCLLSKM 451
Cdd:PRK11231 75 ArRLALLPQHhltpegiTVRELVAYGRSpwlsLWGRL--SAEDnarvnqameqtrinhlADRRLTDLSGGQRQRAFLAMV 152
|
170
....*....|....*....
gi 2124998340 452 MISGANVLLLDEPTNHLDM 470
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDI 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-222 |
4.57e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 10 RVGKKALFEDVNIKFTEGNCYGLIGANGAGKST----FLRILsgqlePSKGDVII--TPGERLSFLQ--------QDHFQ 75
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFdgQPLHNLNRRQllpvrhriQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 76 yDDYMVLdtvmmgNARLyeimkekeviyakedftDEDGIKASELEGEFAAMNGWEAESDAATLLNGLGIDAELHDKAMKD 155
Cdd:PRK15134 370 -DPNSSL------NPRL-----------------NVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDNT----VIVVSHDRYFLNKVCTQI 222
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQV 496
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
142-246 |
5.39e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.64 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 142 LGIDAELhDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLDL----DAIAWLEEFLINFDNTVIVVSHDryfLNK 217
Cdd:PRK11144 116 LGIEPLL-DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDE 191
|
90 100 110
....*....|....*....|....*....|...
gi 2124998340 218 VcTQIAD----IDYGKIKLYAGNYDFWyESSQL 246
Cdd:PRK11144 192 I-LRLADrvvvLEQGKVKAFGPLEEVW-ASSAM 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-71 |
5.82e-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: 44.10 E-value: 5.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2124998340 24 FTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDvIITPGERLSFLQQ 71
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-DEWDGITPVYKPQ 68
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-472 |
5.93e-05 |
|
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: 44.53 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY-----------------KWGVTTSQAYfpLDSG 392
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrdytlaslrrQIGLVSQDVF--LFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 393 SEFDNeytiVEWLTQYSDEKDV------TYVRGFLGRM-----LFSGEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:cd03251 91 TVAEN----IAYGRPGATREEVeeaaraANAHEFIMELpegydTVIGERGVK----LSGGQRQRIAIARALLKDPPILIL 162
|
170
....*....|.
gi 2124998340 462 DEPTNHLDMES 472
Cdd:cd03251 163 DEATSALDTES 173
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-473 |
7.07e-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: 44.14 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 349 AFVGGNELAKTTLFQ----ILTGEMEP--DEGTYKWGVTTSQ---AYFPLDSGSEFDNEYTIVEWLTQYsdeKDVTYVR- 418
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPnsKGGAHDPKLIREGevrAQVKLAFENANGKKYTITRSLAIL---ENVIFCHq 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 419 ----GFLGRMLfsgedgvkkvKVLSGGEKV------RCLLSKMMISGANVLLLDEPTNHLDMESI 473
Cdd:cd03240 103 gesnWPLLDMR----------GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
330-472 |
7.35e-05 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 45.48 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT----------YKWGVTTSQAYFPLDSGSEFDNey 399
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQilldghdladYTLASLRRQVALVSQDVVLFND-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 TIVEWLTqYSDEKDV-----------TYVRGFLGRMLFS-----GEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLLDE 463
Cdd:TIGR02203 421 TIANNIA-YGRTEQAdraeieralaaAYAQDFVDKLPLGldtpiGENGVL----LSGGQRQRLAIARALLKDAPILILDE 495
|
....*....
gi 2124998340 464 PTNHLDMES 472
Cdd:TIGR02203 496 ATSALDNES 504
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-510 |
7.80e-05 |
|
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: 43.94 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 335 LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQ------AYFPLDSGSEFdNEYTIVEWLTQ 407
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVSDlrgraiPYLRRKIGVVF-QDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 408 YSD---EKDVTYVrgflgrmlfSGEDGVKKVKV-----------------LSGGEKVRCLLSKMMISGANVLLLDEPTNH 467
Cdd:cd03292 96 YENvafALEVTGV---------PPREIRKRVPAalelvglshkhralpaeLSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2124998340 468 LDMESITALNNGLVKF--PGV-LLFSSRDHQIVQTTANRIMEIVPG 510
Cdd:cd03292 167 LDPDTTWEIMNLLKKInkAGTtVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-216 |
7.96e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.54 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 32 LIGANGAGKSTFLRILSGQLePSKGDVII--TPGERLS----------FLQQDH-------FQYddymvLDTVMMGNARL 92
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFagQPLEAWSaaelarhrayLSQQQTppfampvFQY-----LTLHQPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 93 YEIMKEKEVIyakedftdedgikaselegefaamngweAESdaatllngLGIDAELHdKAMKDLNGPEKVKVLLAQALF- 171
Cdd:PRK03695 101 EAVASALNEV----------------------------AEA--------LGLDDKLG-RSVNQLSGGEWQRVRLAAVVLq 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124998340 172 ----GNPD--ILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHDryfLN 216
Cdd:PRK03695 144 vwpdINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD---LN 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-229 |
8.30e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.21 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFLqQDH------- 73
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR-GQHIEGL-PGHqiarmgv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 74 ---FQyddymvldtvmmgNARLYeimKEKEVIyakEDF--TDEDGIKASELEGEFAAMNGWEAESD----AATLLNGLGI 144
Cdd:PRK11300 83 vrtFQ-------------HVRLF---REMTVI---ENLlvAQHQQLKTGLFSGLLKTPAFRRAESEaldrAATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 145 dAELHDKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHL------DLDA-IAWLEEfliNFDNTVIVVSHDRYFLNK 217
Cdd:PRK11300 144 -LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDElIAELRN---EHNVTVLLIEHDMKLVMG 219
|
250
....*....|..
gi 2124998340 218 VCTQIADIDYGK 229
Cdd:PRK11300 220 ISDRIYVVNQGT 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
324-519 |
8.84e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.29 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 324 GLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGVT---------------TSQAYFP 388
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafrrDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 389 lDSGSEFDNEYTIVE-------WLTQYSDEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:PRK10419 97 -DSISAVNPRKTVREiireplrHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 462 DEPTNHLDM----ESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMeIVPGGKLIDKITT 519
Cdd:PRK10419 176 DEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM-VMDNGQIVETQPV 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-476 |
1.02e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG------VTTSQAyfpLDSG- 392
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfASTTAA---LAAGv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 393 ----SEFD--NEYTIVE--WLTQYS------DEKDVTY-VRGFLGRMlfsGE--DGVKKVKVLSGGEKVRCLLSKMMISG 455
Cdd:PRK11288 82 aiiyQELHlvPEMTVAEnlYLGQLPhkggivNRRLLNYeAREQLEHL---GVdiDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180
....*....|....*....|.
gi 2124998340 456 ANVLLLDEPTNHLDMESITAL 476
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQL 179
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
335-483 |
1.13e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.47 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 335 LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWgvTTSQAYFPLDSGSEFDNEYTIV-----EWLTQYS 409
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW--SNKNESEPSFEATRSRNRYSVAyaaqkPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 410 DEKDVTYVRGF----------------------LGRMLFSGEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNH 467
Cdd:cd03290 95 VEENITFGSPFnkqrykavtdacslqpdidllpFGDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170
....*....|....*..
gi 2124998340 468 LDME-SITALNNGLVKF 483
Cdd:cd03290 171 LDIHlSDHLMQEGILKF 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-470 |
1.18e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.01 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 321 TVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwgVTTSQAyfPLDSGSE--FDNE 398
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGE----ILLDAQ--PLESWSSkaFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 399 ytiVEWLTQYSDEKDVTYVR-----------GFLGRmlFSGED-----------GVKK-----VKVLSGGEKVRCLLSKM 451
Cdd:PRK10575 87 ---VAYLPQQLPAAEGMTVRelvaigrypwhGALGR--FGAADrekveeaislvGLKPlahrlVDSLSGGERQRAWIAML 161
|
170
....*....|....*....
gi 2124998340 452 MISGANVLLLDEPTNHLDM 470
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDI 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
332-483 |
1.24e-04 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 43.41 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 332 EKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY-----------KWGVTTSQAYfpldsGSEFDN--- 397
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSgqilfngqprkPDQFQKCVAY-----VRQDDIllp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 398 EYTIVEWLTQY---------SDEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHL 468
Cdd:cd03234 95 GLTVRETLTYTailrlprksSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*
gi 2124998340 469 DmeSITALNngLVKF 483
Cdd:cd03234 175 D--SFTALN--LVST 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
319-469 |
1.31e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 43.25 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSkTIDGEKIL-DDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKW-GVTTSQAyfpldsGSEF- 395
Cdd:PRK13538 1 MLEARNLA-CERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRQ------RDEYh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 396 ------------DNEYTIVE---WLTQYSDEKDVTYVRGFLGRMLFSG-EDGVkkVKVLSGGEKVRCLLSKMMISGANVL 459
Cdd:PRK13538 74 qdllylghqpgiKTELTALEnlrFYQRLHGPGDDEALWEALAQVGLAGfEDVP--VRQLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|
gi 2124998340 460 LLDEPTNHLD 469
Cdd:PRK13538 152 ILDEPFTAID 161
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-469 |
1.83e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.78 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY-------------KWGVTT--- 382
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaeNRHVNTvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 383 SQAYFPldSGSEFDNeytiVEW---LTQYSDEKDVTYVRGFLgRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVL 459
Cdd:PRK09452 94 SYALFP--HMTVFEN----VAFglrMQKTPAAEITPRVMEAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170
....*....|
gi 2124998340 460 LLDEPTNHLD 469
Cdd:PRK09452 167 LLDESLSALD 176
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-58 |
2.42e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.24 E-value: 2.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDV 58
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI 58
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-187 |
2.91e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 32 LIGANGAGKSTFLRILSGqlepskgdviitpgerlsflqqDHFQ-YDDymvlDTVMMGNAR-----LYEImkEKEVIYAK 105
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG----------------------DHPQgYSN----DLTLFGRRRgsgetIWDI--KKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 106 EDFTDEDGIKASE----LEGEFAAMNGWEAESD-----AATLLNGLGIDAELHDKAMKDLNGPEKVKVLLAQALFGNPDI 176
Cdd:PRK10938 343 SSLHLDYRVSTSVrnviLSGFFDSIGIYQAVSDrqqklAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTL 422
|
170
....*....|.
gi 2124998340 177 LLLDEPTNHLD 187
Cdd:PRK10938 423 LILDEPLQGLD 433
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-190 |
3.32e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 17 FEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII--------TPGERLS----FLQQDHFQYDDYmvLDT 84
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLngkeinalSTAQRLArglvYLPEDRQSSGLY--LDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 85 VMMGNArlyeimkeKEVIYAKEDFTDEDGIKASELEGEFAAmngweaesdaatllngLGIDAELHDKAMKDLNGPEKVKV 164
Cdd:PRK15439 357 PLAWNV--------CALTHNRRGFWIKPARENAVLERYRRA----------------LNIKFNHAEQAARTLSGGNQQKV 412
|
170 180
....*....|....*....|....*.
gi 2124998340 165 LLAQALFGNPDILLLDEPTNHLDLDA 190
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-375 |
3.45e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.61 E-value: 3.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT 375
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE 62
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
156-230 |
3.62e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 43.28 E-value: 3.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 156 LNGPEKVKVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLInfDNTVIVVSHDRYFLNKVcTQIADIDYGKI 230
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
166-217 |
3.91e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 3.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 166 LAQALFGNPDILLLDEPTNHLDLDAIAW-----LEEFLINFDNTVIVVSHDRYFLNK 217
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-230 |
3.91e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 18 EDVNIKFTEGNCYGLIGANGAGKSTFLRILSgQLEPSKGDVIITPGERLSFLQQDHFQ----------YDDYMVLD---T 84
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVESQGGEIIFNGQRIDTLSPGKLQalrrdiqfifQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 85 VMmgnarlYEIMKEKEViyakedftdedgikaselegeFAAMNGWEAESDAATLLNGLGIDAELHDKAMKDLNGPEKVKV 164
Cdd:PRK10261 420 VG------DSIMEPLRV---------------------HGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 165 LLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLIN----FDNTVIVVSHDRYFLNKVCTQIADIDYGKI 230
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlqrdFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-198 |
4.27e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.46 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRV----GKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQlepsKGDVIITpGErlsflqqdhfqyd 77
Cdd:cd03232 4 LTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR----KTAGVIT-GE------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 78 dymvldtvMMGNARLYEIMKEKEVIYAKEDFTDEDGIKASE-LegEFAAmngweaesdaatLLNGLGIDaelhdkamkdl 156
Cdd:cd03232 66 --------ILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREaL--RFSA------------LLRGLSVE----------- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2124998340 157 ngpEKVKVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFL 198
Cdd:cd03232 113 ---QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-375 |
4.95e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.70 E-value: 4.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLN----HddkvAFVGGNELAKTTLFQILTGEMEPDEGT 375
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRpgevH----ALLGENGAGKSTLMKILSGVYQPDSGE 60
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-60 |
7.17e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 7.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2124998340 12 GKKALfEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVII 60
Cdd:PRK10982 10 GVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF 57
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-187 |
1.18e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.47 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVIITpGERLSFL--QQDH----FQ 75
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVpaENRHvntvFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 76 ydDY-----M-VLDTVMMGnarlyeiMKEKEVIYAKEDFTDEDGIKASELEgEFAamngweaesdaatllnglgidaelh 149
Cdd:PRK09452 94 --SYalfphMtVFENVAFG-------LRMQKTPAAEITPRVMEALRMVQLE-EFA------------------------- 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 2124998340 150 DKAMKDLNGPEKVKVLLAQALFGNPDILLLDEPTNHLD 187
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
330-472 |
1.34e-03 |
|
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: 40.68 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 330 DGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWG------VTTSQ-----AYFPLDSgSEFDN- 397
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdireVTLDSlrraiGVVPQDT-VLFNDt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 398 -EYTIvewltQY-----SDEKDVTYVR-----GFLGRMLFS-----GEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLL 461
Cdd:cd03253 91 iGYNI-----RYgrpdaTDEEVIEAAKaaqihDKIMRFPDGydtivGERGLK----LSGGEKQRVAIARAILKNPPILLL 161
|
170
....*....|.
gi 2124998340 462 DEPTNHLDMES 472
Cdd:cd03253 162 DEATSALDTHT 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-476 |
1.58e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.31 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 320 LTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYkwgVTTSQAYFPLDSGSEFDNEY 399
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI---TINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 400 TIVEWLTQYSDEKDVTYvRGFLGRMLFSGEDGV--------------------------KKVKVLSGGEKVRCLLSKMMI 453
Cdd:PRK09700 83 GIIYQELSVIDELTVLE-NLYIGRHLTKKVCGVniidwremrvraammllrvglkvdldEKVANLSISHKQMLEIAKTLM 161
|
170 180
....*....|....*....|...
gi 2124998340 454 SGANVLLLDEPTNHLDMESITAL 476
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYL 184
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
335-469 |
1.80e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 335 LDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTykwGVTT--SQAYFPLDS-------------GSEFDNEy 399
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA---SVVIrgTVAYVPQVSwifnatvrdnilfGSPFDPE- 708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124998340 400 tivewltQYSDEKDVTYVRGFL-----GRMLFSGEDGVKkvkvLSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:PLN03130 709 -------RYERAIDVTALQHDLdllpgGDLTEIGERGVN----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
163-211 |
2.02e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 39.34 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLDLDAIAWLEEFLINFDN---TVIVVSHD 211
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADagkAVLLISSE 163
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
318-375 |
2.56e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.97 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124998340 318 EVLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT 375
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT 61
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-510 |
3.00e-03 |
|
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: 40.27 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 319 VLTVEGLSKTIDG--EKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPD---EGTYKWGVTTSQAYFPLDSGS 393
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 394 E----FDNEYTIvewLTQYSDEKDVTYVrgfLGRMLFSGEDGVKKVK-----------------VLSGGEKVRCLLSKMM 452
Cdd:COG1123 84 RigmvFQDPMTQ---LNPVTVGDQIAEA---LENLGLSRAEARARVLelleavglerrldryphQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 453 ISGANVLLLDEPTNHLDMES---ITALNNGLVKFPGV-LLFSSRDHQIVQTTANRIMEIVPG 510
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGTtVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
319-375 |
3.10e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 3.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124998340 319 VLTVEGLSKTIDGEKILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGT 375
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT 67
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
333-533 |
3.38e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.40 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 333 KILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTY--------KWGVTTSQAYFPLDSGSEFDNEY-TIVE 403
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitKENIREVRKFVGLVFQNPDDQIFsPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 404 WLTQYS------DEKDVTYVRGFLGRMLFSGEDGVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLD---MESIT 474
Cdd:PRK13652 98 QDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgVKELI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 475 ALNNGLVKFPGV-LLFSSRDHQIVQTTANRIMeIVPGGKLIDKITTYDEYLESDEMARKR 533
Cdd:PRK13652 178 DFLNDLPETYGMtVIFSTHQLDLVPEMADYIY-VMDKGRIVAYGTVEEIFLQPDLLARVH 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-469 |
3.64e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 39.61 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 317 NEVLTVEGLSKTIDGEK--ILDDITFTLNHDDKVAFVGGNELAKTTLFQILTGEMEPDEGTYKWGvttsqaYFPLDS--- 391
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG------GMVLSEetv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 392 -------GSEF---DNEY--TIVewltqysdEKDVTYVRGFLG----RMLFSGEDGVKKVKV----------LSGGEKVR 445
Cdd:PRK13635 77 wdvrrqvGMVFqnpDNQFvgATV--------QDDVAFGLENIGvpreEMVERVDQALRQVGMedflnrephrLSGGQKQR 148
|
170 180
....*....|....*....|....
gi 2124998340 446 CLLSKMMISGANVLLLDEPTNHLD 469
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLD 172
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-188 |
4.00e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 39.42 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPS--------KGDVIIT-------PGER 65
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNgeplaaiDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 66 LSFLQ-------QDHFQYDdymVLDTVMMG---NARlyeimkekeviyAKEDFTDEDGIKASelegefAAMngweAESDA 135
Cdd:PRK13547 81 LARLRavlpqaaQPAFAFS---AREIVLLGrypHAR------------RAGALTHRDGEIAW------QAL----ALAGA 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124998340 136 ATLLNglgidaelhdKAMKDLNGPEKVKVLLAQAL---------FGNPDILLLDEPTNHLDL 188
Cdd:PRK13547 136 TALVG----------RDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-47 |
4.28e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 4.28e-03
10 20 30
....*....|....*....|....*....|.
gi 2124998340 17 FEDVNIKFTEGNCygLIGANGAGKSTFLRIL 47
Cdd:COG4637 13 LRDLELPLGPLTV--LIGANGSGKSNLLDAL 41
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
438-513 |
4.36e-03 |
|
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: 39.32 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 438 LSGGEKVRCLLSKMMISGANVLLLDEPTNHLDM----ESITALNNGLVKFPGVLLFSSRDHQIVQTTANRIMeIVPGGKL 513
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVV-VLEDGRV 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-76 |
4.49e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 1 MISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSGQlePS----KGDVI--------ITPGERLS- 67
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILfkgesildLEPEERAHl 84
|
90
....*....|.
gi 2124998340 68 --FLQqdhFQY 76
Cdd:CHL00131 85 giFLA---FQY 92
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-49 |
5.68e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 5.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2124998340 2 ISTSNITLRVGKKALFEDVNIKFTEGNCYGLIGANGAGKSTFLRILSG 49
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
411-469 |
6.71e-03 |
|
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: 38.24 E-value: 6.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124998340 411 EKDVTYVRGFLGRMLFSGEDgVKKVKVLSGGEKVRCLLSKMMISGANVLLLDEPTNHLD 469
Cdd:cd03298 103 AEDRQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
163-190 |
6.98e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 6.98e-03
10 20
....*....|....*....|....*...
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLDLDA 190
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
9.98e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 38.19 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 19 DVNIKFTEGNCYGLIGANGAGKSTFLRILSGQLEPSKGDVI-----ITPgERLSFLQQD---HFQY-DDYMVLDTV---- 85
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITD-DNFEKLRKHigiVFQNpDNQFVGSIVkydv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124998340 86 ---MMGNARLYEIMKEKeviyAKEDFTDEDGIKASelegefaamngweaesdaatllnglgiDAELHDkamkdLNGPEKV 162
Cdd:PRK13648 106 afgLENHAVPYDEMHRR----VSEALKQVDMLERA---------------------------DYEPNA-----LSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124998340 163 KVLLAQALFGNPDILLLDEPTNHLDLDA----IAWLEEFLINFDNTVIVVSHD 211
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHD 202
|
|
| |
