|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-527 |
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: 743.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDYTVLE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 84 TVIMGHKRLYEVMKEKDAIYMKEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIPEELHDQKMSELTAGQKVK 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 164 VLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYDFWLES 243
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 244 SQLATKLQAQSNAKKEEQIKELQDFIARFSANASKSKQATSRKKMLDKITLDDIQPSSrRYPFVGFTPEREIGNDLLQVE 323
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRD-KTVEIRFPPPERLGKKVLELE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 324 NVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSkDFEEPLTILD 403
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE-ELDPDKTVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 404 WLRQFAgkEEDDNTFLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLM 483
Cdd:COG0488 399 ELRDGA--PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 488284819 484 AFTGSILFASHDHQFIQTLANRIIAVSDKGVIDRaETTYDEFLE 527
Cdd:COG0488 477 DFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY-PGGYDDYLE 519
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-532 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 705.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDYT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRLYEVMKEKDAIYMKEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIPEELHDQKMSELTAGQ 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 161 KVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYDFW 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 241 LESSQLATKLQAQSNAKKEEQIKELQDFIARFSANASKSKQATSRKKMLDKITLDDIQPSSRRYPFVGFTPEREIGNDLL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 321 QVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKDFEEPLT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 401 ILDWLRQFAgKEEDDNTFLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALND 480
Cdd:PRK15064 401 LFDWMSQWR-QEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNM 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 488284819 481 GLMAFTGSILFASHDHQFIQTLANRIIAVSDKGVIDRAeTTYDEFLENPEIQ 532
Cdd:PRK15064 480 ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFS-GTYEEYLRSQGIE 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-528 |
1.32e-96 |
|
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: 304.17 E-value: 1.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 3 TVNDVSLQFP-DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQN-HFDyEDYT 80
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpQLD-PTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRLYEVMKEKDAIYMKedFSDED------GIRAAELEGEFAELDGWEAEPEAAVLLQGLNIPEElhDQKMS 154
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEISAK--YAEPDadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 155 ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYV 234
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 235 GNYDFWLESSQLATKLQAQSNAKKEEQIKELQDFIaRFSANA--SKSKQATSR-KKMLDKITLDDIQPSSRRYPfvgftP 311
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWV-RQSPKGrqAKSKARLARyEELLSQEFQKRNETAEIYIP-----P 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 312 EREIGNDLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLpkDN 391
Cdd:TIGR03719 315 GPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYV--DQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 392 SKD--------FEEPLTILDWLRqfAGKEEDDNtflRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVL 463
Cdd:TIGR03719 393 SRDaldpnktvWEEISGGLDIIK--LGKREIPS---RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 464 DDPTNHLDLESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSDKGVIDRAETTYDEFLEN 528
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEED 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-508 |
5.25e-85 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 273.92 E-value: 5.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 12 PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQN-HFDyEDYTVLETVIMGHK 90
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpQLD-PEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 91 RLYEVMKEKDAIYMK----EDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIPEElhDQKMSELTAGQKVKVLL 166
Cdd:PRK11819 97 EVKAALDRFNEIYAAyaepDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPW--DAKVTKLSGGERRRVAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 167 AQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYDFWLESSQL 246
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 247 ATKLQAQSNAKKEEQIKELQDFIaRFSANA--SKSK-----------QATSRKKMLDKITlddIQPSSRrypfvgftper 313
Cdd:PRK11819 255 RLAQEEKQEAARQKALKRELEWV-RQSPKArqAKSKarlaryeellsEEYQKRNETNEIF---IPPGPR----------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 314 eIGNDLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLpkDNSK 393
Cdd:PRK11819 320 -LGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV--DQSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 394 D--------FEEPLTILDWLRqfAGKEEDDNtflRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDD 465
Cdd:PRK11819 397 DaldpnktvWEEISGGLDIIK--VGNREIPS---RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488284819 466 PTNHLDLESITALNDGLMAFTGSILFASHDHQFIQTLANRIIA 508
Cdd:PRK11819 472 PTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILA 514
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-514 |
4.60e-79 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 260.49 E-value: 4.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHfDYEDYT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQET-PALPQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRLYEVMKEKDAIYMKEDfsdedGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIPEELHDQKMSELTAGQ 160
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQLHDANERND-----GHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 161 KVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYDFW 240
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 241 leSSQLATKLqAQSNA---KKEEQIKELQDFIARFSANASKSKQATSRKKMLDKITLddIQPSSRRYPF-VGFTPEREIG 316
Cdd:PRK10636 235 --EVQRATRL-AQQQAmyeSQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 317 NDLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKDFE 396
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 397 EPLTILDWLRQFAGKEEDDNtfLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESIT 476
Cdd:PRK10636 390 ADESPLQHLARLAPQELEQK--LRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490 500 510
....*....|....*....|....*....|....*...
gi 488284819 477 ALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSDKGV 514
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-499 |
5.08e-78 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 257.57 E-value: 5.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDYT 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRLYEVMKEKDAI--YMKEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIPEelhDQKMSELTA 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDIshLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP---DAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 239 FWLESSQLATKLQAQSNA---KK--EEQIKELQDFIARFSAN--------ASKSKQATSRKKMLD-KITLDDiqpSSRRy 304
Cdd:PRK11147 240 QYLLEKEEALRVEELQNAefdRKlaQEEVWIRQGIKARRTRNegrvralkALRRERSERREVMGTaKMQVEE---ASRS- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 305 pfvgftpereiGNDLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQ 384
Cdd:PRK11147 316 -----------GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 385 AYLpkDNSKDFEEP-LTILDWLRQfaGKEE-DDNTFLRSFLGRM---LFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKAN 459
Cdd:PRK11147 385 AYF--DQHRAELDPeKTVMDNLAE--GKQEvMVNGRPRHVLGYLqdfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSN 460
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488284819 460 VLVLDDPTNHLDLESITALNDGLMAFTGSILFASHDHQFI 499
Cdd:PRK11147 461 LLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-511 |
2.74e-69 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 236.29 E-value: 2.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSgeIQPTTGVVSmgpNERLATLKQNHFDyEDYTV 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGIPK---NCQILHVEQEVVG-DDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 LETV----------------IMGHKRLYEVMKEKDAIYMKE-DFSDEDGI--RAAELEGEFAELDGWEAEPEAAVLLQGL 142
Cdd:PLN03073 252 LQCVlntdiertqlleeeaqLVAQQRELEFETETGKGKGANkDGVDKDAVsqRLEEIYKRLELIDAYTAEARAASILAGL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 143 NIPEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHM 222
Cdd:PLN03073 332 SFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 223 ADLDFSKIKLYVGNYDFWLESSQLATKLQAQSNAKKEEQIKELQDFIARFSANASKSKQATSRKKMLDKITLDDIQPSSR 302
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDP 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 303 RYPFVGFTPEREIGNDLLQVENVSVTIDGKKIL-DNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVT 381
Cdd:PLN03073 492 DYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 382 TSQAYLPKDNSKDFEEPLT-ILDWLRQFAGKEEDDntfLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANV 460
Cdd:PLN03073 572 VRMAVFSQHHVDGLDLSSNpLLYMMRCFPGVPEQK---LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 488284819 461 LVLDDPTNHLDLESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSD 511
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-242 |
7.43e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 192.97 E-value: 7.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNH--FDyED 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQeeLD-PD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVLETVimghKRLYEVMKEKDaiymkedfsdedgIRAaelegefaeldgweaepeaavLLQGLNIPEELHDQKMSELTA 158
Cdd:COG0488 394 KTVLDEL----RDGAPGGTEQE-------------VRG---------------------YLGRFLFSGDDAFKPVGVLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYD 238
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
....
gi 488284819 239 FWLE 242
Cdd:COG0488 516 DYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-513 |
4.66e-48 |
|
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: 163.39 E-value: 4.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKdnskdfeepl 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 400 tildwlrqfagkeeddntflrsflgrmlfsgeevlkpvnvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALN 479
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 488284819 480 DGLMAFTGSILFASHDHQFIQTLANRIIAVSDKG 513
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-221 |
2.78e-45 |
|
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: 156.07 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQnhfdyedytv 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 letvimghkrlyevmkekdaiymkedfsdedgiraaelegefaeldgweaepeaavllqglnipeelhdqkmseLTAGQK 161
Cdd:cd03221 71 --------------------------------------------------------------------------LSGGEK 76
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 162 VKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTH 221
Cdd:cd03221 77 MRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATK 136
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-223 |
1.46e-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: 136.33 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV--------SMGPNE---RLATL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNHFDYEDYTVLETVIMG---HKRLYEVMKEKdaiymkedfsDEDGIRAAelegefaeldgweaepeaavlLQGLNIpE 146
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrypHLGLFGRPSAE----------DREAVEEA---------------------LERTGL-E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDtrsINWLEEFL-----INFEN--TVIVVSHDrhfLN--- 216
Cdd:COG1120 129 HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD---LAHQLEVLellrrLARERgrTVVMVLHD---LNlaa 202
|
....*..
gi 488284819 217 KVCTHMA 223
Cdd:COG1120 203 RYADRLV 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-242 |
2.04e-36 |
|
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: 135.37 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhFDYEDYt 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIL--------------IDGEDV- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 vletvimgHKRLYEVMKE----KDAIYMKEDFSDEDGIRaaeLEGEFAELDGWEAEPEAAVLLQGLNIPEELhDQKMSEL 156
Cdd:COG4555 66 --------RKEPREARRQigvlPDERGLYDRLTVRENIR---YFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFLNKVCTHMADLDFSKIkLY 233
Cdd:COG4555 134 STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV-VA 212
|
....*....
gi 488284819 234 VGNYDFWLE 242
Cdd:COG4555 213 QGSLDELRE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.51e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG------PNERLATLKQNH- 73
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQRAe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 FDyEDY--TVLETVIMG---HKRLYEVMKEKDaiymKEdfsdedgiRAAE-LEgefaeldgweaepeaAVllqGLnipEE 147
Cdd:COG1121 86 VD-WDFpiTVRDVVLMGrygRRGLFRRPSRAD----RE--------AVDEaLE---------------RV---GL---ED 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 148 LHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFEN-TVIVVSHDRHFLNKVCTHMA 223
Cdd:COG1121 132 LADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLreLRREGkTILVVTHDLGAVREYFDRVL 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
1.15e-32 |
|
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: 124.13 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHFDyedyt 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPIRDAREDYRR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 vlETVIMGHkrlyevmkeKDAIymKEDFSdedgirAAELEGEFAELDGWEAEPEAAV-LLQGLNIpEELHDQKMSELTAG 159
Cdd:COG4133 76 --RLAYLGH---------ADGL--KPELT------VRENLRFWAALYGLRADREAIDeALEAVGL-AGLADLPVRQLSAG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFL 215
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLEL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-226 |
3.58e-32 |
|
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: 123.03 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGP------NERLATLKQNH-FDY 76
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQRRsIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 eDY--TVLETVIMG---HKRLYEvmkekdaIYMKEDFSDedgIRAAeLEgefaeldgweaepeaAVllqGLnipEELHDQ 151
Cdd:cd03235 82 -DFpiSVRDVVLMGlygHKGLFR-------RLSKADKAK---VDEA-LE---------------RV---GL---SELADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 152 KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSInwlEEFLINFEN------TVIVVSHDRHFLNKVCTHMADL 225
Cdd:cd03235 129 QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ---EDIYELLRElrregmTILVVTHDLGLVLEYFDRVLLL 205
|
.
gi 488284819 226 D 226
Cdd:cd03235 206 N 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
1.17e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.09 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG----------PNERLATLKQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NHFDYEDYTVLETVIMgHKRLYevmkekdaiymkedfsdedGIRAAELEGEFAEldgweaepeaavLLQGLNIPEELhDQ 151
Cdd:COG1131 81 EPALYPDLTVRENLRF-FARLY-------------------GLPRKEARERIDE------------LLELFGLTDAA-DR 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 152 KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF---ENTVIVVSHDRHFLNKVCTHMA 223
Cdd:COG1131 128 KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-237 |
4.11e-30 |
|
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: 123.89 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYED-YT 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPnKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRL----YEVMKEkdAIYMKEDFSDEDgiraaelegefaeldgweaepeaavllqglnipeelHDQKMSEL 156
Cdd:TIGR03719 403 VWEEISGGLDIIklgkREIPSR--AYVGRFNFKGSD------------------------------------QQKKVGQL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMadLDF---SKIKLY 233
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFegdSHVEWF 522
|
....
gi 488284819 234 VGNY 237
Cdd:TIGR03719 523 EGNF 526
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-223 |
5.89e-29 |
|
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: 112.49 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV-----SMGPN-----ERLATLKQ 71
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkDIKKEpeevkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NHFDYEDYTVLETVimghkrlyevmkekdaiymkedfsdedgiraaelegefaeldgweaepeaavllqglnipeelhdq 151
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------------------------------------ 94
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 152 kmsELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFEN-TVIVVSHDRHFLNKVCTHMA 223
Cdd:cd03230 95 ---KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLreLKKEGkTILLSSHILEEAERLCDRVA 166
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-221 |
2.00e-26 |
|
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: 106.78 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPD--RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHF------- 74
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 75 --DYEDYTVLETVimghkrlyevmkEKDAIYmkedfsdedGIRAAELEGEfaeldgwEAEPEAAVLLQGLNIpEELHDQK 152
Cdd:cd03225 81 fqNPDDQFFGPTV------------EEEVAF---------GLENLGLPEE-------EIEERVEEALELVGL-EGLRDRS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFLNKVCTH 221
Cdd:cd03225 132 PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADR 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-237 |
2.64e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 112.52 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDytv 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP--- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 letvimgHKRLYEVmkekdaiymkedFSDEDgiraaelegEFAELDGWEAEPEAAVLLQGLNIPeelhDQ--KMSELTAG 159
Cdd:PRK11819 402 -------NKTVWEE------------ISGGL---------DIIKVGNREIPSRAYVGRFNFKGG----DQqkKVGVLSGG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMadLDF---SKIKLYVGN 236
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFegdSQVEWFEGN 527
|
.
gi 488284819 237 Y 237
Cdd:PRK11819 528 F 528
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-227 |
2.60e-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: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 3 TVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQnhfdyedytv 81
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 letvimghKRLYEVMKEKDAIYMKEDFSDEDGIRAAELEgefaeldgwEAEPEAAVLLQGLNIpEELHDQKMSELTAGQK 161
Cdd:cd03226 71 --------KSIGYVMQDVDYQLFTDSVREELLLGLKELD---------AGNEQAETVLKDLDL-YALKERHPLSLSGGQK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 162 VKVLLAQSLFGKPDVLLLDEPTNGLDTRSI----NWLEEfLINFENTVIVVSHDRHFLNKVCT---HMADLDF 227
Cdd:cd03226 133 QRLAIAAALLSGKDLLIFDEPTSGLDYKNMervgELIRE-LAAQGKAVIVITHDYEFLAKVCDrvlLLANGAI 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-220 |
3.71e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 102.97 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlaTLKQNhfDYEDYTV 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI---------YLDGK--PLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 LE----------TVIMGHKRLYEVMKEkDAIYMKEDFSDEDGIRaaelegefaeldgweaepeaavLLQGLNIPEELHDQ 151
Cdd:COG4619 70 PEwrrqvayvpqEPALWGGTVRDNLPF-PFQLRERKFDRERALE----------------------LLERLGLPPDILDK 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 152 KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHDRHFLNKVCT 220
Cdd:COG4619 127 PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVAD 199
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
4.11e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 11 FPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQnHFDYED---YTVLETVIM 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDslpLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 88 GhkrlyevmkekdaiymkedfsdedgiraaelegEFAELDGW---EAEPEAAV--LLQGLNIpEELHDQKMSELTAGQKV 162
Cdd:NF040873 81 G---------------------------------RWARRGLWrrlTRDDRAAVddALERVGL-ADLAGRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 163 KVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEfLINFEN----TVIVVSHDRH 213
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIA-LLAEEHargaTVVVVTHDLE 180
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
5.30e-25 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 98.41 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 223 ADLDFSKIKLYVGNYDFWLESSQLATKLQAQSNAKKEEQIKELQDFIARFSANASKSKQATSRKKMLDKitLDDIQPSSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEK--MERIEKPER 78
|
....*..
gi 488284819 303 RYPFVGF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-229 |
5.41e-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: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 3 TVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnhfdyedytvl 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 83 etVIMGHkrlyevmkekdaiymkedfsdedgiraaelegEFAELDGWEAEPEAAVLLQglnipeelhdqkmseLTAGQKV 162
Cdd:cd00267 57 --LIDGK--------------------------------DIAKLPLEELRRRIGYVPQ---------------LSGGQRQ 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 163 KVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF---ENTVIVVSHDRHFLNKVCTHMADLDFSK 229
Cdd:cd00267 88 RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-230 |
1.62e-24 |
|
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: 101.14 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlaTLKQNHFD--YEDY 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------TFDGKSYQknIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVIMGHKrLYEVMKEKDAIYMKedfSDEDGIRAAELEgefaeldgweaEPEAAVLLQGLNipeelhDQKMSELTAG 159
Cdd:cd03268 72 RRIGALIEAPG-FYPNLTARENLRLL---ARLLGIRKKRID-----------EVLDVVGLKDSA------KKKVKGFSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFLNKVCTHMADLDFSKI 230
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-226 |
1.39e-23 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 99.33 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVS-MGPNERLATLK--------- 70
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRelrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 -QNhfdYEDY----TVLETVIMGHKRLyevmkekdaiymkedfsdedGIRAAELEgEFAEldgweaepEAAVLLqGLnip 145
Cdd:COG1122 81 fQN---PDDQlfapTVEEDVAFGPENL--------------------GLPREEIR-ERVE--------EALELV-GL--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 EELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFEN-TVIVVSHDRHFLNKVCTHM 222
Cdd:COG1122 125 EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLkrLNKEGkTVIIVTHDLDLVAELADRV 204
|
....
gi 488284819 223 ADLD 226
Cdd:COG1122 205 IVLD 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-211 |
1.66e-23 |
|
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: 97.51 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 3 TVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKqnhfdyedytvl 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 83 etvimgHKrlyevmkekdaiymkedfsdedgiraaelegEFAELdgweaepeAAVLLQGL---NIpEELHDQKMSELTAG 159
Cdd:cd03214 68 ------PK-------------------------------ELARK--------IAYVPQALellGL-AHLADRPFNELSGG 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:cd03214 102 ERQRVLLARALAQEPPILLLDEPTSHLDIAHqielLELLRRLARERGKTVVMVLHD 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
1.67e-23 |
|
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: 99.39 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--VVSMG---PNERLATLKQN--- 72
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndVRLFGerrGGEDVWELRKRigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 -----HFDY-EDYTVLETVIMGhkrLYevmkekDAIYMKEDFSDEDGIRAAElegefaeldgweaepeaavLLQGLNIpE 146
Cdd:COG1119 83 vspalQLRFpRDETVLDVVLSG---FF------DSIGLYREPTDEQRERARE-------------------LLELLGL-A 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSH 210
Cdd:COG1119 134 HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-505 |
2.54e-23 |
|
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: 103.34 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG--EIQPTTGVV--SMGPNERLATLKQNHFDYE 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 78 DYTVLETVI---------MGHKRLYEVMKeKDAIYMKEDFS--DEDGIRAAELEG-EFAELDGWEAEPEAAVLLQGLNIP 145
Cdd:TIGR03269 81 PCPVCGGTLepeevdfwnLSDKLRRRIRK-RIAIMLQRTFAlyGDDTVLDNVLEAlEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 EEL-HDQKmsELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINW----LEEFLINFENTVIVVSHdrhflnkvct 220
Cdd:TIGR03269 160 HRItHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSH---------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 221 hmadldFSKIKLYVGNYDFWLESSQLAtklqaqsnakkeeQIKELQDFIARFSANASKSKQATsrkkmldkitlddiqps 300
Cdd:TIGR03269 228 ------WPEVIEDLSDKAIWLENGEIK-------------EEGTPDEVVAVFMEGVSEVEKEC----------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 301 srrypfvgftpEREIGNDLLQVENVS---VTIDGK--KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGS 375
Cdd:TIGR03269 272 -----------EVEVGEPIIKVRNVSkryISVDRGvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 376 V------RWGVTTSQAYLPKDNSKDF------EEPL----TILDWLRQFAGKEEDDNTFLRSFLGRMLFSGEEVLKPVNV 439
Cdd:TIGR03269 341 VnvrvgdEWVDMTKPGPDGRGRAKRYigilhqEYDLyphrTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEI 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 440 L-------SGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLM----AFTGSILFASHDHQFIQTLANR 505
Cdd:TIGR03269 421 LdkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVLDVCDR 497
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
2.89e-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: 97.65 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGnCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhFDYEDytv 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIR--------------IDGQD--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 letvimghkrlyeVMKEKDAI-----YMKEDFSDEDGIRAAELEGEFAELDGW---EAEPEAAVLLQGLNIPEELHDqKM 153
Cdd:cd03264 63 -------------VLKQPQKLrrrigYLPQEFGVYPNFTVREFLDYIAWLKGIpskEVKARVDEVLELVNLGDRAKK-KI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 154 SELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF-ENTVIVVS-HDRHFLNKVCTHMADLDFSKIK 231
Cdd:cd03264 129 GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-219 |
3.60e-23 |
|
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: 98.17 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 8 SLQFPDRKLFEEV----NIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG---PNERLATLKQNHfdyed 78
Cdd:cd03267 22 SLKSLFKRKYREVealkGISFTieKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvPWKRRKKFLRRI----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 ytvleTVIMGHK-RLYEVMKEKDAIYMKEDFSDEDGIRAAELEGEFAELdgweaepeaavllqgLNIPEELhDQKMSELT 157
Cdd:cd03267 97 -----GVVFGQKtQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSEL---------------LDLEELL-DTPVRQLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF----ENTVIVVSHDRHFLNKVC 219
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALA 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-515 |
4.65e-23 |
|
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: 95.93 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRwgvttsqaYLPKDNSKDFEEPL 399
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------VLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 400 TILDWLRQFAgkeeddntflrSFLGRMlfSGEEVLKpvnvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALN 479
Cdd:cd03230 73 RRIGYLPEEP-----------SLYENL--TVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 488284819 480 D---GLMAFTGSILFASHDHQFIQTLANRiIAVSDKGVI 515
Cdd:cd03230 136 EllrELKKEGKTILLSSHILEEAERLCDR-VAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
4-184 |
6.18e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 95.02 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPdrklfeevnikftPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-----------PNERLATLKQN 72
Cdd:pfam00005 1 LKNVSLTLN-------------PGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGhkrlyevmkekdaIYMKEDFSDEDGIRAAElegefaeldgweaepeaavLLQGLNIPEELH--- 149
Cdd:pfam00005 68 PQLFPRLTVRENLRLG-------------LLLKGLSKREKDARAEE-------------------ALEKLGLGDLADrpv 115
|
170 180 190
....*....|....*....|....*....|....*
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTN 184
Cdd:pfam00005 116 GERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-230 |
2.44e-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: 95.97 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV--------SMGPNERlATLK----- 70
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPPHEI-ARLGigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 QNHFDYEDYTVLETVIMGHKRlyevmKEKDAIYMKEDFSDEDGIRAaelegefaeldgweaepEAAVLLQ--GLnipEEL 148
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQA-----RTGSGLLLARARREEREARE-----------------RAEELLErvGL---ADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 149 HDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFEN-TVIVVSHDRHFLNKVCTHMADL 225
Cdd:cd03219 137 ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIreLRERGiTVLLVEHDMDVVMSLADRVTVL 216
|
....*
gi 488284819 226 DFSKI 230
Cdd:cd03219 217 DQGRV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-529 |
3.05e-22 |
|
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: 99.98 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFT--PGNCYGLIGANGAGKSTFLKILSGEIqPTTGVVSmGpnerlatlkQNHFDYED 78
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTiaPGETVALVGESGSGKSTLALALMGLL-PHGGRIS-G---------EVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVLETVIMGHKRlyevmkekdAIYMKEDFSDEDGIRAAELEGEFAELDGW---EAEPEAAVLLQGLNIpEELHDQKMSE 155
Cdd:COG1123 73 LLELSEALRGRRI---------GMVFQDPMTQLNPVTVGDQIAEALENLGLsraEARARVLELLEAVGL-ERRLDRYPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHDRhflnKVCTHMADldfSKIK 231
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDL----GVVAEIAD---RVVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 232 LYVGnydfwlessqlatklqaqsnakkeeQIKELQDfiarfsanaskSKQATSRKKMLDKITLDDIQPSSRRypfvgftP 311
Cdd:COG1123 216 MDDG-------------------------RIVEDGP-----------PEEILAAPQALAAVPRLGAARGRAA-------P 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 312 EREIGNDLLQVENVSVT-----IDGKKILDNISFNLTKDDKVAFIADSdittTTLFKVIMGEITPDTGSVRW-GVTTSQa 385
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESgsgkSTLARLLLGLLRPTSGSILFdGKDLTK- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 386 yLPKDNSKDF-------------------------EEPLTILDWLRqfaGKEEDD--NTFL------RSFLGRMLFSgee 432
Cdd:COG1123 332 -LSRRSLRELrrrvqmvfqdpysslnprmtvgdiiAEPLRLHGLLS---RAERRErvAELLervglpPDLADRYPHE--- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 433 vlkpvnvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD-------LESITALND--GLmaftgSILFASHDHQFIQTLA 503
Cdd:COG1123 405 -------LSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQRelGL-----TYLFISHDLAVVRYIA 472
|
570 580
....*....|....*....|....*.
gi 488284819 504 NRIIAVSDKGVIDRAETtyDEFLENP 529
Cdd:COG1123 473 DRVAVMYDGRIVEDGPT--EEVFANP 496
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
6.42e-22 |
|
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: 94.36 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPD-RKLFEEVN-IKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTGV-------VSMGPNERLATL 69
Cdd:cd03266 1 MITADALTKRFRDvKKTVQAVDgVSFTvkPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KqnhfdyedytvletVIMGHKRLYEVMKEKDaiyMKEDFSDEDGIRAAELEGEFAELdgweaepeaAVLLQglniPEELH 149
Cdd:cd03266 81 G--------------FVSDSTGLYDRLTARE---NLEYFAGLYGLKGDELTARLEEL---------ADRLG----MEELL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFLNKVC 219
Cdd:cd03266 131 DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLC 203
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-218 |
6.87e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 99.52 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRK--LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV--------SMGPNE---RLAT 68
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 69 LKQNHFDYEDyTVLETVIMGHkrlyevmkekdaiymkEDFSDEDGIRAAELEGefaeldgweAEPEAAVLLQGLnipeel 148
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGD----------------PDATDEEIIEAARLAG---------LHDFIEALPMGY------ 601
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 149 hDQKMSE----LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFenTVIVVSHDRHFLNKV 218
Cdd:COG2274 602 -DTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLKGR--TVIIIAHRLSTIRLA 676
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-223 |
2.24e-21 |
|
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: 92.57 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 20 VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNH--------FD--YEDYTVLEtvimgH 89
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslgycpqFDalFDELTVRE-----H 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 90 KRLYevmkekdaiymkedfsdedgiraAELEGefaeLDGWEAEPEAAVLLQGLNIpEELHDQKMSELTAGQKVKVLLAQS 169
Cdd:cd03263 96 LRFY-----------------------ARLKG----LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 170 LFGKPDVLLLDEPTNGLD--TRSINWLeefLINFE---NTVIVVSHDRHFLNKVCTHMA 223
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDpaSRRAIWD---LILEVrkgRSIILTTHSMDEAEALCDRIA 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-216 |
3.25e-21 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 97.62 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRK-LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDY 79
Cdd:PLN03073 508 IISFSDASFGYPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVletvimghkrlyevmkeKDAIYMKEDFSD--EDGIRAAelegefaeldgweaepeaavlLQGLNIPEELHDQKMSELT 157
Cdd:PLN03073 588 SS-----------------NPLLYMMRCFPGvpEQKLRAH---------------------LGSFGVTGNLALQPMYTLS 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFLN 216
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
9.83e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 90.63 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEE----VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-------PNERLATLK 70
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkgVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 QNHFDY--------EDYTVLETVIMGhkrlyevmkekdaiymkedfsdedgiraaeleGEFAELDGWEAEPEAAVLLQGL 142
Cdd:cd03255 81 RRHIGFvfqsfnllPDLTALENVELP--------------------------------LLLAGVPKKERRERAEELLERV 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 143 NIpEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHDR 212
Cdd:cd03255 129 GL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
1.06e-20 |
|
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: 91.09 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG-----EIQPTTGVVSMGPnerlatlkQNHFDY 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDG--------KDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 eDYTVLE---TVIMghkrlyeVMKEKDAIYMkedfSDEDGIRAA-ELEGEfaeLDGWEAEPEAAVLLQGLNIPEELHDQ- 151
Cdd:cd03260 73 -DVDVLElrrRVGM-------VFQKPNPFPG----SIYDNVAYGlRLHGI---KLKEELDERVEEALRKAALWDEVKDRl 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 152 KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSHD 211
Cdd:cd03260 138 HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-233 |
1.12e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFP----------------DRKLFEE------VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV 58
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrRRTRREEfwalkdVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 59 SMgpNERLATLkqnhFDY-----EDYTVLETV-----IMGHKRlyEVMKEK-DAIymkEDFsdedgiraAELeGEFAeld 127
Cdd:COG1134 84 EV--NGRVSAL----LELgagfhPELTGRENIylngrLLGLSR--KEIDEKfDEI---VEF--------AEL-GDFI--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 128 gweaepeaavllqglnipeelhDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEptnGLDT-------RSINWLEEFLin 200
Cdd:COG1134 141 ----------------------DQPVKTYSSGMRARLAFAVATAVDPDILLVDE---VLAVgdaafqkKCLARIRELR-- 193
|
250 260 270
....*....|....*....|....*....|....*
gi 488284819 201 fEN--TVIVVSHDRHFLNKVCTHMADLDFSKIKLY 233
Cdd:COG1134 194 -ESgrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-233 |
1.70e-20 |
|
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: 90.03 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHFDYedytv 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-GKPLDIAARNRIGY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 letviMGHKR-LYEVMKEKD-AIYmkedfsdedgiraaelegeFAELDGW---EAEPEAAVLLQGLNIpEELHDQKMSEL 156
Cdd:cd03269 75 -----LPEERgLYPKMKVIDqLVY-------------------LAQLKGLkkeEARRRIDEWLERLEL-SEYANKRVEEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF---ENTVIVVSHDRHFLNKVCTHMADLDFSKIKLY 233
Cdd:cd03269 130 SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-227 |
1.89e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPdrklfeevnikftPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNH---------- 73
Cdd:COG0411 20 VDDVSLEVE-------------RGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRiarlgiartf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 -----FdyEDYTVLETVIMGHKRLYEVMKEKDAIYMKEDFSDEDGIRAaelegefaeldgweaepEAAVLLQGLNIpEEL 148
Cdd:COG0411 86 qnprlF--PELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARE-----------------RAEELLERVGL-ADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 149 HDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLI----NFENTVIVVSHDRHFLNKVCTHMAD 224
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRrlrdERGITILLIEHDMDLVMGLADRIVV 225
|
...
gi 488284819 225 LDF 227
Cdd:COG0411 226 LDF 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-511 |
1.98e-20 |
|
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: 88.07 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 321 QVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDnskdfeeplt 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 401 ildWLRQFAgkeeddntflrsflgrMLFSgeevlkpvnvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALND 480
Cdd:cd00267 71 ---LRRRIG----------------YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....
gi 488284819 481 GLMAFTG---SILFASHDHQFIQTLANRIIAVSD 511
Cdd:cd00267 122 LLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
2.19e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.60 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNE---RLATL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwsPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNH---FdyeDYTVLETVIMGHKRLYEVMKEKDAIymkedfsdedgiraaelegefaeldgweaePEAAVLLQGLnipE 146
Cdd:PRK13548 82 PQHSslsF---PFTVEEVVAMGRAPHGLSRAEDDAL------------------------------VAAALAQVDL---A 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSL------FGKPDVLLLDEPTNGLDTR-SINWLE---EFLINFENTVIVVSHDrhfLN 216
Cdd:PRK13548 126 HLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAhQHHVLRlarQLAHERGLAVIVVLHD---LN 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-515 |
2.93e-20 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 89.13 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 321 QVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVR-WGVTTSQ-----AYLPKDNSKD 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFGKPLEKerkriGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 395 FEEPLTILD-----------WLRQFAGKEEDDntflrsflgrmlfsGEEVLKPVNV----------LSGGEKVRVMLSKL 453
Cdd:cd03235 81 RDFPISVRDvvlmglyghkgLFRRLSKADKAK--------------VDEALERVGLseladrqigeLSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 454 MLSKANVLVLDDPTNHLDLES---ITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVsDKGVI 515
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-187 |
3.06e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.17 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNE---RLATL 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawsPWElarRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQN---HFdyeDYTVLETVIMGhkrlyevmkekdaiymkedfsdedgiRAAELEGEFAEldgwEAEPEAAVLLQGLnipE 146
Cdd:COG4559 81 PQHsslAF---PFTVEEVVALG--------------------------RAPHGSSAAQD----RQIVREALALVGL---A 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488284819 147 ELHDQKMSELTAGQKVKVLLA-------QSLFGKPDVLLLDEPTNGLD 187
Cdd:COG4559 125 HLAGRSYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEPTSALD 172
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-511 |
5.11e-20 |
|
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: 88.30 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQ----------AYLP 388
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdaredyrrrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 389 KDNskDFEEPLTILDWLRqfagkeeddntFLRSFLGrMLFSGEEVL-------------KPVNVLSGGEKVRVMLSKLML 455
Cdd:COG4133 82 HAD--GLKPELTVRENLR-----------FWAALYG-LRADREAIDealeavglagladLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 456 SKANVLVLDDPTNHLDLESITALNDGLMAFT---GSILFASHDHQFIqtLANRIIAVSD 511
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
5.47e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.57 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFP-DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHF----- 74
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIpylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 75 -------DY---EDYTVLETV-----IMGHKRlyEVMKEKdaiymkedfsdedgIRAAelegefaeLDgweaepeaavlL 139
Cdd:COG2884 80 rigvvfqDFrllPDRTVYENValplrVTGKSR--KEIRRR--------------VREV--------LD-----------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 140 QGLnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFlinfeN----TVIVVSHD 211
Cdd:COG2884 125 VGL---SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETsweiMELLEEI-----NrrgtTVLIATHD 196
|
....*.
gi 488284819 212 RHFLNK 217
Cdd:COG2884 197 LELVDR 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-226 |
6.74e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 92.73 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDR-KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN-----------ERLATL 69
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNHFDYEDyTVLETVIMGhkrlyevmkEKDAiymkedfSDEDGIRAAELegefAELDGWEAEpeaavLLQGLNIPEelh 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA---------RPDA-------SDAEIREALER----AGLDEFVAA-----LPQGLDTPI--- 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSHDRHflnkvctHMADLD 226
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA-------LAALAD 524
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-230 |
8.30e-20 |
|
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: 88.71 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV--------SMGPNERLATLK--- 70
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisGLSEAELYRLRRrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 ---QNH--FDyeDYTVLETVIMGhkrlyevmkekdaIYMKEDFSDEDgIRAAELEGefaeldgweaepeaavlLQGLNIP 145
Cdd:cd03261 81 mlfQSGalFD--SLTVFENVAFP-------------LREHTRLSEEE-IREIVLEK-----------------LEAVGLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 EElHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEfLIN-----FENTVIVVSHDRHFLNKVCT 220
Cdd:cd03261 128 GA-EDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDD-LIRslkkeLGLTSIMVTHDLDTAFAIAD 205
|
250
....*....|
gi 488284819 221 HMADLDFSKI 230
Cdd:cd03261 206 RIAVLYDGKI 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-211 |
2.40e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.94 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 11 FPDR-KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNErlatlkqnhFDYEDYTVLETvimgH 89
Cdd:TIGR01166 1 YPGGpEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP---------LDYSRKGLLER----R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 90 KRLYEVMKEKDaiymkedfsdeDGIRAAELEGEFA----ELDGWEAEPEAAV--LLQGLNIpEELHDQKMSELTAGQKVK 163
Cdd:TIGR01166 68 QRVGLVFQDPD-----------DQLFAADVDQDVAfgplNLGLSEAEVERRVreALTAVGA-SGLRERPTHCLSGGEKKR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488284819 164 VLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFE---NTVIVVSHD 211
Cdd:TIGR01166 136 VAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRaegMTVVISTHD 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-286 |
3.12e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 91.17 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYE-DYTVL 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDpEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 83 ETVIMGHKrlyEVM---KEKDAIYMKEDFSdedgiraaelegeFAeldgweaePEAAVllqglnipeelhdQKMSELTAG 159
Cdd:PRK11147 402 DNLAEGKQ---EVMvngRPRHVLGYLQDFL-------------FH--------PKRAM-------------TPVKALSGG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 160 QKVKVLLAQsLFGKPDVLL-LDEPTNGLDTRSINWLEEFLINFENTVIVVSHDRHFL-NKVCTHMADLDFSKIKLYVGNY 237
Cdd:PRK11147 445 ERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGGY 523
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488284819 238 dfwlessQLATKLQAQSNAKKEEQIKELQDFIARFSANASKSKQATSRK 286
Cdd:PRK11147 524 -------HDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSYK 565
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-211 |
4.02e-19 |
|
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: 86.19 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 6 DVSLQFPDRKLFEEVNIKFT-PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------------PNER-LATL 69
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlpPQQRkIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNHFDYEDYTVLETVIMGHKRLYevmkekdaiymkedfSDEDGIRAAELegefaeldgweaepeaavlLQGLNIpEELH 149
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRKR---------------NREDRISVDEL-------------------LDLLGL-DHLL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:cd03297 126 NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-216 |
4.42e-19 |
|
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: 90.59 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRK-LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLK----QNHFDY 76
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDpaswRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 ---EDY----TVLETVIMGhkrlyevmkekdaiymKEDFSDEDGIRAAELegefAELDGWEAEpeaavLLQGLNipEELH 149
Cdd:COG4988 416 vpqNPYlfagTIRENLRLG----------------RPDASDEELEAALEA----AGLDEFVAA-----LPDGLD--TPLG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 150 DQkMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSHDRHFLN 216
Cdd:COG4988 469 EG-GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLA 536
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-515 |
6.23e-19 |
|
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: 86.25 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNltkddkvafIADSDITT---------TTLFKVIMGEITPDTGSVRW-GVTTSQ---- 384
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLS---------LPPGEVTAllgpngsgkSTLLRALAGLLKPSSGEVLLdGRDLASlsrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 385 ------AYLPKDNSKDFeePLTILD--------WLRQFAGKEEDDNTFLRSFLGRMlfsgeEVL----KPVNVLSGGEKV 446
Cdd:COG1120 72 elarriAYVPQEPPAPF--GLTVRElvalgrypHLGLFGRPSAEDREAVEEALERT-----GLEhladRPVDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 447 RVMLSKLMLSKANVLVLDDPTNHLD-------LESITALND--GLmaftgSILFASHD----HQFiqtlANRIIAVSDKG 513
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDlahqlevLELLRRLARerGR-----TVVMVLHDlnlaARY----ADRLVLLKDGR 215
|
..
gi 488284819 514 VI 515
Cdd:COG1120 216 IV 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
1.69e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQN-HFDyedy 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYLD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVIMGHKRLYEVMKEKDAIYMKEDfsdedgIRAAelegefaeldgweaepeaavllqglnipeELHDQKMSELTAG 159
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTKKEDILPALKR------VQAG-----------------------------HLIDAPMQKLSGG 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENT----VIVVSHDRHFLnkvcthMADLD 226
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldcaVLMVSHDLHLV------MAKTD 189
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-243 |
1.73e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 84.65 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNERLATLK-- 70
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGeilvdgqdITGLSEKELYELRRri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 ----QNH--FDyeDYTVLETVimghkrlyevmkekdAIYMKEdfsdedgiraaelegeFAELDGWEAEPEAAVLLQGLNI 144
Cdd:COG1127 85 gmlfQGGalFD--SLTVFENV---------------AFPLRE----------------HTDLSEAEIRELVLEKLELVGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 145 PEelHDQKM-SELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSINwleeFLIN-----FENTVIVVSHDRHFL 215
Cdd:COG1127 132 PG--AADKMpSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVID----ELIRelrdeLGLTSVVVTHDLDSA 205
|
250 260
....*....|....*....|....*...
gi 488284819 216 NKVCTHMADLDFSKIkLYVGNYDFWLES 243
Cdd:COG1127 206 FAIADRVAVLADGKI-IAEGTPEELLAS 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
1.93e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 84.11 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER-LATLKQN 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpPERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVimghkrlyevmkekdAIYMKEDFSDEDGIRAAELEgefaeldgweaepeaavLLQGLNIPEELHdQK 152
Cdd:cd03259 81 YALFPHLTVAENI---------------AFGLKLRGVPKAEIRARVRE-----------------LLELVGLEGLLN-RY 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHDR 212
Cdd:cd03259 128 PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-211 |
1.93e-18 |
|
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: 84.54 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNE--------------RL 66
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 67 ATLKQNHFDYEDYTVLETVIMGhkRLYEVMKEKDAIYMkedFSDEDGIRAAElegefaeldgweaepeaavLLQGLNIpE 146
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG--RLGRRSTWRSLFGL---FPKEEKQRALA-------------------ALERVGL-L 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:cd03256 136 DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
2.66e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 84.17 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDR----KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-------PNERLATL 69
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQN------HFD-YEDYTVLETVimghkrlyevmkekdaiymkedfsdedgirAAELEgefaeLDGWE-AEPEAAVL--- 138
Cdd:cd03258 81 RRRigmifqHFNlLSSRTVFENV------------------------------ALPLE-----IAGVPkAEIEERVLell 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 139 -LQGLnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSInwLEEFL-IN--FENTVIVVSHD 211
Cdd:cd03258 126 eLVGL---EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSI--LALLRdINreLGLTIVLITHE 200
|
250
....*....|....*....
gi 488284819 212 RHFLNKVCTHMADLDFSKI 230
Cdd:cd03258 201 MEVVKRICDRVAVMEKGEV 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
3.10e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHFDY--ED 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLDPEDRRRIGYlpEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 ytvletvimghKRLYEVMKEKD-AIYMkedfsdedgiraAELEGefaeLDGWEAEPEAAVLLQGLNIPEELHDqKMSELT 157
Cdd:COG4152 80 -----------RGLYPKMKVGEqLVYL------------ARLKG----LSKAEAKRRADEWLERLGLGDRANK-KVEELS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHD 211
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkgtTVIFSSHQ 188
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-515 |
3.93e-18 |
|
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: 83.08 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 321 QVENVSVTI-DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGV--------TTSQAYLPKD- 390
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 391 NSKDFEEplTILDWLRQFAGKEEDDNTFLRSFLGRMLFSGEEVLKPVNvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHL 470
Cdd:cd03226 81 DYQLFTD--SVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488284819 471 D---LESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSDKGVI 515
Cdd:cd03226 158 DyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
4.95e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRK-----------LF----EEV----NIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVS 59
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkgLFrreyREVeavdDISFTiePGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 60 ---MGPNERLATLKQNHfdyedytvleTVIMGHK-RL---------YEVMKekdAIYmkedfsdedGIRAAELE---GEF 123
Cdd:COG4586 81 vlgYVPFKRRKEFARRI----------GVVFGQRsQLwwdlpaidsFRLLK---AIY---------RIPDAEYKkrlDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 124 AELdgweaepeaavllqgLNIpEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INF 201
Cdd:COG4586 139 VEL---------------LDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeYNR 202
|
250
....*....|..
gi 488284819 202 EN--TVIVVSHD 211
Cdd:COG4586 203 ERgtTILLTSHD 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
6.93e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-----------PNERLATL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNHFDYEDYTVLETVIMG---HKRLYEVMkekdaiymkedfsDEDGIRAAELEGEFAELDgweaepeaavllqglnipe 146
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrtpHRSRFDTW-------------TETDRAAVERAMERTGVA------------------- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD-TRSINWLE--EFLINFENTVIVVSHDRHFLNKVC 219
Cdd:PRK09536 131 QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVRTLElvRRLVDDGKTAVAAIHDLDLAARYC 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
435-530 |
7.38e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 86.93 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 435 KPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVsDKGV 514
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGK 230
|
90
....*....|....*.
gi 488284819 515 IDRAETTYDEFLENPE 530
Cdd:PRK11147 231 LVSYPGNYDQYLLEKE 246
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-515 |
1.10e-17 |
|
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: 80.94 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 321 QVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKdfeeplt 400
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 401 ILDWLRQFAgkeedDNTFLRSFLGRmlfsgeevlkPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD-------LE 473
Cdd:cd03214 74 KIAYVPQAL-----ELLGLAHLADR----------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqielLE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488284819 474 SITALND--GLmaftgSILFASHDHQFIQTLANRIIAVSDKGVI 515
Cdd:cd03214 139 LLRRLARerGK-----TVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
1.48e-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: 81.48 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD--RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhFDYEDY 79
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL--------------LDGTDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLE-TVIMGHkrLYEVMKE--------KDAIYMKEDF-SDEDGIRAAELEG--EFAELDGweaepeaavllQGLNIpeE 147
Cdd:cd03245 69 RQLDpADLRRN--IGYVPQDvtlfygtlRDNITLGAPLaDDERILRAAELAGvtDFVNKHP-----------NGLDL--Q 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 148 LHDQKMSeLTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSHDRHFLNKV 218
Cdd:cd03245 134 IGERGRG-LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLV 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-233 |
1.50e-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: 81.81 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 20 VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpNERLATLkqnhFDY-----EDYTVLETV-----IMGH 89
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSL----LGLgggfnPELTGRENIylngrLLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 90 KRlyEVMKEK-DAIYmkedfsdedgiraaelegEFAELdgweaepeaavllqglnipEELHDQKMSELTAGQKVKVLLAQ 168
Cdd:cd03220 115 SR--KEIDEKiDEII------------------EFSEL-------------------GDFIDLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 169 SLFGKPDVLLLDEPTNGLDT----RSINWLEEFLINFEnTVIVVSHDRHFLNKVCTHMADLDFSKIKLY 233
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAafqeKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-230 |
2.86e-17 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 82.44 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 20 VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSM--GPNERLATLKQNHFDYEDYTVLETVIMgH 89
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtarvagydVVREprKVRRSIGIVPQYASVDEDLTGRENLEM-M 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 90 KRLYEvmkekdaiymkedfsdedgiraaelegefaeLDGWEAEPEAAVLLQGLNIPEElHDQKMSELTAGQKVKVLLAQS 169
Cdd:TIGR01188 91 GRLYG-------------------------------LPKDEAEERAEELLELFELGEA-ADRPVGTYSGGMRRRLDIAAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 170 LFGKPDVLLLDEPTNGLD--TRSINW-LEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKI 230
Cdd:TIGR01188 139 LIHQPDVLFLDEPTTGLDprTRRAIWdYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
320-528 |
3.29e-17 |
|
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: 84.81 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVT-IDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTS-------------- 383
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSdldpaswrrqiawv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 384 --QAYLPKDnskdfeeplTILDWLRqfagkeeddntflrsfLGRMLFSGEEV---LKPVNV------------------- 439
Cdd:COG4988 417 pqNPYLFAG---------TIRENLR----------------LGRPDASDEELeaaLEAAGLdefvaalpdgldtplgegg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 440 --LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLMAFTGS--ILFASHDHQFIqTLANRIIAVsDKGVI 515
Cdd:COG4988 472 rgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALL-AQADRILVL-DDGRI 549
|
250
....*....|...
gi 488284819 516 dRAETTYDEFLEN 528
Cdd:COG4988 550 -VEQGTHEELLAK 561
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-542 |
3.47e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 26 PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN-----ERLA-TLKQNHFdyedytvletvimghKRLYE----- 94
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlKRFRgTELQNYF---------------KKLYNgeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 95 VMKEK--DAIYMKEDFSDEDGIRAAELEGEFAELdgweaepeaavlLQGLNIpEELHDQKMSELTAGQKVKVLLAQSLFG 172
Cdd:PRK13409 163 VHKPQyvDLIPKVFKGKVRELLKKVDERGKLDEV------------VERLGL-ENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 173 KPDVLLLDEPTNGLD-------TRSINWLEEflinfENTVIVVSHDrhflnkvcthMADLD------------------F 227
Cdd:PRK13409 230 DADFYFFDEPTSYLDirqrlnvARLIRELAE-----GKYVLVVEHD----------LAVLDyladnvhiaygepgaygvV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 228 SKIK-LYVG--NYdfwlessqLATKLqaqsnakKEEQIkelqdfiaRFsanaskskqatsrkkmldkitlddiqpssRRY 304
Cdd:PRK13409 295 SKPKgVRVGinEY--------LKGYL-------PEENM--------RI-----------------------------RPE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 305 P--FVGFTPEREI-GNDLLQVENVSVTIDGkkildnisFNLT-------KDDKVAFIADSDITTTTLFKVIMGEITPDTG 374
Cdd:PRK13409 323 PieFEERPPRDESeRETLVEYPDLTKKLGD--------FSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 375 SVRWGVTTSqaYLPKDNSKDFEEplTILDWLRQFAGKEedDNTFLRSFLGRMLfSGEEVL-KPVNVLSGGEKVRVMLSKL 453
Cdd:PRK13409 395 EVDPELKIS--YKPQYIKPDYDG--TVEDLLRSITDDL--GSSYYKSEIIKPL-QLERLLdKNVKDLSGGELQRVAIAAC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 454 MLSKANVLVLDDPTNHLDLE----------SITALNDglmaftGSILFASHDHQFIQTLANRIIAVSDK-GVIDRAETTY 522
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEqrlavakairRIAEERE------ATALVVDHDIYMIDYISDRLMVFEGEpGKHGHASGPM 541
|
570 580
....*....|....*....|....*.
gi 488284819 523 D------EFLenpeiqKQMDILFSSD 542
Cdd:PRK13409 542 DmregmnRFL------KELGITFRRD 561
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
3.74e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.59 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDR----KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM------GPNERLATLKQ 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NH--FDYedYTVLETVIMGHKRlyevmkekdaiymkedfsdeDGIRAAElegefaeldgWEAEPEAAVLLQGLnipEELH 149
Cdd:cd03293 81 QDalLPW--LTVLDNVALGLEL--------------------QGVPKAE----------ARERAEELLELVGL---SGFE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD--TRSI--NWLEEFLINFENTVIVVSHD 211
Cdd:cd03293 126 NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDalTREQlqEELLDIWRETGKTVLLVTHD 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-527 |
4.86e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 80.49 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIadsdittTTLFKVIMGEITPDTGSVRWG---VTTSQA-------YLPK 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLgpngagkTTTIRMLLGLLRPTSGEVRVLgedVARDPAevrrrigYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 DNSkdFEEPLTILDWLRQFAGKEEDDNTFLRSFLGRML--FSGEEVL-KPVNVLSGGEKVRVMLSKLMLSKANVLVLDDP 466
Cdd:COG1131 81 EPA--LYPDLTVRENLRFFARLYGLPRKEARERIDELLelFGLTDAAdRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 467 TNHLDLESITALNDGLMAFTG---SILFASHDHQFIQTLANRIIAVsDKGVIdRAETTYDEFLE 527
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAII-DKGRI-VADGTPDELKA 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-468 |
6.12e-17 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 78.07 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 335 LDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKD----FEEP-----LTILDWL 405
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEigyvFQDPqlfprLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 406 R-----QFAGKEEDDN--TFLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTN 468
Cdd:pfam00005 81 RlglllKGLSKREKDAraEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-495 |
7.13e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 318 DLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKDFEE 397
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 398 PLTILDWLRQFAGKEEDDntfLRSFLGRMLfSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITA 477
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKED---ILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|..
gi 488284819 478 LNDGL----MAFTGSILFASHD 495
Cdd:PRK09544 159 LYDLIdqlrRELDCAVLMVSHD 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-513 |
7.68e-17 |
|
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: 78.19 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDG--KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWgvttsqaylpkdNSKDFEE 397
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------DGVDLRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 398 pLTILDWLRQFAgkEEDDNTFLrsflgrmlFSG--EEvlkpvNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESI 475
Cdd:cd03228 69 -LDLESLRKNIA--YVPQDPFL--------FSGtiRE-----NILSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488284819 476 TALNDGLMAFTG--SILFASHDHQFIQtLANRIIaVSDKG 513
Cdd:cd03228 133 ALILEALRALAKgkTVIVIAHRLSTIR-DADRII-VLDDG 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-514 |
8.97e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 78.03 E-value: 8.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKK--ILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDnskdfee 397
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 398 pltildwLRQFAGK-EEDDntflrsflgrMLFSG---EevlkpvNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLE 473
Cdd:cd03246 74 -------LGDHVGYlPQDD----------ELFSGsiaE------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488284819 474 SITALND---GLMAFTGSILFASHDHQFIqTLANRIIAVSDKGV 514
Cdd:cd03246 131 GERALNQaiaALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
1.63e-16 |
|
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: 78.70 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEV--NIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNErLATLKQNHFDy 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAldDVSFSikKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKD-LLKLSRRLRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 edytvletvIMGHK----------RLYEVMKEKDAIymKEDFSDEDGIRAAELEGEFAELdgweaepeaavLLQGLNIPE 146
Cdd:cd03257 79 ---------IRRKEiqmvfqdpmsSLNPRMTIGEQI--AEPLRIHGKLSKKEARKEAVLL-----------LLVGVGLPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHDRHFLNKVCTHM 222
Cdd:cd03257 137 EVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRV 216
|
.
gi 488284819 223 A 223
Cdd:cd03257 217 A 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
1.95e-16 |
|
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: 82.16 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQF--PDRKLFEEV-NIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM------------GPN 63
Cdd:TIGR03269 279 IIKVRNVSKRYisVDRGVVKAVdNVSLEvkEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 64 ER------LATLKQNHFDYEDYTVLETVimghkrlyevmkeKDAIYMkeDFSDEDGIRAAELEGEFAELDGWEAepeaav 137
Cdd:TIGR03269 359 GRgrakryIGILHQEYDLYPHRTVLDNL-------------TEAIGL--ELPDELARMKAVITLKMVGFDEEKA------ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 138 llqglnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLIN----FENTVIVVSHDRH 213
Cdd:TIGR03269 418 --------EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKareeMEQTFIIVSHDMD 489
|
250
....*....|....*..
gi 488284819 214 FLNKVCTHMADLDFSKI 230
Cdd:TIGR03269 490 FVLDVCDRAALMRDGKI 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-511 |
2.22e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 77.23 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYlpKDNSKDFEEPL 399
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL--EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 400 TILdwLRQFAgkeeddntflrsflgrmLFSGEEVLKpvNV---LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLES-- 474
Cdd:cd03229 79 GMV--FQDFA-----------------LFPHLTVLE--NIalgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITrr 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488284819 475 -----ITALNDGLmAFTgsILFASHDHQFIQTLANRIIAVSD 511
Cdd:cd03229 138 evralLKSLQAQL-GIT--VVLVTHDLDEAARLADRVVVLRD 176
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-210 |
2.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.68 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFE-----EVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpnerlatlkqnhfdy 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 edytvlETVIMGHKR---------------------LYEVMKEKDAIYMKEDF--SDEdgiraaelegefaeldgwEAEP 133
Cdd:PRK13634 68 ------ERVITAGKKnkklkplrkkvgivfqfpehqLFEETVEKDICFGPMNFgvSEE------------------DAKQ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 134 EAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSinwLEEFLINFEN-------TVI 206
Cdd:PRK13634 124 KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG---RKEMMEMFYKlhkekglTTV 200
|
....
gi 488284819 207 VVSH 210
Cdd:PRK13634 201 LVTH 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-210 |
4.19e-16 |
|
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: 76.10 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRK--LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpneRLatlkqnhfdyeDY 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV------RL-----------DG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVIMGHKRlyevmkekDAI-YMKEDfsdedgiraAELegefaeLDGWEAEpeaavllqglNIpeelhdqkmseLTA 158
Cdd:cd03246 64 ADISQWDPNELG--------DHVgYLPQD---------DEL------FSGSIAE----------NI-----------LSG 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFE---NTVIVVSH 210
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-193 |
5.59e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM--------GPNERLATLKQNH 73
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsrARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 FDY--EDYTVLETVIMghkrlyevmkekdaiymkedFSDEDGIRAAELEG------EFAELdgweaepeaavllqglnip 145
Cdd:PRK13537 88 FDNldPDFTVRENLLV--------------------FGRYFGLSAAAARAlvppllEFAKL------------------- 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 EELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD--TRSINW 193
Cdd:PRK13537 129 ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMW 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-527 |
5.85e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.45 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNERL----AT 68
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGeilldgepVRFRSPRDAQaagiAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 69 LKQ--NHFDyeDYTVLETVIMGH----------KRLYEvmkekdaiymkedfsdedgiRAAELegeFAELdgweaepeaa 136
Cdd:COG1129 84 IHQelNLVP--NLSVAENIFLGReprrgglidwRAMRR--------------------RAREL---LARL---------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 137 vllqGLNIPEelhDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLeeflinFEN---------TVIV 207
Cdd:COG1129 129 ----GLDIDP---DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL------FRIirrlkaqgvAIIY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 208 VSHdrhflnkvcthmadldfskiKLyvgnydfwlessqlatklqaqsnakkeEQIKELQD---------FIARFSAnask 278
Cdd:COG1129 196 ISH--------------------RL---------------------------DEVFEIADrvtvlrdgrLVGTGPV---- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 279 skQATSRKKMLDKITLDDIqpsSRRYPfvgfTPEREIGNDLLQVENVSVtidgKKILDNISFNLTKDDKVAFiadsditT 358
Cdd:COG1129 225 --AELTEDELVRLMVGREL---EDLFP----KRAAAPGEVVLEVEGLSV----GGVVRDVSFSVRAGEILGI-------A 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 359 -------TTLFKVIMGEITPDTGSVRWG------VTTSQA------YLPKDNSKD--FEEpLTILD-----WLRQFA--- 409
Cdd:COG1129 285 glvgagrTELARALFGADPADSGEIRLDgkpvriRSPRDAiragiaYVPEDRKGEglVLD-LSIREnitlaSLDRLSrgg 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 410 ----GKEEDD-NTFLRSFlgRMLFSGEEvlKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD-------LESITA 477
Cdd:COG1129 364 lldrRRERALaEEYIKRL--RIKTPSPE--QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiYRLIRE 439
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 488284819 478 L-NDGLmaftgSILFASHDHQFIQTLANRIIAVSD---KGVIDRAETTYDEFLE 527
Cdd:COG1129 440 LaAEGK-----AVIVISSELPELLGLSDRILVMREgriVGELDREEATEEAIMA 488
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-230 |
6.06e-16 |
|
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: 77.02 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGvvsmgpnerlatlkqnhfdyedytv 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 lETVIMGHKRLYEVMKEKDAI-YMKEDFSDEDGIRAAE---LEGEFAELDGWEAEPEAAVLLQGLNIpEELHDQKMSELT 157
Cdd:cd03265 56 -RATVAGHDVVREPREVRRRIgIVFQDLSVDDELTGWEnlyIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLD--TRSINW--LEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKI 230
Cdd:cd03265 134 GGMRRRLEIARSLVHRPEVLFLDEPTIGLDpqTRAHVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-223 |
7.59e-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: 75.69 E-value: 7.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhFDYEDYTV 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL--------------IDGEDLTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 LETVIMGHKRlyevmkekDAIYMKEDFSdedgiraaelegefaeldgweaepeaavLLQGLNIPEELhdqkMSELTAGQK 161
Cdd:cd03229 67 LEDELPPLRR--------RIGMVFQDFA----------------------------LFPHLTVLENI----ALGLSGGQQ 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 162 VKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLI----NFENTVIVVSHDRHFLNKVCTHMA 223
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVV 172
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
7.93e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 11 FPDRKLFEeVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDYTVLETVIMGHK 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 91 RLYEVMKEKDAIYMKEDFsdedGIRAAElegefaeldgweAEPEAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLAQSL 170
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNF----GIPKEK------------AEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488284819 171 FGKPDVLLLDEPTNGLDTRS---INWLEEFLINFENTVIVVSH 210
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
2.11e-15 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 73.96 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDR--KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHFdyedy 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-GVDLRDLDLESL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 tvletvimgHKRLYEVmkekdaiymkedfsdedgiraaelegefaeldgweaePEAAVLLQGL---NIpeelhdqkmseL 156
Cdd:cd03228 75 ---------RKNIAYV-------------------------------------PQDPFLFSGTireNI-----------L 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSHDRH 213
Cdd:cd03228 98 SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLS 156
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
2.15e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV--------SMGPNE---RLATL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpisMLSSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNHFDYEDYTVLETVIMG---HKRLYEVMKEKDaiymkedfsdedgiraaelegefaeldgwEAEPEAAvlLQGLNIpE 146
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLWGRLSAED-----------------------------NARVNQA--MEQTRI-N 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDtrsINWLEEFL-----INFE-NTVIVVSHDrhfLNKVC 219
Cdd:PRK11231 130 HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHQVELMrlmreLNTQgKTVVTVLHD---LNQAS 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-542 |
3.33e-15 |
|
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: 78.29 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 26 PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN-----ERLA-TLKQNHFdyedytvletvimghKRLYEvmKEK 99
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlKRFRgTELQDYF---------------KKLAN--GEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 100 DAIYmKEDFSDE-----DGIRAAELEG--EFAELDGweaepeaavLLQGLNIpEELHDQKMSELTAGQKVKVLLAQSLFG 172
Cdd:COG1245 161 KVAH-KPQYVDLipkvfKGTVRELLEKvdERGKLDE---------LAEKLGL-ENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 173 KPDVLLLDEPTNGLD-------TRSINWLEEflinfEN-TVIVVSHDrhflnkvcthMADLD------------------ 226
Cdd:COG1245 230 DADFYFFDEPSSYLDiyqrlnvARLIRELAE-----EGkYVLVVEHD----------LAILDyladyvhilygepgvygv 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 227 FSKIK-LYVG--NY-DFWLessqlatklqaqsnakKEEQIKELQDFIaRFSANASKSKQATSrkkmlDKITLDDIqpsSR 302
Cdd:COG1245 295 VSKPKsVRVGinQYlDGYL----------------PEENVRIRDEPI-EFEVHAPRREKEEE-----TLVEYPDL---TK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 303 RYPfvGFTPEREIGNdlLQVENVsVTIDGKkildnisfnltkddkvafiadSDITTTTLFKVIMGEITPDTGSVRWGVTT 382
Cdd:COG1245 350 SYG--GFSLEVEGGE--IREGEV-LGIVGP---------------------NGIGKTTFAKILAGVLKPDEGEVDEDLKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 383 SqaYLPKDNSKDFEEplTILDWLRQFAGKEEDDNTF----LRSF-LGRMLfsgeevLKPVNVLSGGEKVRVMLSKLMLSK 457
Cdd:COG1245 404 S--YKPQYISPDYDG--TVEEFLRSANTDDFGSSYYkteiIKPLgLEKLL------DKNVKDLSGGELQRVAIAACLSRD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 458 ANVLVLDDPTNHLDLESITALNDGLMAFT----GSILFASHDHQFIQTLANRIIAVSDK-GVIDRAETTYD------EFL 526
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFAenrgKTAMVVDHDIYLIDYISDRLMVFEGEpGVHGHASGPMDmregmnRFL 553
|
570
....*....|....*.
gi 488284819 527 enpeiqKQMDILFSSD 542
Cdd:COG1245 554 ------KELGITFRRD 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-218 |
4.05e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 78.27 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD--RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNE---RLAT 68
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldEDDlrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 69 LKQNH--FDYedyTVLETVIMGhkrlyevmkekdaiymKEDFSDEDGIRAAELegefAELDGWEAEpeaavLLQGLNIP- 145
Cdd:COG4987 414 VPQRPhlFDT---TLRENLRLA----------------RPDATDEELWAALER----VGLGDWLAA-----LPDGLDTWl 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 146 EELHDQkmseLTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT---RSInwLEEFLINFEN-TVIVVSHDRHFLNKV 218
Cdd:COG4987 466 GEGGRR----LSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAGrTVLLITHRLAGLERM 536
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
4.41e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.20 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILS--GEIQP---TTGVVSM------GPNERLATL 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYnghniySPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQ---------NHFDYedyTVLETVIMGhKRLYEVmKEKDAIymkeDFSDEDGIRAAELegefaeldgWEaepeaavllq 140
Cdd:PRK14239 85 RKeigmvfqqpNPFPM---SIYENVVYG-LRLKGI-KDKQVL----DEAVEKSLKGASI---------WD---------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 141 glNIPEELHDQKMSeLTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSH 210
Cdd:PRK14239 137 --EVKDRLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
5.03e-15 |
|
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: 74.68 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNER-LATLKQN 72
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGtilfggedATDVPVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHKrlyevmkekdaIYMKEDFSDEDGIRAAELEG-EFAELDGweaepeaavllqglnipeeLHDQ 151
Cdd:cd03296 83 YALFRHMTVFDNVAFGLR-----------VKPRSERPPEAEIRAKVHELlKLVQLDW-------------------LADR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 152 KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:cd03296 133 YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHD 196
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
320-494 |
5.73e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTS--QAYLPKDNS----- 392
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENIlylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 393 ----KDFEEPLTILDWLRQFAGKEedDNTFLRSfLGRMLFSGEEVLkPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTN 468
Cdd:TIGR01189 81 lpglKPELSALENLHFWAAIHGGA--QRTIEDA-LAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 488284819 469 HLDLESITALNDGLMAFT---GSILFASH 494
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLargGIVLLTTH 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
6.31e-15 |
|
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: 74.01 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFP-----DRKL--FEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG---VVSMGPNERLATLk 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsilVRHDGGWVDLAQA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 qnhfdyEDYTVLE-------------TVImghKRL--YEVMKEKdAIymkedfsdEDGIRAAElegefaeldgweAEPEA 135
Cdd:COG4778 83 ------SPREILAlrrrtigyvsqflRVI---PRVsaLDVVAEP-LL--------ERGVDREE------------ARARA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 136 AVLLQGLNIPEELHDqkMSELT--AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINfENTVIVVS 209
Cdd:COG4778 133 RELLARLNLPERLWD--LPPATfsGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR-GTAIIGIF 209
|
250
....*....|....*..
gi 488284819 210 HDRHFLNKVCTHMADLD 226
Cdd:COG4778 210 HDEEVREAVADRVVDVT 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-534 |
9.97e-15 |
|
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: 73.52 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTI-DGKKILDNISFNLTKDDKVAFIADsditT----TTLFKVIMGEITPDTGSVRW-GVTTSQAYLPKdnsk 393
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGP----NgsgkSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 394 dfeepltildwLRQ-------------FAGKEEDDNTF-LRSfLGrmlFSGEEVL-----------------KPVNVLSG 442
Cdd:COG1122 73 -----------LRRkvglvfqnpddqlFAPTVEEDVAFgPEN-LG---LPREEIRerveealelvglehladRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 443 GEKVRVMLSKLMLSKANVLVLDDPTNHLDLES-------ITALNDGLMaftgSILFASHDHQFIQTLANRIIAVSDKGVI 515
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGrrellelLKRLNKEGK----TVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
250
....*....|....*....
gi 488284819 516 drAETTYDEFLENPEIQKQ 534
Cdd:COG1122 214 --ADGTPREVFSDYELLEE 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.17e-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: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnHFDYEDYTV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI--------------LVDGKEVSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 LETvimghkrlyevmkeKDAIymkedfsdEDGIraaelegefaeldgweaepeaAVLLQglnipeelhdqkmseLTAGQK 161
Cdd:cd03216 67 ASP--------------RDAR--------RAGI---------------------AMVYQ---------------LSVGER 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488284819 162 VKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-524 |
1.42e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 20 VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM--------GPNERLAT----LKQnHF-DYEDYTVLETVI 86
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvrirSPRDAIALgigmVHQ-HFmLVPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 87 MGHKRLyevmkekdaiymKEDFSDEDGIRA--AELEGEFaeldGWEAEPEAAVllqglnipeelhdqkmSELTAG--QKV 162
Cdd:COG3845 103 LGLEPT------------KGGRLDRKAARAriRELSERY----GLDVDPDAKV----------------EDLSVGeqQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 163 KVLLAqsLFGKPDVLLLDEPTNGLDTRSInwlEEFLINFEN------TVIVVSHdrhflnkvcthmadldfskiKLyvgn 236
Cdd:COG3845 151 EILKA--LYRGARILILDEPTAVLTPQEA---DELFEILRRlaaegkSIIFITH--------------------KL---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 237 ydfwlessqlatklqaqsnakkEEqIKELQDFIA-----RFSANASKSKqaTSRKKMLDKITLDDIQPSSRRypfvgftP 311
Cdd:COG3845 202 ----------------------RE-VMAIADRVTvlrrgKVVGTVDTAE--TSEEELAELMVGREVLLRVEK-------A 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 312 EREIGNDLLQVENVSVTID-GKKILDNISFNLTKDDKVAfIAdsd-ittTTLFKVIMGEITPDTGSVRW------GVTTS 383
Cdd:COG3845 250 PAEPGEVVLEVENLSVRDDrGVPALKDVSLEVRAGEILG-IAgvagngqSELAEALAGLRPPASGSIRLdgeditGLSPR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 384 Q------AYLPkdnskdfEEPL---TILDW-------LRQFagkeeDDNTFLRSFL---GRMLFSGEEVLK--------- 435
Cdd:COG3845 329 ErrrlgvAYIP-------EDRLgrgLVPDMsvaenliLGRY-----RRPPFSRGGFldrKAIRAFAEELIEefdvrtpgp 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 436 --PVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLMAFT---GSILFASHDHQFIQTLANRIIAVS 510
Cdd:COG3845 397 dtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLISEDLDEILALSDRIAVMY 476
|
570
....*....|....*..
gi 488284819 511 D---KGVIDRAETTYDE 524
Cdd:COG3845 477 EgriVGEVPAAEATREE 493
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-193 |
1.66e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVS-MG---PNE-RLATLKQN---H 73
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGvpvPARaRLARARIGvvpQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 FDYED--YTVLETVIMghkrlyevmkekdaiymkedFSDEDGIRAAELEG------EFAELdgweaepeaavllqglnip 145
Cdd:PRK13536 122 FDNLDleFTVRENLLV--------------------FGRYFGMSTREIEAvipsllEFARL------------------- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 EELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD--TRSINW 193
Cdd:PRK13536 163 ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIW 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-471 |
1.75e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 10 QFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILS---------GEI----QPTT----------GVVSMgpNERL 66
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphgtyeGEIifegEELQasnirdteraGIAII--HQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 67 ATLKQnhfdyedYTVLETVIMGHKRLYEVMKEKDAIYmkedfsdedgIRAAELegeFAELdgweaepeaavllqGLNIPE 146
Cdd:PRK13549 92 ALVKE-------LSVLENIFLGNEITPGGIMDYDAMY----------LRAQKL---LAQL--------------KLDINP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 elhDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHdrhflnkvcthma 223
Cdd:PRK13549 138 ---ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISH------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 224 dldfskiklyvgnydfwlessqlatklqaqsnakKEEQIKELQDFIA--RfsanasKSKQATSRKKmlDKITLDDI---- 297
Cdd:PRK13549 202 ----------------------------------KLNEVKAISDTICviR------DGRHIGTRPA--AGMTEDDIitmm 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 298 --QPSSRRYPFVgftpEREIGNDLLQVENVS---VTIDGKKILDNISFNLTKDD--KVAFIADSDITTT--TLFKVIMG- 367
Cdd:PRK13549 240 vgRELTALYPRE----PHTIGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEilGIAGLVGAGRTELvqCLFGAYPGr 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 368 ------------EITPDTGSVRWGVttsqAYLPKDNSKDFEEPL------TILDWLRQFAGK----EEDDNTFLRSFLGR 425
Cdd:PRK13549 316 wegeifidgkpvKIRNPQQAIAQGI----AMVPEDRKRDGIVPVmgvgknITLAALDRFTGGsridDAAELKTILESIQR 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 488284819 426 MLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD 471
Cdd:PRK13549 392 LKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-516 |
2.45e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---------VTTSQ--AYLP 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaRAASRrvASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 389 KDNSKDFE-EPLTILDWLR-----QFAGKEEDDNTFLRSFLGRMlFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLV 462
Cdd:PRK09536 84 QDTSLSFEfDVRQVVEMGRtphrsRFDTWTETDRAAVERAMERT-GVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 463 LDDPTNHLD-------LESITALNDglmafTG-SILFASHDHQFIQTLANRIIAVSDKGVID 516
Cdd:PRK09536 163 LDEPTASLDinhqvrtLELVRRLVD-----DGkTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-511 |
2.73e-14 |
|
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: 71.73 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 321 QVENVSVTIDG--KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKD---- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 395 FEEP------LTILD----WLRQFAGKEEDDNTFLRSFLGRMLFSGEEvLKPVNVLSGGEKVRVMLSKLMLSKANVLVLD 464
Cdd:cd03225 81 FQNPddqffgPTVEEevafGLENLGLPEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 465 DPTNHLDLESITAL--------NDGLmaftgSILFASHDHQFIQTLANRIIAVSD 511
Cdd:cd03225 160 EPTAGLDPAGRRELlellkklkAEGK-----TIIIVTHDLDLLLELADRVIVLED 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-530 |
3.79e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 74.94 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDG--KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPD---TGSVRWG----VTTSQAYLPK 389
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgrdlLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 DNSKDFEEPLTILDWLR---QFAGKEEDDNTFLRSFLGRMLFSGEEV------LKPVNVLSGGEKVRVMLSKLMLSKANV 460
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTvgdQIAEALENLGLSRAEARARVLELLEAVglerrlDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 461 LVLDDPTNHLDLES---ITALNDGLMAFTG-SILFASHDHQFIQTLANRIIaVSDKGVIdRAETTYDEFLENPE 530
Cdd:COG1123 164 LIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVV-VMDDGRI-VEDGPPEEILAAPQ 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-211 |
4.43e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.89 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFE-----EVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDY 76
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEhqaihDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 EDYTVLETVIMGHKRLYEVMKEKDAIYMKEDFSdedgiraaelegefaeLDGWEAEPEAAVLLQGLNIPEELHDQKMSEL 156
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREIIFGPKNFK----------------MNLDEVKNYAHRLLMDLGFSRDVMSQSPFQM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
320-535 |
1.16e-13 |
|
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: 73.65 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDG--KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG-----------------V 380
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeddlrrriaV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 381 TTSQAYLpkdnskdFEEplTILDWLRqFAGKEEDDN------------TFLRSF---LGRMLfsGEEVLKpvnvLSGGEK 445
Cdd:COG4987 414 VPQRPHL-------FDT--TLRENLR-LARPDATDEelwaalervglgDWLAALpdgLDTWL--GEGGRR----LSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 446 VRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLMAFTG--SILFASHDHQFIQtLANRIIAVSDKGVIDRAetTYD 523
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLE-RMDRILVLEDGRIVEQG--THE 554
|
250
....*....|..
gi 488284819 524 EFLENPEIQKQM 535
Cdd:COG4987 555 ELLAQNGRYRQL 566
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
1.25e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.88 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-------PNE----RLATL 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRelakRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQ-NHFDYEdYTVLETVIMG----HK-RLyevmkekdaiymkedfSDEDgiraaelegefaeldgWEAEPEAavlLQGLN 143
Cdd:COG4604 81 RQeNHINSR-LTVRELVAFGrfpySKgRL----------------TAED----------------REIIDEA---IAYLD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 144 IpEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSI-NWLEEFLINFENTVIVVSHD 211
Cdd:COG4604 125 L-EDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhSVQMmKLLRRLADELGKTVVIVLHD 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-211 |
2.03e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.80 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 18 EEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM--------GPnERLATLkQNHFDYEDYTVLETVIMGH 89
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILegkqitepGP-DRMVVF-QNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 90 KRLYEVMKEKDAIYMKEDFSDEDGIRAAElegefaeldgweaepeaavllqglnipeelhDQKMSELTAGQKVKVLLAQS 169
Cdd:TIGR01184 80 DRVLPDLSKSERRAIVEEHIALVGLTEAA-------------------------------DKRPGQLSGGMKQRVAIARA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488284819 170 LFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSHD 211
Cdd:TIGR01184 129 LSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEehrvTVLMVTHD 174
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-211 |
2.45e-13 |
|
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: 69.21 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER-LATLKQN 72
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlpPKDRdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHKRLYEvmkEKDAIymkedfsDEDGIRAAELegefaeldgweaepeaavllqgLNIpEELHDQK 152
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKV---PKDEI-------DERVREVAEL----------------------LQI-EHLLDRK 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTR----SINWLEEFLINFENTVIVVSHD 211
Cdd:cd03301 128 PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKlrvqMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-211 |
2.55e-13 |
|
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: 69.67 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLfEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNER-LATLKQN 72
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkillngkdITNLPPEKRdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHKRLYEVMKEKDAIYMkedfsdedgiraaelegEFAELdgweaepeaavllqgLNIpEELHDQK 152
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVL-----------------EIAEM---------------LGI-DHLLNRK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:cd03299 127 PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-515 |
2.96e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 69.07 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGK----KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQAYLPKDN 391
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 392 SKD----FEEP-------LTILDWLR---QFAGKEEDDNTFLRsflgRMLFSGEEVLKPVNV-------LSGGEKVRVML 450
Cdd:cd03257 81 RKEiqmvFQDPmsslnprMTIGEQIAeplRIHGKLSKKEARKE----AVLLLLVGVGLPEEVlnrypheLSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 451 SKLMLSKANVLVLDDPTNHLD-------LESITALNDglmAFTGSILFASHDHQFIQTLANRiIAVSDKGVI 515
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQE---ELGLTLLFITHDLGVVAKIADR-VAVMYAGKI 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-509 |
2.96e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW--------GVTTSQAYL-PKD 390
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdiddpDVAEACHYLgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 391 NSKDFeepLTILDWLRqfagkeeddntFLRSFLGRMLFSGEEVLK----------PVNVLSGGEKVRVMLSKLMLSKANV 460
Cdd:PRK13539 83 AMKPA---LTVAENLE-----------FWAAFLGGEELDIAAALEavglaplahlPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488284819 461 LVLDDPTNHLDLESItALNDGLMAF---TGSILFAShDHQFIQTLANRIIAV 509
Cdd:PRK13539 149 WILDEPTAALDAAAV-ALFAELIRAhlaQGGIVIAA-THIPLGLPGARELDL 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
3.16e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILS------GEIQPTTGVVSMGPN--ERLATL---- 69
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNiyERRVNLnrlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 --------KQNHFDYedyTVLETVIMGHKRL-YEVMKEKDAIYmkedfsdEDGIRAAELegefaeldgWEaepeaavllq 140
Cdd:PRK14258 88 rqvsmvhpKPNLFPM---SVYDNVAYGVKIVgWRPKLEIDDIV-------ESALKDADL---------WD---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 141 glNIPEELHDQKMsELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF----ENTVIVVSHDRHFLN 216
Cdd:PRK14258 139 --EIKHKIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVS 215
|
..
gi 488284819 217 KV 218
Cdd:PRK14258 216 RL 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-223 |
3.42e-13 |
|
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: 72.74 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 26 PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDY---EDYTVLETVIMGHKRLYEVMKEKdai 102
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycPQFDAIDDLLTGREHLYLYARLR--- 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 103 ymkedfsdedGIRAAELEgefaELDGWEAEPeaavllQGLNIpeeLHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEP 182
Cdd:TIGR01257 2041 ----------GVPAEEIE----KVANWSIQS------LGLSL---YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488284819 183 TNGLDTRSINWLEEFLINF---ENTVIVVSHDRHFLNKVCTHMA 223
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRLA 2141
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
3.83e-13 |
|
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: 69.19 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNER-LATLKQN 72
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeilldgkdITNLPPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHKRLyevmkekdaiymkedfsdedGIRAAELEGEFAEldgweaepeaAVLLQGLnipEELHDQK 152
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLK--------------------KLPKAEIKERVAE----------ALDLVQL---EGYANRK 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSHD 211
Cdd:cd03300 128 PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-226 |
5.17e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.11 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRK-----LfEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-------PNERLAT 68
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtaL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 69 LKQN------HFD-YEDYTVLETV-----IMGHKRlyevmKEKDAiymkedfsdedgiRAAELegefaeLDgweaepeaa 136
Cdd:COG1135 80 ARRKigmifqHFNlLSSRTVAENValpleIAGVPK-----AEIRK-------------RVAEL------LE--------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 137 vlLQGLnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSInwLEefL---INFE-N-TVIVV 208
Cdd:COG1135 127 --LVGL---SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSI--LD--LlkdINRElGlTIVLI 197
|
250
....*....|....*...
gi 488284819 209 SHDRHFLNKVCTHMADLD 226
Cdd:COG1135 198 THEMDVVRRICDRVAVLE 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-231 |
5.33e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.23 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM-GPNERLATLKQNHFDYEDYT 80
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLE------TVIMGHKRLYEVMKEKDAIymkedfsdedgiraAELEGEFAELDGWEAEPEAAVLLQGLNIPEELHDQKMS 154
Cdd:PRK10619 86 QLRllrtrlTMVFQHFNLWSHMTVLENV--------------MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 155 ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFE---NTVIVVSHDRHFLNKVCTHMADLDFSKIK 231
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-210 |
7.83e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.96 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFP-DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG----PNERLATLK------ 70
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLESLRrqigvv 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 -QNHFDYEDyTVLETVIMGhkrlyevmkekdaiymKEDFSDEDGIRAAELegefAELDGWEAEpeaavLLQGLnipeelh 149
Cdd:COG1132 420 pQDTFLFSG-TIRENIRYG----------------RPDATDEEVEEAAKA----AQAHEFIEA-----LPDGY------- 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 150 DQKMSE----LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSinwleEFLI--NFEN-----TVIVVSH 210
Cdd:COG1132 467 DTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTET-----EALIqeALERlmkgrTTIVIAH 533
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-224 |
8.33e-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: 67.55 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM------GPNERLATLKQN--- 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkltDDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 ---HFD-YEDYTVLETVIMGhkrLYEVMKEKDAiymkedfsdedgiraaelegefaeldgwEAEPEAAVLLQ--GLnipE 146
Cdd:cd03262 81 vfqQFNlFPHLTVLENITLA---PIKVKGMSKA----------------------------EAEERALELLEkvGL---A 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFLNKVCTH-- 221
Cdd:cd03262 127 DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRvi 206
|
....
gi 488284819 222 -MAD 224
Cdd:cd03262 207 fMDD 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-211 |
1.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFpDRKL------FEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpNERLATLKQNHFD 75
Cdd:PRK13651 3 IKVKNIVKIF-NKKLptelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI----EWIFKDEKNKKKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 76 YEDYTVLETVIMGHKRLYEVMKEKD-----------AIY-MKEDFSDEDGIRAAELEGEFAEldgwEAEPEAAVLLQGLN 143
Cdd:PRK13651 78 KEKEKVLEKLVIQKTRFKKIKKIKEirrrvgvvfqfAEYqLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 144 IPEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSInwlEEFLINFEN------TVIVVSHD 211
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGV---KEILEIFDNlnkqgkTIILVTHD 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-523 |
1.12e-12 |
|
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: 67.74 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 335 LDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGvttsqAYLPKDNSKDFEEPLTI-------LDW--- 404
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPWKRRKKFLRRIGVvfgqktqLWWdlp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 405 -------LRQFAGKEEDDNTFLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITA 477
Cdd:cd03267 112 vidsfylLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488284819 478 LNDGLMAFT----GSILFASHDHQFIQTLANRIIavsdkgVIDRAETTYD 523
Cdd:cd03267 192 IRNFLKEYNrergTTVLLTSHYMKDIEALARRVL------VIDKGRLLYD 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
320-535 |
1.23e-12 |
|
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: 70.63 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVT--IDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWgvttsqaylpkdNSKDfee 397
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI------------DGID--- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 398 pltildwLRQFagkeedDNTFLRSFLG-----RMLFSG------------------EEVLKPVNV--------------- 439
Cdd:COG2274 539 -------LRQI------DPASLRRQIGvvlqdVFLFSGtirenitlgdpdatdeeiIEAARLAGLhdfiealpmgydtvv 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 440 ------LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLMAFTG--SILFASHDHQFIQtLANRIIaVSD 511
Cdd:COG2274 606 geggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIR-LADRII-VLD 683
|
250 260
....*....|....*....|....
gi 488284819 512 KGVIdRAETTYDEFLENPEIQKQM 535
Cdd:COG2274 684 KGRI-VEDGTHEELLARKGLYAEL 706
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-532 |
1.56e-12 |
|
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: 67.14 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSV--------------------RWG 379
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 380 VTTSQAYLPKDnskdfeepLTILD----WLRQ-FAGKEEDDNTFLRSFLGRMLFSGEEVLKPVNvLSGGEKVRVMLSKLM 454
Cdd:cd03261 81 MLFQSGALFDS--------LTVFEnvafPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 455 LSKANVLVLDDPTNHLD-------LESITALNDglmAFTGSILFASHDHQFIQTLANRIIAVSDKGVIdrAETTYDEFL- 526
Cdd:cd03261 152 ALDPELLLYDEPTAGLDpiasgviDDLIRSLKK---ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV--AEGTPEELRa 226
|
....*..
gi 488284819 527 -ENPEIQ 532
Cdd:cd03261 227 sDDPLVR 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-515 |
2.42e-12 |
|
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: 66.09 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVR-WGVTtsqaylPKDNSKDF--- 395
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKS------YQKNIEALrri 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 ----EEP-----LTILDWLRQFA-----GKEEDDNTflrsfLGRMLFSGEEVLKpVNVLSGGEKVRVMLSKLMLSKANVL 461
Cdd:cd03268 75 galiEAPgfypnLTARENLRLLArllgiRKKRIDEV-----LDVVGLKDSAKKK-VKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 462 VLDDPTNHLDLESITALND---GLMAFTGSILFASHDHQFIQTLANRiIAVSDKGVI 515
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADR-IGIINKGKL 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-210 |
2.75e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 13 DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM------GPNERLATLKQNH---FDYEDYTVLE 83
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDIRKKVglvFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 84 TVImghkrlyevmkEKDAIYMKEDFsdedGIRAAELEGEFAEldgweaepeaAVLLQGLNIpEELHDQKMSELTAGQKVK 163
Cdd:PRK13637 99 ETI-----------EKDIAFGPINL----GLSEEEIENRVKR----------AMNIVGLDY-EDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488284819 164 VLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSH 210
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGrdeiLNKIKELHKEYNMTIILVSH 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-472 |
3.29e-12 |
|
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: 68.70 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILS---------GEI----QPTTGvVSMGPNER-- 65
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIywsgSPLKA-SNIRDTERag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 66 LATLKQNHFDYEDYTVLETVIMGHK-RLYEVMKEKDAIYMKedfsdedgiraaelegefaeldgweaepeAAVLLQGLNI 144
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEiTLPGGRMAYNAMYLR-----------------------------AKNLLRELQL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 145 PEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSInwleEFLINfentvIVVSHDRHflNKVCTHMad 224
Cdd:TIGR02633 131 DADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKET----EILLD-----IIRDLKAH--GVACVYI-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 225 ldfskiklyvgnydfwlessqlatklqaqsnAKKEEQIKELQDFIARFSANASKSKQATSRKKMLDKITLDDIQPSSRRY 304
Cdd:TIGR02633 198 -------------------------------SHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREITSLY 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 305 PfvgfTPEREIGNDLLQVENVS---VTIDGKKILDNISFNLTKDD--KVAFIADSDIT--TTTLF---------KVIMGE 368
Cdd:TIGR02633 247 P----HEPHEIGDVILEARNLTcwdVINPHRKRVDDVSFSLRRGEilGVAGLVGAGRTelVQALFgaypgkfegNVFING 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 369 ITPDTGSVRWGVTTSQAYLPKDNSKDFEEPL------TILDWLRQFAGK----EEDDNTFLRSFLGRMLFSGEEVLKPVN 438
Cdd:TIGR02633 323 KPVDIRNPAQAIRAGIAMVPEDRKRHGIVPIlgvgknITLSVLKSFCFKmridAAAELQIIGSAIQRLKVKTASPFLPIG 402
|
490 500 510
....*....|....*....|....*....|....
gi 488284819 439 VLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDL 472
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-210 |
3.40e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFP---DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLkqNHFDYED 78
Cdd:TIGR00958 479 IEFQDVSFSYPnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLVQY--DHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVL---ETVIMGHKRlyevmkeKDAIYMKEDFSDEDGIRAAELEgefAELDGWEAEPEaavllQGLNIPEelhDQKMSE 155
Cdd:TIGR00958 556 QVALvgqEPVLFSGSV-------RENIAYGLTDTPDEEIMAAAKA---ANAHDFIMEFP-----NGYDTEV---GEKGSQ 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSH 210
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
3.54e-12 |
|
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: 65.57 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRK-----LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERL---------A 67
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYvsqepwiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 68 TLKQNhfdyedytvletvIMGHKRLYEVMkekdaiYmkedfsdEDGIRAAELEGEFAELDGweaepeaavllqGLNIpeE 147
Cdd:cd03250 81 TIREN-------------ILFGKPFDEER------Y-------EKVIKACALEPDLEILPD------------GDLT--E 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 148 LHDQKMSeLTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLIN----FENTVIVVSHDRHFLNKV 218
Cdd:cd03250 121 IGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILglllNNKTRILVTHQLQLLPHA 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-225 |
6.10e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 3 TVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN-----------ERLATLKQ 71
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NHFDYEDYTVLETVIMG----HKRLyevmkekdaiymkedfsdedgiraaeleGEFAELDgwEAEPEAAVLLQGLnipEE 147
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGrypwHGAL----------------------------GRFGAAD--REKVEEAISLVGL---KP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 148 LHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDtrsINWLEEFLINFEN-------TVIVVSHDRHFLNKVCT 220
Cdd:PRK10575 140 LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD---IAHQVDVLALVHRlsqerglTVIAVLHDINMAARYCD 216
|
....*
gi 488284819 221 HMADL 225
Cdd:PRK10575 217 YLVAL 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
320-509 |
6.30e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 68.08 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGK-KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQ----------AYL 387
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADadadswrdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 388 PKdnsKDFEEPLTILDWLRqFAGKEEDD------------NTFLRSfLGRMLfsGEEVLKPVNVLSGGEKVRVMLSKLML 455
Cdd:TIGR02857 402 PQ---HPFLFAGTIAENIR-LARPDASDaeirealeraglDEFVAA-LPQGL--DTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 456 SKANVLVLDDPTNHLDLESITALNDGLMAFTG--SILFASHDHQFIqTLANRIIAV 509
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
7.15e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 65.52 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNE-------RLATL----K-Q 71
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDltgldehEIARLgigrKfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NHFDYEDYTVLETVIM---GHKRLYEVMkekdaiymkedfsdedgiraaelegeFAELDGWEAEPEAAVL-LQGLnipEE 147
Cdd:COG4674 93 KPTVFEELTVFENLELalkGDRGVFASL--------------------------FARLTAEERDRIEEVLeTIGL---TD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 148 LHDQKMSELTAGQK----VKVLLAQslfgKPDVLLLDEPTNGLDTRSINWLEEFL--INFENTVIVVSHDRHF 214
Cdd:COG4674 144 KADRLAGLLSHGQKqwleIGMLLAQ----DPKLLLLDEPVAGMTDAETERTAELLksLAGKHSVVVVEHDMEF 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
7.60e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 66.66 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER-LATLKQ 71
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglpPEKRnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 nhfdyeDY------TVLETV-----IMGHKRlyevmKEKDAiymkedfsdedgiRAAELegefaeLDgweaepeaavlLQ 140
Cdd:COG3842 85 ------DYalfphlTVAENVafglrMRGVPK-----AEIRA-------------RVAEL------LE-----------LV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 141 GLnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT----------RSInwLEEFLInfenTVIVVSH 210
Cdd:COG3842 124 GL---EGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklreemreelRRL--QRELGI----TFIYVTH 194
|
..
gi 488284819 211 DR 212
Cdd:COG3842 195 DQ 196
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
8.28e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.92 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 11 FPDRKLFEeVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYEDYTVLETVIMGHK 90
Cdd:PRK13649 18 FEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 91 RLYEVMKEKDAIYMKEDF--SDEdgiraaelegefaeldgwEAEPEAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLAQ 168
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFgvSQE------------------EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAG 158
|
170
....*....|....*....
gi 488284819 169 SLFGKPDVLLLDEPTNGLD 187
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLD 177
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-230 |
9.16e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLK-------ILSGEIQpTTGVVSMGPN--ERLATLK- 70
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLI-VDGLKVNDPKvdERLIRQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 ----QNHFDYEDYTVLETVIMGHKRlyevmkekdaiymkedfsdedgIRAAELEgefaeldgwEAEPEAAVLLQGLNIPE 146
Cdd:PRK09493 80 gmvfQQFYLFPHLTALENVMFGPLR----------------------VRGASKE---------EAEKQARELLAKVGLAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 ELHDQKmSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD----------TRSInwLEEFLinfenTVIVVSHDRHFLN 216
Cdd:PRK09493 129 RAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpelrhevlkvMQDL--AEEGM-----TMVIVTHEIGFAE 200
|
250
....*....|....
gi 488284819 217 KVCTHMADLDFSKI 230
Cdd:PRK09493 201 KVASRLIFIDKGRI 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-210 |
9.60e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKqnhfdyEDYT 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRRQR------DEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 vLETVIMGHkrlyevmkeKDAIymKEDFSDEDGIR-AAELEGEFAELDGWEAepEAAVLLQG-LNIPeelhdqkMSELTA 158
Cdd:PRK13538 74 -QDLLYLGH---------QPGI--KTELTALENLRfYQRLHGPGDDEALWEA--LAQVGLAGfEDVP-------VRQLSA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEE-FLINFEN--TVIVVSH 210
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAlLAQHAEQggMVILTTH 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
1.02e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatLKQNH-FDYEDY 79
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV----------LWQGKpLDYSKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETvimgHKRLYEVMKEKDAIYMKEDFSDEDGIRAAEL---EGEFA-ELDgweaepEAAVLLQGlnipEELHDQKMSE 155
Cdd:PRK13638 71 GLLAL----RQQVATVFQDPEQQIFYTDIDSDIAFSLRNLgvpEAEITrRVD------EALTLVDA----QHFRHQPIQC 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD----TRSINWLEEfLINFENTVIVVSHD 211
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRR-IVAQGNHVIISSHD 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-216 |
1.09e-11 |
|
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: 64.35 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFP-DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNErLATLKQNHFDY---- 76
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGRAIPYlrrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 -----------EDYTVLETVIMGHKRLYEVMKEkdaiymkedfsdedgiraaelegefaeldgWEAEPEAAVLLQGLnip 145
Cdd:cd03292 80 igvvfqdfrllPDRNVYENVAFALEVTGVPPRE------------------------------IRKRVPAALELVGL--- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 146 EELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHDRHFLN 216
Cdd:cd03292 127 SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVD 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
1.72e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNErlatlkqnhfdyEDYT 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------------IDDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVI--MGHkrlyevmkeKDAiyMKEDFSDEDGIraaelegEF--AELDGWEAEPEAAVLLQGLNipeELHDQKMSEL 156
Cdd:PRK13539 70 DVAEAChyLGH---------RNA--MKPALTVAENL-------EFwaAFLGGEELDIAAALEAVGLA---PLAHLPFGYL 128
|
170 180 190
....*....|....*....|....*....|....*
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSI 191
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-209 |
2.38e-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: 63.44 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 5 NDVSLQFP----DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQP---TTGVVSMGPNERLATLKQNHFDY- 76
Cdd:cd03234 7 WDVGLKAKnwnkYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 --EDY-----TVLETV-IMGHKRLYEVMKEKdaiymkedfsdedgIRAAElegefaeldgweaepEAAVLLQGLNIpEEL 148
Cdd:cd03234 87 rqDDIllpglTVRETLtYTAILRLPRKSSDA--------------IRKKR---------------VEDVLLRDLAL-TRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 149 HDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVS 209
Cdd:cd03234 137 GGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILT 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-230 |
2.50e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 5 NDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV-----------SMGPNERLATLKQNH 73
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 FDYEDYTVLETVIMG---HKRLYEVMKEKDaiymkedfsdEDGIRAAelegefaeldgweaepeaavlLQGLNIpEELHD 150
Cdd:PRK10253 91 TTPGDITVQELVARGrypHQPLFTRWRKED----------EEAVTKA---------------------MQATGI-THLAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 151 QKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD-TRSINWLEEFL-INFEN--TVIVVSHDrhfLNKVC---THMA 223
Cdd:PRK10253 139 QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLELLSeLNREKgyTLAAVLHD---LNQACryaSHLI 215
|
....*..
gi 488284819 224 DLDFSKI 230
Cdd:PRK10253 216 ALREGKI 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-211 |
2.84e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 15 KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGV-------VSMGPNERLATLKQNHFDY--EDYTVLETV 85
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALAQLRREHFGFifQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 86 IMGHKrlyevmKEKDAIYMkedfsdedGI-RAAELEgefaeldgweaepEAAVLLQGLNIPEELHDQKmSELTAGQKVKV 164
Cdd:PRK10535 102 TAAQN------VEVPAVYA--------GLeRKQRLL-------------RAQELLQRLGLEDRVEYQP-SQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488284819 165 LLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEfLINFENTVIVVSHD 211
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSgeevMAILHQ-LRDRGHTVIIVTHD 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-198 |
3.49e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 21 NIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGvvsmgpnERlatlkQNHFDYEDYTVLETVimgHKRLYEVMKEKD 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG-------ER-----QSQFSHITRLSFEQL---QKLVSDEWQRNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 101 AIYMKEDfSDEDGIRAAELEgefaeLDGWEAEPEAAVLLQGLNIpEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLD 180
Cdd:PRK10938 88 TDMLSPG-EDDTGRTTAEII-----QDEVKDPARCEQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170
....*....|....*...
gi 488284819 181 EPTNGLDTRSINWLEEFL 198
Cdd:PRK10938 161 EPFDGLDVASRQQLAELL 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-210 |
3.89e-11 |
|
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: 62.87 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 12 PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpNERLATLKQNHFDYEDYTVL--ETVIMGH 89
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL--DGKPISQYEHKYLHSKVSLVgqEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 90 KRlyevmkeKDAI-YMKEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVllqglnipeelhDQKMSELTAGQKVKVLLAQ 168
Cdd:cd03248 103 SL-------QDNIaYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEV------------GEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488284819 169 SLFGKPDVLLLDEPTNGLDTRSINWLEEFLI--NFENTVIVVSH 210
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAH 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
4.33e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLfeEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER-LATLKQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdltalpPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NH--FDYedYTVLETVIMG-HKRLyevmkekdaiymkeDFSDEDGIRAAElegefaeldgweaepeaavLLQGLNIpEEL 148
Cdd:COG3840 79 ENnlFPH--LTVAQNIGLGlRPGL--------------KLTAEQRAQVEQ-------------------ALERVGL-AGL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 149 HDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT--RS--INWLEEFLINFENTVIVVSHD 211
Cdd:COG3840 123 LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalRQemLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-191 |
4.84e-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: 62.95 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnHFDYEDYTV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI--------------LLDGQDITK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 LETvimgHKRlyevmKEKDAIYMKED---FSD---EDGIRAAElegEFAELDGWEAEPEAAVLLQGLNIpEELHDQKMSE 155
Cdd:cd03218 67 LPM----HKR-----ARLGIGYLPQEasiFRKltvEENILAVL---EIRGLSKKEREEKLEELLEEFHI-THLRKSKASS 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSI 191
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
4.86e-11 |
|
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: 65.53 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFP-DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGP----NERLATLKQ--NHF 74
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkDIDRHTLRQfiNYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 75 DYEDY----TVLETVIMGHKrlyevmkekdaiymkEDFSDEDGIRAAElegeFAELDgweAEPEAAVLLQGLNIPEElhd 150
Cdd:TIGR01193 554 PQEPYifsgSILENLLLGAK---------------ENVSQDEIWAACE----IAEIK---DDIENMPLGYQTELSEE--- 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 151 qkMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF-ENTVIVVSH 210
Cdd:TIGR01193 609 --GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLqDKTIIFVAH 667
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
6.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGeiqpttgVVSMGPNERLAtlKQNHFDYEDYTV 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNR-------LIELYPEARVS--GEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 LEtVIMGHKRLYEVMKEKDAIYMKEDFSDED-GIRAAELEGEFAELdgweaEPEAAVLLQGLNIPEELHDQ---KMSELT 157
Cdd:PRK14247 75 MD-VIELRRRVQMVFQIPNPIPNLSIFENVAlGLKLNRLVKSKKEL-----QERVRWALEKAQLWDEVKDRldaPAGKLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSH 210
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-196 |
6.07e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.13 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 14 RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM--GPNERLATLKQNHFDYedytvletviMGHkr 91
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLngGPLDFQRDSIARGLLY----------LGH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 92 lyevmkekdAIYMKEDFSDEDGIRaaelegeFAELDGWEAEPEAAVLLQGLNipeELHDQKMSELTAGQKVKVLLAQSLF 171
Cdd:cd03231 81 ---------APGIKTTLSVLENLR-------FWHADHSDEQVEEALARVGLN---GFEDRPVAQLSAGQQRRVALARLLL 141
|
170 180
....*....|....*....|....*
gi 488284819 172 GKPDVLLLDEPTNGLDTRSINWLEE 196
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAE 166
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-189 |
6.09e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 14 RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEI--QPTTGVVSmgpnerlatLKQNHFdYEDYTVLetvimghkr 91
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVD---------VPDNQF-GREASLI--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 92 lyevmkekDAIYMKEDFSDedgirAAELegefaeLdgweaepeAAVllqGLNIPeELHDQKMSELTAGQKVKVLLAQSLF 171
Cdd:COG2401 104 --------DAIGRKGDFKD-----AVEL------L--------NAV---GLSDA-VLWLRRFKELSTGQKFRFRLALLLA 152
|
170
....*....|....*...
gi 488284819 172 GKPDVLLLDEPTNGLDTR 189
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQ 170
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-211 |
6.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 13 DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnhfDYEDYTVleTVIMGHKRL 92
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI----------------TIAGYHI--TPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 93 YEVMKEKDAIYmkeDFSDEDGIRAAELEG-EFAELD-GW---EAEPEAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLA 167
Cdd:PRK13641 81 KKLRKKVSLVF---QFPEAQLFENTVLKDvEFGPKNfGFsedEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488284819 168 QSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFE---NTVIVVSHD 211
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHN 204
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-495 |
6.64e-11 |
|
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: 62.91 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQ--------AYLP 388
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgvdLHGLSrrararrvALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 389 KDNskDFEEPLTILD--------WLRQFAGKEEDDNTFLRSFLGRMlfsGEEVL--KPVNVLSGGEKVRVMLSKLMLSKA 458
Cdd:TIGR03873 82 QDS--DTAVPLTVRDvvalgripHRSLWAGDSPHDAAVVDRALART---ELSHLadRDMSTLSGGERQRVHVARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488284819 459 NVLVLDDPTNHLD----LESITALNDgLMAFTGSILFASHD 495
Cdd:TIGR03873 157 KLLLLDEPTNHLDvraqLETLALVRE-LAATGVTVVAALHD 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-210 |
7.53e-11 |
|
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: 62.17 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDR---KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM-GPNERLATLKQ--NHFD 75
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 76 Y---E----DYTVLETVIMGhkrlyevmkekdaiymKEDFSDEDGIRAAELEG--EFAEldgweaepeaavllqglNIPE 146
Cdd:cd03249 81 LvsqEpvlfDGTIAENIRYG----------------KPDATDEEVEEAAKKANihDFIM-----------------SLPD 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 147 ELHDQ---KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSH 210
Cdd:cd03249 128 GYDTLvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-211 |
8.30e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 5 NDVSLQFPDRKLFEEV--NIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTG-VVSMGP--------------NER 65
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVlhNVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFNGQpmsklssaakaelrNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 66 LATLKQNHFDYEDYTVLETVIM----GHKRLYEVMKekdaiymkedfsdedgiRAAELEgefaeldgweaepeAAVllqG 141
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMplliGKKKPAEINS-----------------RALEML--------------AAV---G 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 142 LnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFEN--TVIVVSHD 211
Cdd:PRK11629 135 L---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgeLNRLQgtAFLVVTHD 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-212 |
8.61e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 18 EEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV--------SMGPNER-LATLKQNHFDYEDYTVLETVIMG 88
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRpINMMFQSYALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 89 HKrlyevmkekdaiymkedfsdEDGIRAAELEGEFAELdgweaepEAAVLLQglnipeELHDQKMSELTAGQKVKVLLAQ 168
Cdd:PRK11607 116 LK--------------------QDKLPKAEIASRVNEM-------LGLVHMQ------EFAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488284819 169 SLFGKPDVLLLDEPTNGLDT--RSINWLE--EFLINFENTVIVVSHDR 212
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKklRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-210 |
9.37e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 5 NDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNER------------LATLKQN 72
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaagVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHkrlyevmkekdaiymkedfsdedgiraaeLEGEFAELDGWEAEPEAAVLLQGLNI---Peelh 149
Cdd:PRK11288 88 LHLVPEMTVAENLYLGQ-----------------------------LPHKGGIVNRRLLNYEAREQLEHLGVdidP---- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLeeF-LIN---FENTVIV-VSH 210
Cdd:PRK11288 135 DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL--FrVIRelrAEGRVILyVSH 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
9.61e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 64.30 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNH------F 74
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEvrrrvsV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 75 DYEDYTVLETVIMGHKRLyevmkekdaiyMKEDFSDEDGIRAAELEGefaeLDGWEAEpeaavLLQGLNIPEELHDQKMS 154
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRL-----------ARPDATDEELWAALERVG----LADWLRA-----LPDGLDTVLGEGGARLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 155 eltAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSHD 211
Cdd:TIGR02868 474 ---GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-191 |
9.93e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.28 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFP-DRKLFE---EVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNErLAT 68
Cdd:PRK11153 1 MIELKNISKVFPqGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGrvlvdgqdLTALSEKE-LRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 69 LKQN------HFDY-EDYTVLETVimghkrlyevmkekdaiymkedfsdedgirAAELEgefaeLDGW-EAEPEAAV--L 138
Cdd:PRK11153 80 ARRQigmifqHFNLlSSRTVFDNV------------------------------ALPLE-----LAGTpKAEIKARVteL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 139 LQ--GLnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSI 191
Cdd:PRK11153 125 LElvGL---SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSI 179
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-523 |
1.21e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.65 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 317 NDLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLP----KDNS 392
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 393 KDFEEPL----TILDWLR---QFAGKEEDDNTFLRsFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDD 465
Cdd:PRK10247 85 YCAQTPTlfgdTVYDNLIfpwQIRNQQPDPAIFLD-DLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 466 PTNHLDLESITALNDGLMAFTG----SILFASHDHQFIQTlANRIIAVSDKGViDRAETTYD 523
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVReqniAVLWVTHDKDEINH-ADKVITLQPHAG-EMQEARYE 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-211 |
1.36e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNdVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPnerLATLKQNHFDYEDyt 80
Cdd:PRK14271 22 MAAVN-LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGD---VLLGGRSIFNYRD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETvimgHKRLYEVMKEKDAIYMKEDFSDEDGIRAAEL----------EGEFAELDGWEAepeaavllqglnIPEELHD 150
Cdd:PRK14271 96 VLEF----RRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLvprkefrgvaQARLTEVGLWDA------------VKDRLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 151 QKMsELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSHD 211
Cdd:PRK14271 160 SPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-211 |
1.45e-10 |
|
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: 61.66 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 24 FTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG-------VVSMGPNERLAtlkqnhfdyeDYTVletvimghkRLYEVM 96
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldTVSYKPQYIKA----------DYEG---------TVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 97 KEKDAIYMKEDFsdedgiraaelegefaeldgWEAEpeaavLLQGLNIpEELHDQKMSELTAGQKVKVLLAQSLFGKPDV 176
Cdd:cd03237 83 SSITKDFYTHPY--------------------FKTE-----IAKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488284819 177 LLLDEPTNGLD-------TRSINwleEFLINFENTVIVVSHD 211
Cdd:cd03237 137 YLLDEPSAYLDveqrlmaSKVIR---RFAENNEKTAFVVEHD 175
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-507 |
1.57e-10 |
|
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: 60.76 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW---GVTTSQ----AYLPKDns 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkPLDIAArnriGYLPEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 393 KDFEEPLTILDWLRQFAG----KEEDDNTFLRSFLGRMLFSGEEvLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTN 468
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQlkglKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488284819 469 HLDLESITALNDGLMAFTG---SILFASHDHQFIQTLANRII 507
Cdd:cd03269 158 GLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVL 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-494 |
1.64e-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: 60.58 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW----------GVTTSQAYLPK 389
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfqrdSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 DNSkdFEEPLTILDWLRQFAGKEEDDNTFlrSFLGRMLFSGEEVLkPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNH 469
Cdd:cd03231 81 APG--IKTTLSVLENLRFWHADHSDEQVE--EALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 488284819 470 LDLESITALNDGLMAFT---GSILFASH 494
Cdd:cd03231 156 LDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-186 |
1.85e-10 |
|
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: 60.91 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 20 VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER----LATLKQNHFDYEDYTVLETVIM 87
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpPHERaragIGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 88 GhkrlyevmkekdaIYMKEDFSDEDGIraAELEGEFAELdgweaepeaavllqglnipEELHDQKMSELTAGQKVKVLLA 167
Cdd:cd03224 99 G-------------AYARRRAKRKARL--ERVYELFPRL-------------------KERRKQLAGTLSGGEQQMLAIA 144
|
170
....*....|....*....
gi 488284819 168 QSLFGKPDVLLLDEPTNGL 186
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGL 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-211 |
3.13e-10 |
|
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: 60.78 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnHFDYEDYT 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI--------------FIDGEDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRLYeVMKEkdaIYMKEDFSDEDGIraaeleGEFAELDGWEAE---PEAAVLLQGLNI-PEELHDQKMSEL 156
Cdd:cd03295 67 EQDPVELRRKIGY-VIQQ---IGLFPHMTVEENI------ALVPKLLKWPKEkirERADELLALVGLdPAEFADRYPHEL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD--TRSiNWLEEFL-INFE--NTVIVVSHD 211
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDpiTRD-QLQEEFKrLQQElgKTIVFVTHD 195
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-219 |
3.32e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNErlatlkQNHFDYEDYT 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN------YNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVImghkrlyevmkekdaIYMKEDFSDEDGIraaeLEGEFAE------------LDGWEAEPEAAVLLQGLNIPEEL 148
Cdd:PRK09700 79 QLGIGI---------------IYQELSVIDELTV----LENLYIGrhltkkvcgvniIDWREMRVRAAMMLLRVGLKVDL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 149 hDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLeeFLI----NFENTVIV-VSHDRHFLNKVC 219
Cdd:PRK09700 140 -DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLImnqlRKEGTAIVyISHKLAEIRRIC 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-210 |
5.66e-10 |
|
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: 62.34 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 14 RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN----------ERLATLKQNHFDYEDYTVLE 83
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 84 tvimgHKRLYevmkekdaiymkedfsdedgiraAELEGEFAEldgwEAEPEAAVLLQGLNIPEElHDQKMSELTAGQKVK 163
Cdd:TIGR01257 1023 -----HILFY-----------------------AQLKGRSWE----EAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRK 1069
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488284819 164 VLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSH 210
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTH 1118
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-211 |
6.71e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 26 PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM-GPN------ERLATLKQNH--FDYEDYTVLETVimghkrlyevm 96
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPlhqmdeEARAKLRAKHvgFVFQSFMLIPTL----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 97 kekDAIymkedfsdEDGIRAAELEGEFAEldgwEAEPEAAVLLQGLNIPEELHDQKmSELTAGQKVKVLLAQSLFGKPDV 176
Cdd:PRK10584 104 ---NAL--------ENVELPALLRGESSR----QSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 488284819 177 LLLDEPTNGLDTRSINWLEEFLI----NFENTVIVVSHD 211
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFslnrEHGTTLILVTHD 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
8.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.71 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlaTLKQNHFDYEDy 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV---------LIKGEPIKYDK- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 tvletvimghKRLYEVMKEKDAIYMKEDfsdeDGIRAAELEGEFA------ELDGWEAEPEAAVLLQGLNIpEELHDQKM 153
Cdd:PRK13639 71 ----------KSLLEVRKTVGIVFQNPD----DQLFAPTVEEDVAfgplnlGLSKEEVEKRVKEALKAVGM-EGFENKPP 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 154 SELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHD 211
Cdd:PRK13639 136 HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-210 |
1.17e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.78 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD--RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM-GPNERLATLKQ--NHFDY 76
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 edytVLETVIMGHKRLYEvmkekDAIYMKEDFSDEDGIRAAELEG--EFAEldgweaepeaavllqglNIPEELHD---Q 151
Cdd:cd03251 81 ----VSQDVFLFNDTVAE-----NIAYGRPGATREEVEEAARAANahEFIM-----------------ELPEGYDTvigE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 152 KMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINfeNTVIVVSH 210
Cdd:cd03251 135 RGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKN--RTTFVIAH 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-471 |
1.28e-09 |
|
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: 57.71 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDG--KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYlpkdnSKDFEE 397
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-----EKALSS 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 398 PLTILDwlrQ----FagkeeddNTFLRSFLGRMLfsgeevlkpvnvlSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD 471
Cdd:cd03247 76 LISVLN---QrpylF-------DTTLRNNLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-513 |
1.30e-09 |
|
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: 58.36 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTkDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQ---------AYLPK 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKqpqklrrriGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 DNS--KDF--EEPLTILDWLRQFAGKEED---DNTFLRSFLGrmlfsgEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLV 462
Cdd:cd03264 80 EFGvyPNFtvREFLDYIAWLKGIPSKEVKarvDEVLELVNLG------DRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488284819 463 LDDPTNHLDLESITALNDGL--MAFTGSILFASHDHQFIQTLANRiIAVSDKG 513
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLseLGEDRIVILSTHIVEDVESLCNQ-VAVLNKG 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-226 |
1.37e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.57 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 5 NDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsMGPNERLATLKQNHFDYE-DYTVLE 83
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEGEDISTLKPEIYRQQvSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 84 TVIMGhkrlyevmkekDAIYMKEDFSDEdgIRaaelegefaeldgwEAEPEAAVLLQGL---NIPEELHDQKMSELTAGQ 160
Cdd:PRK10247 90 PTLFG-----------DTVYDNLIFPWQ--IR--------------NQQPDPAIFLDDLerfALPDTILTKNIAELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 161 KVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSINWLEEFLINFEN-TVIVVSHDRHFLN---KVCT---HMADLD 226
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDesnKHNVNEIIHRYVREQNiAVLWVTHDKDEINhadKVITlqpHAGEMQ 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-211 |
1.92e-09 |
|
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: 58.53 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 26 PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN------ERLATLKQNHFDyedyTVLE-TVIMGHKRLY----- 93
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdeildEFRGSELQNYFT----KLLEgDVKVIVKPQYvdlip 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 94 --------EVMKEKDAIYMKEDFsdedgIRAAELEGefaeldgweaepeaavllqglnipeeLHDQKMSELTAGQKVKVL 165
Cdd:cd03236 101 kavkgkvgELLKKKDERGKLDEL-----VDQLELRH--------------------------VLDRNIDQLSGGELQRVA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488284819 166 LAQSLFGKPDVLLLDEPTNGLDTR---SINWLEEFLINFENTVIVVSHD 211
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-211 |
2.02e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM-GPN-------------ERL 66
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENipamsrsrlytvrKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 67 ATLKQNHFDYEDYTVLETV---IMGHKRLYEVMKeKDAIYMKedfsdedgIRAAELEGefaeldgweaepeAAVLLQgln 143
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVaypLREHTQLPAPLL-HSTVMMK--------LEAVGLRG-------------AAKLMP--- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 144 ipeelhdqkmSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEfLINFEN-----TVIVVSHD 211
Cdd:PRK11831 142 ----------SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK-LISELNsalgvTCVVVSHD 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-495 |
2.15e-09 |
|
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: 60.07 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKI-LDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKDF--- 395
Cdd:TIGR02868 335 LELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVsvc 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 -EEP----LTILDWLRqFAGKEEDDNTFLRSF----LGRMLFSGEEVLKPV-----NVLSGGEKVRVMLSKLMLSKANVL 461
Cdd:TIGR02868 415 aQDAhlfdTTVRENLR-LARPDATDEELWAALervgLADWLRALPDGLDTVlgeggARLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 488284819 462 VLDDPTNHLDLES----ITALNDGLMAFTgsILFASHD 495
Cdd:TIGR02868 494 LLDEPTEHLDAETadelLEDLLAALSGRT--VVLITHH 529
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
2.30e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNE--RL-ATLKQNHFDYED 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvsRLhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 Y------TVLETVIMG------HKRLyevmkEKDAIYMKedfsdedgiraaelegefaeldgweaepeAAVLLQGLNIpE 146
Cdd:PRK10851 83 YalfrhmTVFDNIAFGltvlprRERP-----NAAAIKAK-----------------------------VTQLLEMVQL-A 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT------RSinWLEEFLINFENTVIVVSHDR 212
Cdd:PRK10851 128 HLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkelRR--WLRQLHEELKFTSVFVTHDQ 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
2.34e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV-----------SMGPNERLATL 69
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNH--FDYEDY------TVLETVIMGhkrlyevmkekdAIYMKEDFSDEDGIRAAELEgefaeldgweaepeAAVllqG 141
Cdd:PRK11264 83 LRQHvgFVFQNFnlfphrTVLENIIEG------------PVIVKGEPKEEATARARELL--------------AKV---G 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 142 LNIPEELHDQKMSeltAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTR-------SINWLEEflinfEN-TVIVVSHDRH 213
Cdd:PRK11264 134 LAGKETSYPRRLS---GGQQQRVAIARALAMRPEVILFDEPTSALDPElvgevlnTIRQLAQ-----EKrTMVIVTHEMS 205
|
....*
gi 488284819 214 FLNKV 218
Cdd:PRK11264 206 FARDV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-515 |
2.39e-09 |
|
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: 57.50 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKK----ILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQAylpKDNSKD 394
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDISKL---SEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 395 ----------FEEP-----LTILDWLR---QFAGKE-EDDNTFLRSFLGRM-LfsGEEVLKPVNVLSGGEKVRVMLSKLM 454
Cdd:cd03255 78 afrrrhigfvFQSFnllpdLTALENVElplLLAGVPkKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 455 LSKANVLVLDDPTNHLDLES-------ITALNDglmAFTGSILFASHDHQFIQtLANRIIAVSDkGVI 515
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETgkevmelLRELNK---EAGTTIVVVTHDPELAE-YADRIIELRD-GKI 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-186 |
2.87e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhFDYEDYT 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV--------------FDGKDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVimghkrlyEVMKEKDAIYM--KEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLqglnIPE--ELHDQKMSEL 156
Cdd:PRK11614 71 DWQTA--------KIMREAVAIVPegRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYEL----FPRlhERRIQRAGTM 138
|
170 180 190
....*....|....*....|....*....|
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGL 186
Cdd:PRK11614 139 SGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
3.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFE-----EVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpnerlatlkqnhfDY 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG-------------DY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 EdytvletVIMGHKRLYEVMKEKDAIYMKEDFSD----EDGIraaELEGEFAEL----DGWEAEPEAAVLLQGLNIPEEL 148
Cdd:PRK13645 74 A-------IPANLKKIKEVKRLRKEIGLVFQFPEyqlfQETI---EKDIAFGPVnlgeNKQEAYKKVPELLKLVQLPEDY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 149 HDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:PRK13645 144 VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHN 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
3.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.69 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLF--EEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhfdyed 78
Cdd:PRK13632 7 MIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 ytvLETVIMGHKRLYEVMKEKDAIYMKED-----FSDEDGIrAAELEGEfaELDGWEAEPEAAVLLQGLNIpEELHDQKM 153
Cdd:PRK13632 68 ---IDGITISKENLKEIRKKIGIIFQNPDnqfigATVEDDI-AFGLENK--KVPPKKMKDIIDDLAKKVGM-EDYLDKEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 154 SELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSHD 211
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-210 |
4.82e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGE-IQPTTGVVSM-----GPNERLATLKQN--- 72
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGYSNDLTLfgrrrGSGETIWDIKKHigy 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 -----HFDYEDYTVLETVIM-GHKrlyevmkekDAIYMKEDFSDEDGIRAAElegefaeldgWeaepeaavlLQGLNIPE 146
Cdd:PRK10938 341 vssslHLDYRVSTSVRNVILsGFF---------DSIGIYQAVSDRQQKLAQQ----------W---------LDILGIDK 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 147 ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTrsIN------WLEEFLINFENTVIVVSH 210
Cdd:PRK10938 393 RTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP--LNrqlvrrFVDVLISEGETQLLFVSH 460
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-530 |
5.33e-09 |
|
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: 56.68 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFI----ADSdittTTLFKVIMGEITPDTGSVRWG---VTTsqayLPKD-- 390
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIgpngAGK----TTLFNLISGFLRPTSGSVLFDgedITG----LPPHei 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 391 ----------NSKDFEEpLTILDWLR---QFAGKEEDDNTFLRSFLGRMLFSGEEVLK----------PVNVLSGGEKVR 447
Cdd:cd03219 73 arlgigrtfqIPRLFPE-LTVLENVMvaaQARTGSGLLLARARREEREARERAEELLErvgladladrPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 448 VMLSKLMLSKANVLVLDDPT---NHLDLESITALNDGLMAFTGSILFASHDHQFIQTLANRIIaVSDKG-VIdrAETTYD 523
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT-VLDQGrVI--AEGTPD 228
|
....*..
gi 488284819 524 EFLENPE 530
Cdd:cd03219 229 EVRNNPR 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-511 |
5.74e-09 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 56.26 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 335 LDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQ------AYLPKDNSKDFEEPLTILDW--- 404
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVSDlrgraiPYLRRKIGVVFQDFRLLPDRnvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 405 ------LRQFAGKEEDDNTFLRSFLGRMLFSGEEVLKPvNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITAL 478
Cdd:cd03292 97 envafaLEVTGVPPREIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 488284819 479 NDGLMAFT---GSILFASHDHQFIQTLANRIIAVSD 511
Cdd:cd03292 176 MNLLKKINkagTTVVVATHAKELVDTTRHRVIALER 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
7.82e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.54 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG-------PNERLATLK--- 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglPGHQIARMGvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 --QNHFDYEDYTVLETVIMGHKRlyevmkekdaiYMKEDFsdedgiraaeLEGEFAELDGWEAEPE----AAVLLQGLNI 144
Cdd:PRK11300 85 tfQHVRLFREMTVIENLLVAQHQ-----------QLKTGL----------FSGLLKTPAFRRAESEaldrAATWLERVGL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 145 pEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSHD 211
Cdd:PRK11300 144 -LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehnvTVLLIEHD 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-472 |
8.02e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVR-----------WGVTTSQAYL 387
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 388 PKDNSKDFeePLTILDWLRqfagkeeddntflrsfLGRMLFSG---------EEVLKPVNV----------LSGGEKVRV 448
Cdd:PRK13548 82 PQHSSLSF--PFTVEEVVA----------------MGRAPHGLsraeddalvAAALAQVDLahlagrdypqLSGGEQQRV 143
|
170 180 190
....*....|....*....|....*....|
gi 488284819 449 MLSKLM--LSKAN----VLVLDDPTNHLDL 472
Cdd:PRK13548 144 QLARVLaqLWEPDgpprWLLLDEPTSALDL 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
9.47e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.22 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQnhfdyedytv 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEARE---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 lETVIMGHK-RLyevMKEKDAIymkedfsDEDGIraaELEGEfaeldgWEAEPEAAVLLQGLnipEELHDQKMSELTAGQ 160
Cdd:PRK11247 82 -DTRLMFQDaRL---LPWKKVI-------DNVGL---GLKGQ------WRDAALQALAAVGL---ADRANEWPAALSGGQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 161 KVKVLLAQSLFGKPDVLLLDEPTNGLD--TRsIN--------WLEEfliNFenTVIVVSHD 211
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDalTR-IEmqdlieslWQQH---GF--TVLLVTHD 193
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-515 |
1.03e-08 |
|
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: 55.59 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVT--IDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSV---RWGVTTSQA-------YL 387
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyinGYSIRTDRKaarqslgYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 388 PKDNSKdFEEpLTILDWLRQFA---GKEEDDNTFLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLD 464
Cdd:cd03263 81 PQFDAL-FDE-LTVREHLRFYArlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488284819 465 DPTNHLDLESITALNDGLMAFTG--SILFASHDHQFIQTLANRIIAVSDKGVI 515
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-221 |
1.05e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.18 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 16 LFEeVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM---------GPNER-LATLKQN------------H 73
Cdd:PRK11124 18 LFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfskTPSDKaIRELRRNvgmvfqqynlwpH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 FdyedyTVLETVIMGHKRLYEVMKEkdaiymkedfsdedgiraaelegefaeldgwEAEPEAAVLLQGLNIpEELHDQKM 153
Cdd:PRK11124 97 L-----TVQQNLIEAPCRVLGLSKD-------------------------------QALARAEKLLERLRL-KPYADRFP 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 154 SELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD-------TRSINWLEEFLInfenTVIVVSHDRHFLNKVCTH 221
Cdd:PRK11124 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI----TQVIVTHEVEVARKTASR 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-210 |
1.08e-08 |
|
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: 56.08 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQF-PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLATLKQNHF------ 74
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLrraigv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 75 ---DyedyTVL--ETVimghkrLYEVMkekdaiYMKEDFSDEDGIRAAELegefaeldgweAEPEAAVllqgLNIPEElH 149
Cdd:cd03253 80 vpqD----TVLfnDTI------GYNIR------YGRPDATDEEVIEAAKA-----------AQIHDKI----MRFPDG-Y 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 150 DQKMSE----LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT---RSInwLEEFLINFEN-TVIVVSH 210
Cdd:cd03253 128 DTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDThteREI--QAALRDVSKGrTTIVIAH 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-210 |
1.20e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.96 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQF-PD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNErLATLKQNHFDYEDY 79
Cdd:cd03252 1 ITFEHVRFRYkPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD-LALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVIMGHKRLYEVMKEKDaiymkEDFSDEDGIRAAELEGEFAELdgweaepeaavllqgLNIPEElHDQKMSE---- 155
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALAD-----PGMSMERVIEAAKLAGAHDFI---------------SELPEG-YDTIVGEqgag 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFENTVIVVSH 210
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMhdICAGRTVIIIAH 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
317-537 |
1.27e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.28 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 317 NDLLQVENVSVTI-DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVR-WGVTTSQAYLPKDNSKD 394
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 395 ---FEEPLTILdwlrqFAGKEEDDNTFLRSFLG----RMLFSGEEVLKPVNV----------LSGGEKVRVMLSKLMLSK 457
Cdd:PRK13647 82 glvFQDPDDQV-----FSSTVWDDVAFGPVNMGldkdEVERRVEEALKAVRMwdfrdkppyhLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 458 ANVLVLDDPTNHLD---LESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSDKGVIDRAETtydEFLENPEIQKQ 534
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK---SLLTDEDIVEQ 233
|
...
gi 488284819 535 MDI 537
Cdd:PRK13647 234 AGL 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
318-515 |
1.33e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 318 DLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEI--TPDTGSVRwgvttsqayLPKDnskDF 395
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVD---------VPDN---QF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 EEPLTILDWLrqfaGKEEDDNTFLRsFLGRM-LFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLES 474
Cdd:COG2401 97 GREASLIDAI----GRKGDFKDAVE-LLNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488284819 475 --ITALNDGLMA--FTGSILFASHDHQFIQTLA-NRIIAVSDKGVI 515
Cdd:COG2401 172 akRVARNLQKLArrAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-190 |
1.50e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 6 DVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIqpTTGVVSMGpnERLAT--------------LKQ 71
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGG--DRLVNgrpldssfqrsigyVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 72 NHFDYEDYTVLETVIMGhkrLYEVMKEKDAIYMKEDFSDEDgIRAAELEgEFAeldgweaepEAAVLL--QGLNIPeelh 149
Cdd:TIGR00956 844 QDLHLPTSTVRESLRFS---AYLRQPKSVSKSEKMEYVEEV-IKLLEME-SYA---------DAVVGVpgEGLNVE---- 905
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488284819 150 dqkmseltagQKVKVLLAQSLFGKPDVLL-LDEPTNGLDTRS 190
Cdd:TIGR00956 906 ----------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-515 |
1.53e-08 |
|
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: 55.22 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQAYLpKDNSKDFE 396
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdVTGVPPER-RNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 397 EP-----LTILD----WLRQFAGKEEDDNTFLRSFLGRMLFSGEEVLKPvNVLSGGEKVRVMLSKLMLSKANVLVLDDPT 467
Cdd:cd03259 80 DYalfphLTVAEniafGLKLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488284819 468 NHLDLESITALND---GLMAFTG-SILFASHDHQFIQTLANRiIAVSDKGVI 515
Cdd:cd03259 159 SALDAKLREELREelkELQRELGiTTIYVTHDQEEALALADR-IAVMNEGRI 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.58e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.01 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpNERLatlkqnhfdyeDY 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-GKPI-----------DY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TvletvimgHKRLYEVMKEKDAIYMKED---FSDE--DGIRAAELEGEFAElDGWEAEPEAAVLLQGLnipEELHDQKMS 154
Cdd:PRK13636 73 S--------RKGLMKLRESVGMVFQDPDnqlFSASvyQDVSFGAVNLKLPE-DEVRKRVDNALKRTGI---EHLKDKPTH 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 155 ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSHD 211
Cdd:PRK13636 141 CLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHD 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-471 |
1.59e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 11 FPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNER----LATLKQNHFDYED 78
Cdd:PRK10762 14 FPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkeVTFNGPKSSqeagIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVLETVIMGHkrlyevmkekdaiymkedfsdedgiraaELEGEFAELDGWEAEPEAAVLLQGLNIPEELHdQKMSELTA 158
Cdd:PRK10762 94 LTIAENIFLGR----------------------------EFVNRFGRIDWKKMYAEADKLLARLNLRFSSD-KLVGELSI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGL-DT------RSINWLEEflinfENTVIV-VSHDRHFLNKVC---THMADLDF 227
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPTDALtDTeteslfRVIRELKS-----QGRGIVyISHRLKEIFEICddvTVFRDGQF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 228 skiklyVGNYDFwlesSQLatklqaqsnakKEEQIKELQdfiarfsanaskskqaTSRKkmldkitLDDiqpssrRYPFV 307
Cdd:PRK10762 220 ------IAEREV----ADL-----------TEDSLIEMM----------------VGRK-------LED------QYPRL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 308 gftpEREIGNDLLQVENVSvtidGKKIlDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW--------- 378
Cdd:PRK10762 250 ----DKAPGEVRLKVDNLS----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdghevvtrs 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 379 ---GVTTSQAYLPKDNSKD-------FEE--PLTILDWLRQFAG--KEEDDNTFLRSFLgrMLF-----SGEevlKPVNV 439
Cdd:PRK10762 321 pqdGLANGIVYISEDRKRDglvlgmsVKEnmSLTALRYFSRAGGslKHADEQQAVSDFI--RLFniktpSME---QAIGL 395
|
490 500 510
....*....|....*....|....*....|..
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD 471
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-219 |
1.61e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQN-------- 72
Cdd:PRK15056 7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlvayvpqs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 -HFDYEDYTVLETVIM----GHKRLYEVMKEKDaiymkedfsdedgiraaelegefaeldgwEAEPEAAvlLQGLNIPEE 147
Cdd:PRK15056 87 eEVDWSFPVLVEDVVMmgryGHMGWLRRAKKRD-----------------------------RQIVTAA--LARVDMVEF 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 148 LHDQkMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD----TRSINWLEEfLINFENTVIVVSHDRHFLNKVC 219
Cdd:PRK15056 136 RHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvkteARIISLLRE-LRDEGKTMLVSTHNLGSVTEFC 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
1.68e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpNERLATLKQNHFDYEDYT 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV--DGKVLYFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMghkrlyeVMKEKDAIymkEDFSDEDGIrAAELEGEFAElDGWEAEPEAAVLLQGLNIPEELHDQ---KMSELT 157
Cdd:PRK14246 88 LRKEVGM-------VFQQPNPF---PHLSIYDNI-AYPLKSHGIK-EKREIKKIVEECLRKVGLWKEVYDRlnsPASQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSHDRHFLNKVCTHMADL 225
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFL 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
2.23e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnHFDYEDYT 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------------HYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVIMGHKRLYEVMKeKDAIYMKEDfsDEDGIR----AAELEGEFAELDGW----EAEPEAAVLLQGLNIPEELHDQK 152
Cdd:PRK11701 72 LRDLYALSEAERRRLLR-TEWGFVHQH--PRDGLRmqvsAGGNIGERLMAVGArhygDIRATAGDWLERVEIDAARIDDL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD----TRSINWLEEFLINFENTVIVVSHD 211
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
2.27e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM------GPNERLATLKQNHF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 75 DYEDYTVLETVIMGhKRLYEVMKEkdaiymkedfsdedgiraaelegefaeldgwEAEPEAAVLLQGLNIpEELHDQKMS 154
Cdd:PRK11248 81 LLPWRNVQDNVAFG-LQLAGVEKM-------------------------------QRLEIAHQMLKKVGL-EGAEKRYIW 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 155 ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF----ENTVIVVSHD 211
Cdd:PRK11248 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqetGKQVLLITHD 188
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-534 |
2.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.19 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDG-KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVrwgvTTSQAYLPKDNSKDfee 397
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV----LIRGEPITKENIRE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 398 pltildwLRQFAG---KEEDDNTFLRSFLGRMLFSG--------------EEVLKPVNV----------LSGGEKVRVML 450
Cdd:PRK13652 76 -------VRKFVGlvfQNPDDQIFSPTVEQDIAFGPinlgldeetvahrvSSALHMLGLeelrdrvphhLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 451 SKLMLSKANVLVLDDPTNHLDLESITAL----NDGLMAFTGSILFASHDHQFIQTLANRIIaVSDKGVIdRAETTYDEFL 526
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELidflNDLPETYGMTVIFSTHQLDLVPEMADYIY-VMDKGRI-VAYGTVEEIF 226
|
....*...
gi 488284819 527 ENPEIQKQ 534
Cdd:PRK13652 227 LQPDLLAR 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
2.87e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.02 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGpnerlatlkqnHFDYEDY 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSvyEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-----------GMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETvimgHKRLYEVMKEKDAIYMKEDFSDEdgiRAAELEGEFAELDGWEAEPEAAVLLQGLnipEELHDQKMSELTAG 159
Cdd:PRK13635 75 TVWDV----RRQVGMVFQNPDNQFVGATVQDD---VAFGLENIGVPREEMVERVDQALRQVGM---EDFLNREPHRLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSinwLEEFL-----INFEN--TVIVVSHD 211
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRG---RREVLetvrqLKEQKgiTVLSITHD 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-507 |
5.97e-08 |
|
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: 52.43 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGvttsqaylpkdnskdfeepl 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 400 tildwlrqfaGKEeddntflRSFLG--RMLFSGEEVlkpVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITA 477
Cdd:cd03216 61 ----------GKE-------VSFASprDARRAGIAM---VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190
....*....|....*....|....*....|...
gi 488284819 478 LNDGLMAFTG---SILFASHDHQFIQTLANRII 507
Cdd:cd03216 121 LFKVIRRLRAqgvAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-542 |
6.44e-08 |
|
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: 53.57 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 356 ITTTTLFKVIMGEITPDTGSVRWGVTTSqAYLPKDNSKDFeePLTILDWLRqfagkEEDDNTFLRSFLGrmlfsgEEVLK 435
Cdd:cd03237 36 IGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADY--EGTVRDLLS-----SITKDFYTHPYFK------TEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 436 P----------VNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESIT---------ALNDGLMAFTgsilfASHDH 496
Cdd:cd03237 102 PlqieqildreVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLmaskvirrfAENNEKTAFV-----VEHDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488284819 497 QFIQTLANRIIAVSDK-GVIDRAETTY------DEFLENpeiqkqMDILFSSD 542
Cdd:cd03237 177 IMIDYLADRLIVFEGEpSVNGVANPPQslrsgmNRFLKN------LDITFRRD 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-530 |
7.25e-08 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 53.39 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG----------------VTTS 383
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpphkrpvntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 384 QAYLPKDNSKD---FeePLTIldwlrqfAGKEEDDntfLRSFLGRML----FSGEEVLKPvNVLSGGEKVRVMLSKLMLS 456
Cdd:cd03300 81 YALFPHLTVFEniaF--GLRL-------KKLPKAE---IKERVAEALdlvqLEGYANRKP-SQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 457 KANVLVLDDPTNHLDLESITALNDGLMAF---TG-SILFASHDHQFIQTLANRiIAVSDKGVIDRAETTYDEFlENPE 530
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLqkeLGiTFVFVTHDQEEALTMSDR-IAVMNKGKIQQIGTPEEIY-EEPA 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-215 |
7.61e-08 |
|
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: 52.33 E-value: 7.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFG--KPDVLLLDEPTNGLDTRSIN-WLEEF--LINFENTVIVVSHDRHFL 215
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINqLLEVIkgLIDLGNTVILIEHNLDVL 152
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-217 |
9.22e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQF-PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNE--------------R 65
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlknrevpflrrQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 66 LATLKQNHFDYEDYTVLETVIMGhkrlyevmkekdaiYMKEDFSDEDGIRAAElegefAELDgweaepEAAVLLQGLNIP 145
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIP--------------LIIAGASGDDIRRRVS-----AALD------KVGLLDKAKNFP 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 146 eelhdqkmSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSINWLEEFLINFENTVIVVSHDRHFLNK 217
Cdd:PRK10908 136 --------IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISR 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-211 |
1.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnhfdyedyT 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---------------------K 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETVImGHKRLYEVMKEKDAIYMKEDfsdeDGIRAAELEGEFA------ELDGWEAEPEAAVLLQGLNIpEELHDQKMS 154
Cdd:PRK13647 64 VMGREV-NAENEKWVRSKVGLVFQDPD----DQVFSSTVWDDVAfgpvnmGLDKDEVERRVEEALKAVRM-WDFRDKPPY 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 155 ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSHD 211
Cdd:PRK13647 138 HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHD 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-210 |
1.07e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRK---LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQNHFDYED 78
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVLETVIMGHKRL-----YEVMKEKDAIYMkEDFSDEDGIRA-----------AELEGEFAELDGWEAEPEAAVLLQGL 142
Cdd:PTZ00265 463 GVVSQDPLLFSNSIknnikYSLYSLKDLEAL-SNYYNEDGNDSqenknkrnscrAKCAGDLNDMSNTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 143 NIPEE-----------LHD--------------QKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEF 197
Cdd:PTZ00265 542 QTIKDsevvdvskkvlIHDfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*..
gi 488284819 198 LINF---ENTV-IVVSH 210
Cdd:PTZ00265 622 INNLkgnENRItIIIAH 638
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-190 |
1.14e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFP-----DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNE--RLATLKQNH 73
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 F------D-----YEDYTVLETVIM----GHKRlyevmkekdaiymkedfsdedGIRAA---ELEGEFAELdgweaepeA 135
Cdd:COG1101 81 YigrvfqDpmmgtAPSMTIEENLALayrrGKRR---------------------GLRRGltkKRRELFREL--------L 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 136 AVLLQGLnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS 190
Cdd:COG1101 132 ATLGLGL---ENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKT 183
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
1.39e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.15 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 12 PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqnhFDYEDYTVLETVIMGHKR 91
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS--------------WRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 92 LYEVMKEKDAIymkEDFSDEDGIRA--AELEGEFAELDGWEAEPEAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLAQS 169
Cdd:PRK10419 89 RDIQMVFQDSI---SAVNPRKTVREiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 170 LFGKPDVLLLDEPTNGLD----TRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHMADLDFSKI 230
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.67e-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: 51.76 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKilsgeiqpttgvvsmgpnerlatlkqnhfdyedytv 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 82 letVIMGHKRlYEVMKEKdaIYmkedFSDEDgIRAAELEgEFAELD---GWEAEPEaavlLQGLNIPEELHDQKMSeLTA 158
Cdd:cd03217 45 ---TIMGHPK-YEVTEGE--IL----FKGED-ITDLPPE-ERARLGiflAFQYPPE----IPGVKNADFLRYVNEG-FSG 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEF---LINFENTVIVVSHDRHFLNKV 218
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-187 |
2.13e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 10 QFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVV----SMG--PNERL---ATLKQN--HFDYED 78
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAyvPQQAWimnATVRGNilFFDEED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVLEtvimghkrlyevmkekdaiymkedfsdeDGIRAAELEGEFAELD-GWEAEpeaavllqglnIPEelhdqKMSELT 157
Cdd:PTZ00243 749 AARLA----------------------------DAVRVSQLEADLAQLGgGLETE-----------IGE-----KGVNLS 784
|
170 180 190
....*....|....*....|....*....|
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLD 187
Cdd:PTZ00243 785 GGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
2.24e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFP-DRKLFEEVNIkFTPGNC-YGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpnerlatlkqnhfdyed 78
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINF-IAPRNSrIAVIGPNGAGKSTLFRHFNGILKPTSGSV-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 ytVLETVIMGHKRLYEVMKEKDAIYMKEDfsdeDGIRAAELEGEFA------ELDGWEAEPEAAVLLQGLNIpEELHDQK 152
Cdd:PRK13652 62 --LIRGEPITKENIREVRKFVGLVFQNPD----DQIFSPTVEQDIAfgpinlGLDEETVAHRVSSALHMLGL-EELRDRV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSHD 211
Cdd:PRK13652 135 PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQ 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
2.57e-07 |
|
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: 50.77 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFP--DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpnerlatlkqnhfdyedy 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 tvletvimghkrlyevmkekdaiymkedfsdeDGIRAAELEGEFAELDG-WEAEPE--AAVLLQGLNIPeelhdqkmseL 156
Cdd:cd03247 62 --------------------------------DGVPVSDLEKALSSLISvLNQRPYlfDTTLRNNLGRR----------F 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINF--ENTVIVVSH 210
Cdd:cd03247 100 SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITH 155
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
320-515 |
2.69e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSqaylpkDNSKDFEEPL 399
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI------DTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 400 TILDWLRQFAG----------------------------KEEDDNTFLRSFLGRMLFSGEEVLKPVNvLSGGEKVRVMLS 451
Cdd:PRK11264 78 GLIRQLRQHVGfvfqnfnlfphrtvleniiegpvivkgePKEEATARARELLAKVGLAGKETSYPRR-LSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 452 KLMLSKANVLVLDDPTNHLDLESI-TALND--GLMAFTGSILFASHDHQFIQTLANRIIAVsDKGVI 515
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFM-DQGRI 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
319-517 |
2.84e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 51.60 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKK----ILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQAylPKD--- 390
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKE--PAEarr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 391 ------NSKDFEEPLTILDWLRQFAG----KEEDDNTFLRSFLGRMLFsgEEVL-KPVNVLSGGEKVRVMLSKLMLSKAN 459
Cdd:cd03266 79 rlgfvsDSTGLYDRLTARENLEYFAGlyglKGDELTARLEELADRLGM--EELLdRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 460 VLVLDDPTNHLDLESITALND---GLMAFTGSILFASHDHQFIQTLANRIIAVSDKGVIDR 517
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREfirQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
3.06e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILS-----GEIQPTTGVV----------SMGPNE-- 64
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVrlfgrniyspDVDPIEvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 65 -RLATLKQNHFDYEDYTVLETVIMGHKrLYEVMKEKDAIymkeDFSDEDGIRAAELegefaeldgWEaepeaavllqglN 143
Cdd:PRK14267 85 rEVGMVFQYPNPFPHLTIYDNVAIGVK-LNGLVKSKKEL----DERVEWALKKAAL---------WD------------E 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 144 IPEELHDqKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSHDRHFLNKVCTH 221
Cdd:PRK14267 139 VKDRLND-YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDY 217
|
....*....
gi 488284819 222 MADLDFSKI 230
Cdd:PRK14267 218 VAFLYLGKL 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-190 |
3.55e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 3 TVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPT--TGVVsMGPNERLA--TLKQNHFDYED 78
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTI-LANNRKPTkqILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 ytvleTVIMGHKRLYEVMKEKDAIYMKEDFSDEDGIRAAelEGEFAELdgweaepeaavllqGLNIPEE--LHDQKMSEL 156
Cdd:PLN03211 149 -----DILYPHLTVRETLVFCSLLRLPKSLTKQEKILVA--ESVISEL--------------GLTKCENtiIGNSFIRGI 207
|
170 180 190
....*....|....*....|....*....|....
gi 488284819 157 TAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS 190
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-515 |
3.58e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 51.10 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG----------------VTTS 383
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlppkdrdiamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 384 QAYLPKDNSKD-FEEPLTildwLRQFaGKEEDDNTFLRsfLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLV 462
Cdd:cd03301 81 YALYPHMTVYDnIAFGLK----LRKV-PKDEIDERVRE--VAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 463 LDDPTNHLD----LESITALNDGLMAFTGSILFASHDHQFIQTLANRiIAVSDKGVI 515
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADR-IAVMNDGQI 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-210 |
4.00e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 50.63 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 14 RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG--EIQPTTG-VVSMGPNERLATLKQnhfdYEDYTVLETVIMGHK 90
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGeVLINGRPLDKRSFRK----IIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 91 RLYEVMkekdaiymkeDFSdedgiraAELEGefaeldgweaepeaavllqglnipeelhdqkmseLTAGQKVKVLLAQSL 170
Cdd:cd03213 98 TVRETL----------MFA-------AKLRG----------------------------------LSGGERKRVSIALEL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488284819 171 FGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN---TVIVVSH 210
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtgrTIICSIH 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-506 |
5.26e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--PNERLATLK-------- 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnPCARLTPAKahqlgiyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 71 --QNHFDYEDYTVLETVIMG---HKRLYEVMKEKdaiymkedfsdedgirAAELEGEFaELDGweaepEAAVLlqglnip 145
Cdd:PRK15439 91 vpQEPLLFPNLSVKENILFGlpkRQASMQKMKQL----------------LAALGCQL-DLDS-----SAGSL------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 eELHDQKMSELTAGqkvkvllaqsLFGKPDVLLLDEPTNGL---DTRSINWLEEFLINFENTVIVVSHDRHFLNKVCTHM 222
Cdd:PRK15439 142 -EVADRQIVEILRG----------LMRDSRILILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 223 ADLDFSKIKLYvGNydfwLESSQLATKLQAQSNAKKEEQIKELQdfiarfsanaskskqatsrkkmldKITLDdiQPSSR 302
Cdd:PRK15439 211 SVMRDGTIALS-GK----TADLSTDDIIQAITPAAREKSLSASQ------------------------KLWLE--LPGNR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 303 RypfvgftpEREIGNDLLQVENvsVTIDGKKildNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW---- 378
Cdd:PRK15439 260 R--------QQAAGAPVLTVED--LTGEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLngke 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 379 --GVTTSQA------YLPKDNSKD---FEEPLTildW--------LRQFAGKEEDDNTFLRSF---LGrMLFSGEEvlKP 436
Cdd:PRK15439 327 inALSTAQRlarglvYLPEDRQSSglyLDAPLA---WnvcalthnRRGFWIKPARENAVLERYrraLN-IKFNHAE--QA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 437 VNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDlesITALND------GLMAFTGSILFASHDHQFIQTLANRI 506
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD---VSARNDiyqlirSIAAQNVAVLFISSDLEEIEQMADRV 473
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-494 |
5.85e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMG----EITpdTGSVRwgvttsqaylpkdnskdf 395
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyEVT--EGEIL------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 eepltildwlrqFAGKeedDNTFL----RSFLGRML-------FSG---EEVLKPVNV-LSGGEKVRVMLSKLMLSKANV 460
Cdd:cd03217 61 ------------FKGE---DITDLppeeRARLGIFLafqyppeIPGvknADFLRYVNEgFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 488284819 461 LVLDDPTNHLDLESITALNDGLMAF---TGSILFASH 494
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITH 162
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-210 |
7.33e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 24 FTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPnerlaTLKQNHFDYEDYTVLETvimgHKRLYEVMKEKDAIY 103
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD-----IYIGDKKNNHELITNPY----SKKIKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 104 MKEDFSD----EDGIRAAELEGEFA-ELDGWEAEPEAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLL 178
Cdd:PRK13631 120 MVFQFPEyqlfKDTIEKDIMFGPVAlGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190
....*....|....*....|....*....|....*
gi 488284819 179 LDEPTNGLDTRSINWLEEFLINFE---NTVIVVSH 210
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKannKTVFVITH 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
440-511 |
7.63e-07 |
|
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: 49.99 E-value: 7.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD----LESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSD 511
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-511 |
9.03e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 49.35 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 316 GNDLLQVENVSVtidgKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQ-------- 384
Cdd:cd03215 1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpVTRRSprdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 385 -AYLPKDNSKDfeepLTILDW-LRqfagkeedDNTFLRSFLgrmlfsgeevlkpvnvlSGGEKVRVMLSKLMLSKANVLV 462
Cdd:cd03215 77 iAYVPEDRKRE----GLVLDLsVA--------ENIALSSLL-----------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488284819 463 LDDPTNHLDLESITALNDGLMAFT---GSILFASHDHQFIQTLANRIIAVSD 511
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYE 179
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-217 |
9.26e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpnERlATLKQNHFDYEDyt 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF---ER-QSIKKDLCTYQK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 vlETVIMGHKR-LYEVMKEKDAIYMKEDFSDEDgiraaeleGEFAELdgweaepeaaVLLQGLnipEELHDQKMSELTAG 159
Cdd:PRK13540 75 --QLCFVGHRSgINPYLTLRENCLYDIHFSPGA--------VGITEL----------CRLFSL---EHLIDYPCGLLSSG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 160 QKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSInwlEEFLINFE------NTVIVVSHDRHFLNK 217
Cdd:PRK13540 132 QKRQVALLRLWMSKAKLWLLDEPLVALDELSL---LTIITKIQehrakgGAVLLTSHQDLPLNK 192
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-471 |
1.00e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.08 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG-------------VTTSQA 385
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegpgaergvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 386 YLPKDNSKDFeepltiLDWLRQFAG--KEEDDNTfLRSFLGRMLFSGEEVlKPVNVLSGGEKVRVMLSKLMLSKANVLVL 463
Cdd:PRK11248 81 LLPWRNVQDN------VAFGLQLAGveKMQRLEI-AHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
....*...
gi 488284819 464 DDPTNHLD 471
Cdd:PRK11248 153 DEPFGALD 160
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
337-515 |
1.04e-06 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 49.80 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 337 NISFNLT--KDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDN--SKDFEEP-----LTIldwlRQ 407
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpvSMLFQENnlfahLTV----EQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 408 FAGK--------EEDDNTFLRSFLGRMLFSGEEVLKPvNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD---LESIT 476
Cdd:cd03298 90 NVGLglspglklTAEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488284819 477 ALNDGLMAFTG-SILFASHDHQFIQTLANRIIAVsDKGVI 515
Cdd:cd03298 169 DLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFL-DNGRI 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-226 |
1.21e-06 |
|
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: 48.69 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPNERLATLKQnhfdyEDYT 80
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ-----RPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 VLETvimghkrLYEVMkekdaIYmkedfsdedgiraaelegefaeldGWeaepeaavllqglnipeelhdqkMSELTAGQ 160
Cdd:cd03223 76 PLGT-------LREQL-----IY------------------------PW-----------------------DDVLSGGE 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 161 KVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFENTVIVVSHdRHFLNKVCTHMADLD 226
Cdd:cd03223 97 QQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-520 |
1.26e-06 |
|
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: 49.49 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVI-----MGEITPDTGSVRWGvtTSQAYLPKDNSKD 394
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLD--GKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 395 --------FEEP----LTILD------WLRQFAGKEEDDNTFLRSFLGRMLFsgEEVLKPVNV--LSGGEKVRVMLSKLM 454
Cdd:cd03260 79 lrrrvgmvFQKPnpfpGSIYDnvayglRLHGIKLKEELDERVEEALRKAALW--DEVKDRLHAlgLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 455 LSKANVLVLDDPTNHLDLES-------ITALNDGLmaftgSILFASHDHQFIQTLANRIIAVSDKGVIDRAET 520
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPIStakieelIAELKKEY-----TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-210 |
1.66e-06 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 49.15 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQF-PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPN-----------ERLATL 69
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 KQNHFDYEDyTVLETVIMGHkrlyevmkekdaiymkEDFSDEDGIRAAELEGefaeldgweAEPEAAVLLQGLnipeelh 149
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGR----------------PNATDEEVIEAAKEAG---------AHDFIMKLPNGY------- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 150 DQKMSE----LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--TVIVVSH 210
Cdd:cd03254 130 DTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKgrTSIIIAH 196
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-210 |
1.74e-06 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 49.03 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 22 IKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER-LATLKQNHFDYEDYTVLETVIMGHK-- 90
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaapPADRpVSMLFQENNLFAHLTVEQNVGLGLSpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 91 -RLYEVMKEKdaiymkedfsdedgIRAAELEGEFAELDgweaepeaavllqgLNIPEELhdqkmselTAGQKVKVLLAQS 169
Cdd:cd03298 99 lKLTAEDRQA--------------IEVALARVGLAGLE--------------KRLPGEL--------SGGERQRVALARV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488284819 170 LFGKPDVLLLDEPTNGLDTRSINWLEEFLINF----ENTVIVVSH 210
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaetKMTVLMVTH 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
1.75e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEE------VNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpnERLATLKQNH- 73
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklalddVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV---DGLDTSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 74 ----------FDYEDYTVLETVImghkrlyevmkEKDAIYMKEDFS-DEDGIRaAELEGEFAELDGWEAEPEAAVLLQGl 142
Cdd:PRK13633 81 wdirnkagmvFQNPDNQIVATIV-----------EEDVAFGPENLGiPPEEIR-ERVDESLKKVGMYEYRRHAPHLLSG- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 143 nipeelhdqkmseltaGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSH 210
Cdd:PRK13633 148 ----------------GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGrrevVNTIKELNKKYGITIILITH 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-190 |
1.82e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.39 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 13 DRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGeiQPTTGVVSmGpnerlatlkqnhfdyedytvlETVIMGHKRl 92
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-G---------------------EILINGRPL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 93 yevmkekdaiymKEDFSDEDGiraaelegeFAE-LDgweaepeaaVLLQGLNIPEELH-DQKMSELTAGQKVKVLLAQSL 170
Cdd:cd03232 74 ------------DKNFQRSTG---------YVEqQD---------VHSPNLTVREALRfSALLRGLSVEQRKRLTIGVEL 123
|
170 180
....*....|....*....|
gi 488284819 171 FGKPDVLLLDEPTNGLDTRS 190
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQA 143
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-510 |
2.07e-06 |
|
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: 49.01 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGK----KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVR------WGVTTSQAYLpk 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 dnskdFEEPlTILDWL------------RQFAGKEEDDNTflRSFLGRMLFSGEEVLKPVNvLSGGEKVRVMLSKLMLSK 457
Cdd:cd03293 79 -----FQQD-ALLPWLtvldnvalglelQGVPKAEARERA--EELLELVGLSGFENAYPHQ-LSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 458 ANVLVLDDPTNHLDLESITALNDGLMA------FTgsILFASHDhqfIQ---TLANRIIAVS 510
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDiwretgKT--VLLVTHD---IDeavFLADRVVVLS 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-225 |
2.09e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIqptTGVVSMGPNERLatlkqnhfdyedyt 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSAGSHIEL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 vLETVIMGHKRLYEVMKEKDA----IYMKEDFSDEDGIRAAELEGEFAELDGWE------AEPEAAVLLQGLNIPEELH- 149
Cdd:PRK09984 67 -LGRTVQREGRLARDIRKSRAntgyIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVGMVHf 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 150 -DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFEN--TVIVVSHDRHFLNKVCTHMAD 224
Cdd:PRK09984 146 aHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDgiTVVVTLHQVDYALRYCERIVA 225
|
.
gi 488284819 225 L 225
Cdd:PRK09984 226 L 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
319-471 |
2.18e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQ---------AYLP 388
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRqrdeyhqdlLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 389 KDNS-KDFEEPLTILDWLRQFAGKEEDDNtfLRSFLGRMLFSGEEVLkPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPT 467
Cdd:PRK13538 81 HQPGiKTELTALENLRFYQRLHGPGDDEA--LWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....
gi 488284819 468 NHLD 471
Cdd:PRK13538 158 TAID 161
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-194 |
2.46e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 6 DVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG-VVSMGPNERLATLKQnhfdyedytVLET 84
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGsILFQGKEIDFKSSKE---------ALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 85 -VIMGHKRLYEVMKEK--DAIY-----MKEDFSDEDGIRaAELEGEFAELDgweaepeaavllqgLNI-PEElhdqKMSE 155
Cdd:PRK10982 74 gISMVHQELNLVLQRSvmDNMWlgrypTKGMFVDQDKMY-RDTKAIFDELD--------------IDIdPRA----KVAT 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWL 194
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-506 |
4.04e-06 |
|
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: 48.10 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSvtIDGKKI-LDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTT------SQAYLPK 389
Cdd:cd03299 1 LKVENLS--KDWKEFkLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkdITNlppekrDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 DNS----KDFEEplTILDWLR-QFAGKEEDDNTFLRsfLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLD 464
Cdd:cd03299 79 NYAlfphMTVYK--NIAYGLKkRKVDKKEIERKVLE--IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488284819 465 DPTNHLDLES----ITALNDGLMAFTGSILFASHDHQFIQTLANRI 506
Cdd:cd03299 155 EPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-513 |
5.21e-06 |
|
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: 46.76 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTI-DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVImGEITPdTGSVRWGVTTSQA--YLPkdnskdfE 396
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWP-WGSGRIGMPEGEDllFLP-------Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 397 EPLTILDWLRqfagkeeddntflrsflgrmlfsgEEVLKP-VNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLES- 474
Cdd:cd03223 72 RPYLPLGTLR------------------------EQLIYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESe 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488284819 475 ---ITALNDGLMAftgsILFASHDHQFIQtLANRIIAVSDKG 513
Cdd:cd03223 128 drlYQLLKELGIT----VISVGHRPSLWK-FHDRVLDLDGEG 164
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-190 |
5.27e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 13 DR-KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGeiQPTTGV------VSMGP--NERLATL----KQNHFDYEDY 79
Cdd:PLN03140 891 DRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYiegdirISGFPkkQETFARIsgycEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVIM-GHKRL-YEVMKEKDAIYMKEDFsdedgiraaelegEFAELDGWEaepEAAVLLQGLnipeelhdqkmSELT 157
Cdd:PLN03140 969 TVRESLIYsAFLRLpKEVSKEEKMMFVDEVM-------------ELVELDNLK---DAIVGLPGV-----------TGLS 1021
|
170 180 190
....*....|....*....|....*....|...
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS 190
Cdd:PLN03140 1022 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
320-495 |
5.94e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTI-DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVR-WGVTTSQA-------YLPKD 390
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRQAlqknlvaYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 391 NSKDFEEPLTILD-----------WLRQfagKEEDDNTFLRSFLGRMLFSgEEVLKPVNVLSGGEKVRVMLSKLMLSKAN 459
Cdd:PRK15056 87 EEVDWSFPVLVEDvvmmgryghmgWLRR---AKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 488284819 460 VLVLDDPTNHLDLES---ITALNDGLMAFTGSILFASHD 495
Cdd:PRK15056 163 VILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-537 |
7.22e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.76 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 330 DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQAYLPKDNSKD---FEEPLTILd 403
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepIKYDKKSLLEVRKTVgivFQNPDDQL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 404 wlrqFAGKEEDDNTFLRSFLGrmlFSGEEV-------LKPVNV----------LSGGEKVRVMLSKLMLSKANVLVLDDP 466
Cdd:PRK13639 92 ----FAPTVEEDVAFGPLNLG---LSKEEVekrvkeaLKAVGMegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 467 TNHLD-------LESITALNDGLMaftgSILFASHDHQFIQTLANRIIAVSDKGVIdrAETTYDEFLENPEIQKQMDI 537
Cdd:PRK13639 165 TSGLDpmgasqiMKLLYDLNKEGI----TIIISTHDVDLVPVYADKVYVMSDGKII--KEGTPKEVFSDIETIRKANL 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-472 |
7.93e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 47.32 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKDFE--- 396
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAllp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 397 ------EPLTILD--------WLRQFAGKEEDDNTFLRSFLGRMLFSgEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLV 462
Cdd:PRK11231 83 qhhltpEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170
....*....|
gi 488284819 463 LDDPTNHLDL 472
Cdd:PRK11231 162 LDEPTTYLDI 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-186 |
8.01e-06 |
|
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: 47.28 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLqfpdrklfeEVNikftPGNCYGLIGANGAGKSTFLKILSGEIQPTTG--------VVSMGPNERL--------- 66
Cdd:COG0410 19 LHGVSL---------EVE----EGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgedITGLPPHRIArlgigyvpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 67 -----ATLkqnhfdyedyTVLETVIMG---HKRLYEVMKEKDAIYmkedfsdedgiraaELegeFAELdgweaepeaavl 138
Cdd:COG0410 86 grrifPSL----------TVEENLLLGayaRRDRAEVRADLERVY--------------EL---FPRL------------ 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488284819 139 lqglnipEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGL 186
Cdd:COG0410 127 -------KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
320-474 |
1.00e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVT-IDGKKILDNISFNLTKDDKVAFIAdsdiTT----TTLFKVIMGEITPDTGSVRW-GVTTSQaylpkdnsk 393
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVG----PSgsgkSTLVNLLLRFYDPTSGRILIdGVDIRD--------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 394 dfeepLTILDWLRQFAGKEEDdnTFLrsF---------LGRMLFSGEEV---LKPVNV---------------------L 440
Cdd:COG1132 407 -----LTLESLRRQIGVVPQD--TFL--FsgtirenirYGRPDATDEEVeeaAKAAQAhefiealpdgydtvvgergvnL 477
|
170 180 190
....*....|....*....|....*....|....
gi 488284819 441 SGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLES 474
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
311-535 |
1.02e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 311 PEREIGNDLLQVENVSVTIDGK---KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITP-DTGSVRwgVTTSQAY 386
Cdd:PLN03232 606 PPLQPGAPAISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVV--IRGSVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 387 LPKD----NSKDFEEPLTILDWLRQFAGKEEDDNTF---LRSFLGRMLFS-GEevlKPVNVlSGGEKVRVMLSKLMLSKA 458
Cdd:PLN03232 684 VPQVswifNATVRENILFGSDFESERYWRAIDVTALqhdLDLLPGRDLTEiGE---RGVNI-SGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 459 NVLVLDDPTNHLDLESI-----TALNDGLMAFTgSILFASHDHqFIqTLANRIIAVSDkGVIdRAETTYDEFLENPEIQK 533
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAhqvfdSCMKDELKGKT-RVLVTNQLH-FL-PLMDRIILVSE-GMI-KEEGTFAELSKSGSLFK 834
|
..
gi 488284819 534 QM 535
Cdd:PLN03232 835 KL 836
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-533 |
1.17e-05 |
|
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: 46.77 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQ---------AYL 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdITKLPmhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 388 PKDNSKdFEEpLTILDWLRQFAGKEEDDNTFLRSFLGRML--FSGEEVLK-PVNVLSGGEKVRVMLSKLMLSKANVLVLD 464
Cdd:cd03218 81 PQEASI-FRK-LTVEENILAVLEIRGLSKKEREEKLEELLeeFHITHLRKsKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 465 ------DPTNHLDLESITA-LND-GLmaftgSILFAshDHQFIQTLA--NRIIAVSDKGVIdrAETTYDEFLENPEIQK 533
Cdd:cd03218 159 epfagvDPIAVQDIQKIIKiLKDrGI-----GVLIT--DHNVRETLSitDRAYIIYEGKVL--AEGTPEEIAANELVRK 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-211 |
1.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRK--LFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPttgvvsmgpnerlatlkqnHFDYEDY 79
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-------------------DDNPNSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVIMGHKRLYEVmKEKDAIYmkedFSDEDGiraaelegefaELDGWEAEPEAAVLLQGLNIPEE---------LHD 150
Cdd:PRK13640 67 ITVDGITLTAKTVWDI-REKVGIV----FQNPDN-----------QFVGATVGDDVAFGLENRAVPRPemikivrdvLAD 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 151 QKMSE--------LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD----TRSINWLEEFLINFENTVIVVSHD 211
Cdd:PRK13640 131 VGMLDyidsepanLSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
288-515 |
1.50e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 46.61 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 288 MLDKITLDDIqpsSRRYPfVGFTPEREIGNDLLQVENVSVtiDGKKILDNISFNLTKDDKVAFIAD-----SditttTLF 362
Cdd:COG1134 1 MSSMIEVENV---SKSYR-LYHEPSRSLKELLLRRRRTRR--EEFWALKDVSFEVERGESVGIIGRngagkS-----TLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 363 KVIMGEITPDTGSVRW--------GVTTSqaylpkdnskdFEEPLTildwlrqfaGKEeddNTFLRsflGRML-FSGEEV 433
Cdd:COG1134 70 KLIAGILEPTSGRVEVngrvsallELGAG-----------FHPELT---------GRE---NIYLN---GRLLgLSRKEI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 434 LK-----------------PVNVLSGGEKVRVMLSKLMLSKANVLVLDDptnhldlesitALNDGLMAF----------- 485
Cdd:COG1134 124 DEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDE-----------VLAVGDAAFqkkclarirel 192
|
250 260 270
....*....|....*....|....*....|...
gi 488284819 486 ---TGSILFASHDHQFIQTLANRIIaVSDKGVI 515
Cdd:COG1134 193 resGRTVIFVSHSMGAVRRLCDRAI-WLEKGRL 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-524 |
2.08e-05 |
|
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: 45.82 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW----------GVTTSQAYLPK 389
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprEVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 DNSKDFE----EPLTILDWLRQFAGKEEDDNTF-LRSFLGRMLFSGeevlKPVNVLSGGEKVRVMLSKLMLSKANVLVLD 464
Cdd:cd03265 81 DLSVDDEltgwENLYIHARLYGVPGAERRERIDeLLDFVGLLEAAD----RLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 465 DPTNHLDLES-------ITALNDglmAFTGSILFASHDHQFIQTLANRiIAVSDKGVIdRAETTYDE 524
Cdd:cd03265 157 EPTIGLDPQTrahvweyIEKLKE---EFGMTILLTTHYMEEAEQLCDR-VAIIDHGRI-IAEGTPEE 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
319-494 |
2.34e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWgvttSQAYLPKDNSKdFEEP 398
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF----ERQSIKKDLCT-YQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 399 LTildwlrqFAGKEEDDNTFL----------RSFLGRM-------LFSGEEVLK-PVNVLSGGEKVRVMLSKLMLSKANV 460
Cdd:PRK13540 76 LC-------FVGHRSGINPYLtlrenclydiHFSPGAVgitelcrLFSLEHLIDyPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 488284819 461 LVLDDPTNHLD---LESITALNDGLMAFTGSILFASH 494
Cdd:PRK13540 149 WLLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
317-494 |
2.38e-05 |
|
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: 45.85 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 317 NDLLQVENVSVTIDGKKILDNISFNLTKDDKVAfiadsdIT------TTTLFKVIMGEITPDTG-------------SVR 377
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWA------ILgpngagKSTLLSLITGDLPPTYGndvrlfgerrggeDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 378 W-----GVTTS--QAYLPKDNS-KD------------FEEP-----LTILDWLRQFAgkeeddntfLRSFLGRmlfsgee 432
Cdd:COG1119 75 ElrkriGLVSPalQLRFPRDETvLDvvlsgffdsiglYREPtdeqrERARELLELLG---------LAHLADR------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 433 vlkPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDL---ESITALNDGLMAFTG-SILFASH 494
Cdd:COG1119 139 ---PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGApTLVLVTH 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
127-211 |
2.62e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 127 DGWEAEpEAAVLLQGLNIPEELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN--- 203
Cdd:PRK11288 369 NRWEAE-NADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqgv 447
|
....*...
gi 488284819 204 TVIVVSHD 211
Cdd:PRK11288 448 AVLFVSSD 455
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
332-515 |
2.84e-05 |
|
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: 45.60 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 332 KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRwgvTTSQAYLPKDNSKDFEEPLT----------I 401
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT---VRGRVSSLLGLGGGFNPELTgreniylngrL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 402 LDWLRQFAGKEEDDntflrsFLGrmlFS--GEEVLKPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPT----NHLDLESI 475
Cdd:cd03220 112 LGLSRKEIDEKIDE------IIE---FSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488284819 476 TALNDgLMAFTGSILFASHDHQFIQTLANRIIaVSDKGVI 515
Cdd:cd03220 183 RRLRE-LLKQGKTVILVSHDPSSIKRLCDRAL-VLEKGKI 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
332-515 |
3.34e-05 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 45.34 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 332 KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPD---TGSV--------RWGVTTSQAYLPKDNskDFEEPLT 400
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprkPDQFQKCVAYVRQDD--ILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 401 ILDWL------------RQFAGKEEDDNTFLR----SFLGRMLFSGeevlkpvnvLSGGEKVRVMLSKLMLSKANVLVLD 464
Cdd:cd03234 98 VRETLtytailrlprksSDAIRKKRVEDVLLRdlalTRIGGNLVKG---------ISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488284819 465 DPTNHLDleSITAlndglmaftgsilfashdHQFIQTLANriIAVSDKGVI 515
Cdd:cd03234 169 EPTSGLD--SFTA------------------LNLVSTLSQ--LARRNRIVI 197
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
313-478 |
3.42e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.72 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 313 REIGNDLLQVENVSVTI-DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIM-------GEIT-PDTGSVrwgvtts 383
Cdd:COG4178 356 ETSEDGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsGRIArPAGARV------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 384 qAYLPkdnskdfEEPLTILDWLRQF----AGKEEDDNTFLRsflgrmlfsgeEVLKPVN----------------VLSGG 443
Cdd:COG4178 429 -LFLP-------QRPYLPLGTLREAllypATAEAFSDAELR-----------EALEAVGlghlaerldeeadwdqVLSLG 489
|
170 180 190
....*....|....*....|....*....|....*
gi 488284819 444 EKVRVMLSKLMLSKANVLVLDDPTNHLDLESITAL 478
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
150-187 |
3.51e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 3.51e-05
10 20 30
....*....|....*....|....*....|....*...
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD 187
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
3.60e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG--EIQP---TTGVVSM------GPNERLATL- 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPgarVEGEILLdgediyDPDVDVVELr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 70 --------KQNHFDYedyTVLETVIMGHkRLYEVM--KEKDAIYmkedfsdEDGIRAAELegefaeldgWEaepeaavll 139
Cdd:COG1117 92 rrvgmvfqKPNPFPK---SIYDNVAYGL-RLHGIKskSELDEIV-------EESLRKAAL---------WD--------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 140 qglnipeELHDQ-KMS--ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD---TRSInwlEEFLINFEN--TVIVVSH 210
Cdd:COG1117 143 -------EVKDRlKKSalGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKI---EELILELKKdyTIVIVTH 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-56 |
3.68e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 3.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 1 MITVNDVSLQFPDRKLFEeVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG 56
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSG 55
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-49 |
4.43e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 4.43e-05
10 20 30
....*....|....*....|....*....|....*....
gi 488284819 11 FPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG 49
Cdd:NF040905 11 FPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
320-527 |
4.50e-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: 44.91 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTI--DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-----------------GV 380
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaslrrqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 381 TTSQAYLPKDN-------SKDFEEPLTILDWLRQFAGKEeddntFLRSF-LGRMLFSGEEVLKpvnvLSGGEKVRVMLSK 452
Cdd:cd03251 81 VSQDVFLFNDTvaeniayGRPGATREEVEEAARAANAHE-----FIMELpEGYDTVIGERGVK----LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 453 LMLSKANVLVLDDPTNHLDLES---ITALNDGLMAFTGSILFAsHDHQFIQTlANRIIAVSDKGVIDRAetTYDEFLE 527
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESerlVQAALERLMKNRTTFVIA-HRLSTIEN-ADRIVVLEDGKIVERG--THEELLA 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
319-511 |
4.69e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVS-VTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGvttsqaylPKDNS--KDF 395
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS--------GHDITrlKNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 EEPltildWLRQFAGKEEDDNTFLrsfLGRMLF------------SGEEVLKPVNV-----------------LSGGEKV 446
Cdd:PRK10908 73 EVP-----FLRRQIGMIFQDHHLL---MDRTVYdnvaipliiagaSGDDIRRRVSAaldkvglldkaknfpiqLSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 447 RVMLSKLMLSKANVLVLDDPTNHLDlesiTALNDGLMAF------TG-SILFASHDHQFIQTLANRIIAVSD 511
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLD----DALSEGILRLfeefnrVGvTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
316-530 |
5.22e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.14 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 316 GNDLLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVrW-------GVTTSQAY-L 387
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LfdgenipAMSRSRLYtV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 388 PKDNSKDFEE-----PLTILD---W-LRQFAGKEEddnTFLRSFLGRML----FSGEEVLKPvNVLSGGEKVRVMLSKLM 454
Cdd:PRK11831 83 RKRMSMLFQSgalftDMNVFDnvaYpLREHTQLPA---PLLHSTVMMKLeavgLRGAAKLMP-SELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 455 LSKANVLVLDDP-------TNHLDLESITALNDGLMAftgSILFASHDHQFIQTLANRIIAVSDKGVIdrAETTYDEFLE 527
Cdd:PRK11831 159 ALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHDVPEVLSIADHAYIVADKKIV--AHGSAQALQA 233
|
...
gi 488284819 528 NPE 530
Cdd:PRK11831 234 NPD 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
319-484 |
6.01e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQ-----AYLPK- 389
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgktATRGDrsrfmAYLGHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 390 ---DNSKDFEEPLTILDWLRQFAGKEEDDNTFlrSFLGrmLFSGEEVLkpVNVLSGGEKVRVMLSKLMLSKANVLVLDDP 466
Cdd:PRK13543 91 pglKADLSTLENLHFLCGLHGRRAKQMPGSAL--AIVG--LAGYEDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170
....*....|....*...
gi 488284819 467 TNHLDLESITALNDGLMA 484
Cdd:PRK13543 165 YANLDLEGITLVNRMISA 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
156-210 |
6.19e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFLINFEN----TVIVVSH 210
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
437-479 |
6.35e-05 |
|
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: 44.18 E-value: 6.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488284819 437 VNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDleSITALN 479
Cdd:cd03233 116 VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTALE 156
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-224 |
6.51e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 6 DVSLQFPDRKlFE--EVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVsmgpneRLATLKQNHFDYEDYTVLE 83
Cdd:PRK10522 327 NVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI------LLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 84 TVImghkrlyevmkekdaiymkedFSDedgiraAELEGEFAELDGWEAEPEAA-VLLQGLNIPE--ELHDQKMS--ELTA 158
Cdd:PRK10522 400 SAV---------------------FTD------FHLFDQLLGPEGKPANPALVeKWLERLKMAHklELEDGRISnlKLSK 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLD--------TRSINWLEEFLInfenTVIVVSHDRHFLnkvctHMAD 224
Cdd:PRK10522 453 GQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEMGK----TIFAISHDDHYF-----IHAD 517
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-190 |
7.73e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.59 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPD-RKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpnerlatlkqNHFDYEDY 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV-----------SGIDTGDF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 80 TVLETVimghKRLYevmkekdaiymkedfsdedGIRAAELEGEFAeldGWEAEPEAAVLLQGLNIP----EELHDQKMSE 155
Cdd:PRK13644 70 SKLQGI----RKLV-------------------GIVFQNPETQFV---GRTVEEDLAFGPENLCLPpieiRKRVDRALAE 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488284819 156 -------------LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS 190
Cdd:PRK13644 124 iglekyrhrspktLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
105-192 |
8.42e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 105 KEDFSDEDGIRaaeLEGEFAELDGWEAEPEAAVLLQGLNIPEELhDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTN 184
Cdd:NF000106 98 RESFSGRENLY---MIGR*LDLSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
....*...
gi 488284819 185 GLDTRSIN 192
Cdd:NF000106 174 GLDPRTRN 181
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
319-482 |
8.60e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFK----VIMGEITPDTGSVRWGVTTSQA-YLPKDNSK 393
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREgRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 394 D-------FEE-----PLTILD------------W---LRQFAGKEEDDNTFLRSFLGRMLFSGEEVlkpvNVLSGGEKV 446
Cdd:PRK09984 84 SrantgyiFQQfnlvnRLSVLEnvligalgstpfWrtcFSWFTREQKQRALQALTRVGMVHFAHQRV----STLSGGQQQ 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 488284819 447 RVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGL 482
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
438-515 |
9.58e-05 |
|
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: 44.00 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 438 NVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESIT----ALNDGLMAFTgsILFASHDHQFIQTlANRIIaVSDKG 513
Cdd:cd03248 149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQqvqqALYDWPERRT--VLVIAHRLSTVER-ADQIL-VLDGG 224
|
..
gi 488284819 514 VI 515
Cdd:cd03248 225 RI 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-471 |
1.25e-04 |
|
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: 44.90 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSV--TIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIM------GEITPDtgSVRWGVTTSQAY----- 386
Cdd:TIGR01271 1218 MDVQGLTAkyTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQID--GVSWNSVTLQTWrkafg 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 387 -LPKdnsKDFEEPLTI---LDWLRQFAGKE---EDDNTFLRSFLGRmlFSGEEVLKPVN---VLSGGEKVRVMLSKLMLS 456
Cdd:TIGR01271 1296 vIPQ---KVFIFSGTFrknLDPYEQWSDEEiwkVAEEVGLKSVIEQ--FPDKLDFVLVDggyVLSNGHKQLMCLARSILS 1370
|
170
....*....|....*
gi 488284819 457 KANVLVLDDPTNHLD 471
Cdd:TIGR01271 1371 KAKILLLDEPSAHLD 1385
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
320-515 |
1.29e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 43.17 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTI--DGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW-GVTTSQAYLpkdnsKDFE 396
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDISTIPL-----EDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 397 EPLTILdwlrqfagkEEDDNTF---LRSFLGRM-LFSGEEVLKPVNV------LSGGEKVRVMLSKLMLSKANVLVLDDP 466
Cdd:cd03369 82 SSLTII---------PQDPTLFsgtIRSNLDPFdEYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488284819 467 TNHLDLESITALNDGLMA-FTGS-ILFASHDHQFIQTLANriIAVSDKGVI 515
Cdd:cd03369 153 TASIDYATDALIQKTIREeFTNStILTIAHRLRTIIDYDK--ILVMDAGEV 201
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
320-527 |
1.30e-04 |
|
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: 43.76 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTID-GKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG------VTTSQ-----AYL 387
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdireVTLDSlrraiGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 388 PKDNskdfeePL---TILD---WLRQFAGKEED---------DNTFLRSFLGRMLFSGEEVLKpvnvLSGGEKVRVMLSK 452
Cdd:cd03253 81 PQDT------VLfndTIGYnirYGRPDATDEEVieaakaaqiHDKIMRFPDGYDTIVGERGLK----LSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 453 LMLSKANVLVLDDPTNHLDLESITALNDGLMAFTG---SILFASHDHQFIQtlANRIIAVSDKGVIDRAetTYDEFLE 527
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrtTIVIAHRLSTIVN--ADKIIVLKDGRIVERG--THEELLA 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-212 |
1.42e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 44.33 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 6 DVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGvvsmgpnerlatlkQNHFDYEDYT----- 80
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG--------------QIFIDGEDVThrsiq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 81 ------VLET-VIMGHKRLYE----------VMKEKDAIYMKEdfsdedgirAAELegefAELDGWEaepeaavllqgln 143
Cdd:PRK11432 77 qrdicmVFQSyALFPHMSLGEnvgyglkmlgVPKEERKQRVKE---------ALEL----VDLAGFE------------- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284819 144 ipeelhDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT---RSI-NWLEEFLINFENTVIVVSHDR 212
Cdd:PRK11432 131 ------DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrRSMrEKIRELQQQFNITSLYVTHDQ 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
405-495 |
1.46e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.38 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 405 LRQFAGKEEDDNTFLRSFLGRMLFSGEEVLKPVNVLSGGEKVRVMLSKLML-------SKANVLVLDDPTNHLDLESITA 477
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAA 171
|
90 100
....*....|....*....|.
gi 488284819 478 LNDGLMAFT---GSILFASHD 495
Cdd:PRK03695 172 LDRLLSELCqqgIAVVMSSHD 192
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
319-530 |
1.52e-04 |
|
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: 43.34 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGK----KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG----VTTSQAYLPKD 390
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdlTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 391 --------------NSKDFEE----PLTILDWLRQFAGKEEDDntfLRSFLGrmlFSGEEVLKPVNvLSGGEKVRVMLSK 452
Cdd:cd03258 81 rrrigmifqhfnllSSRTVFEnvalPLEIAGVPKAEIEERVLE---LLELVG---LEDKADAYPAQ-LSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 453 LMLSKANVLVLDDPTNHLDLE---SITALNDGLMAFTG-SILFASHDHQFIQTLANRiIAVSDKGVIDRAETTYDEFLeN 528
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITHEMEVVKRICDR-VAVMEKGEVVEEGTVEEVFA-N 231
|
..
gi 488284819 529 PE 530
Cdd:cd03258 232 PQ 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-291 |
1.61e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 19 EVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQP--TTGVVSMGpneRLATLKQNHFDYeDYTVLETVIMGhkrlyevm 96
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG---SVAYVPQVSWIF-NATVRENILFG-------- 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 97 kekdaiymkEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIpeelhdqkmselTAGQKVKVLLAQSLFGKPDV 176
Cdd:PLN03232 703 ---------SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNI------------SGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 177 LLLDEPTNGLDTRSINWLEEFLINFE---NTVIVVSHDRHFLNKVcTHMADLDFSKIKlYVGNYDFWLESSQLATKLQAQ 253
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMKDElkgKTRVLVTNQLHFLPLM-DRIILVSEGMIK-EEGTFAELSKSGSLFKKLMEN 839
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488284819 254 SNAKKEEQ-IKELQDFIARFSA---------NASKSKQATSRKKMLDK 291
Cdd:PLN03232 840 AGKMDATQeVNTNDENILKLGPtvtidvserNLGSTKQGKRGRSVLVK 887
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-479 |
1.75e-04 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 42.54 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDG------KKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITP--DTGSVRWgvttsqaylpkdN 391
Cdd:cd03213 4 LSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLI------------N 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 392 SKDFEepltiLDWLRQFAGKEEDDNTFLRSFLGR--MLFSGEevLKpvnVLSGGEKVRVMLSKLMLSKANVLVLDDPTNH 469
Cdd:cd03213 72 GRPLD-----KRSFRKIIGYVPQDDILHPTLTVRetLMFAAK--LR---GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170
....*....|
gi 488284819 470 LDleSITALN 479
Cdd:cd03213 142 LD--SSSALQ 149
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
440-513 |
1.87e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 1.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDL----ESITALNDGLMAFTGSILFASHDHQFIQTLANRiIAVSDKG 513
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADR-VAVMQNG 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
320-520 |
1.87e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.92 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPKDNSKDFE--- 396
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 397 ----EPLTILD----WLRQFAGKEEDDNTFLRSFLGRMLfsgeEVLK--------PVNvLSGGEKVRVMLSKLMLSKANV 460
Cdd:PRK10851 83 yalfRHMTVFDniafGLTVLPRRERPNAAAIKAKVTQLL----EMVQlahladryPAQ-LSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 461 LVLDDPTNHLDLESITALNDGL------MAFTGsiLFASHDHQFIQTLANRIIAVSdKGVIDRAET 520
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlheeLKFTS--VFVTHDQEEAMEVADRVVVMS-QGNIEQAGT 220
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
15-219 |
1.89e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 15 KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSmgpnerlatlkqNHFDYEDYTVLETV------IMG 88
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTA------------DRMRFDDIDLLRLSprerrkLVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 89 HKrLYEVMKEKDAIYmkeDFSDEDG------IRAAELEGEFAELDGWEAEpEAAVLLQGLNIPEelHDQKMS----ELTA 158
Cdd:PRK15093 89 HN-VSMIFQEPQSCL---DPSERVGrqlmqnIPGWTYKGRWWQRFGWRKR-RAIELLHRVGIKD--HKDAMRsfpyELTE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 159 GQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHDRHFLNKVC 219
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
320-532 |
1.94e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGK-----KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQaylPKDNSKD 394
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEK---NKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 395 FEEPLT--------------ILDWLR------QFAGKE------EDDNTFLRSFLG--------------RMLFSGEEVL 434
Cdd:PRK13651 80 KEKVLEklviqktrfkkikkIKEIRRrvgvvfQFAEYQlfeqtiEKDIIFGPVSMGvskeeakkraakyiELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 435 K--PVNvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD---LESITALNDGLMAFTGSILFASHDHQFIQTLANRIIAV 509
Cdd:PRK13651 160 QrsPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250 260
....*....|....*....|....*...
gi 488284819 510 SDKGVIDRAEtTYD-----EFLENPEIQ 532
Cdd:PRK13651 239 KDGKIIKDGD-TYDilsdnKFLIENNME 265
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
2.26e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.20 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLF--EEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMgpnERLATLKQNHFDYED 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 Y---------------TVLETVIMG---HKRLYEVMKEKdaiyMKEDFSDEDGIRAAElegefaeldgweAEPEAavllq 140
Cdd:PRK13648 84 HigivfqnpdnqfvgsIVKYDVAFGlenHAVPYDEMHRR----VSEALKQVDMLERAD------------YEPNA----- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284819 141 glnipeelhdqkmseLTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:PRK13648 143 ---------------LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHD 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-224 |
2.26e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.36 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 15 KLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGV------------VSMGPNER-------LATLKQNHFD 75
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrfrwngidlLKLSPRERrkiigreIAMIFQEPSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 76 YEDYTvlETVimgHKRLYEVMKEKdaiymkedfsdedgiraaELEGEFAELDGWEAEpEAAVLLQGLNIPEelHDQKMS- 154
Cdd:COG4170 101 CLDPS--AKI---GDQLIEAIPSW------------------TFKGKWWQRFKWRKK-RAIELLHRVGIKD--HKDIMNs 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 155 ---ELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD--TRS-INWLEEFLINFENTVIV-VSHDrhfLNKVcTHMAD 224
Cdd:COG4170 155 yphELTEGECQKVMIAMAIANQPRLLIADEPTNAMEstTQAqIFRLLARLNQLQGTSILlISHD---LESI-SQWAD 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-211 |
2.31e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.48 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 18 EEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMGPnerlatlkqnhfdyedytvLETVIMGHKRLYEVMK 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 98 EKDAIYMkEDFSDEDGIRAAELEGEFAELDGWEAEPEAAVLLQGLNIP--EELHDQKMSELTAGQKVKVLLAQSLFGKPD 175
Cdd:PRK10070 106 KKIAMVF-QSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVglENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488284819 176 VLLLDEPTNGLDTRSINWLEEFLINF----ENTVIVVSHD 211
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISHD 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-217 |
2.35e-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: 42.59 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 22 IKFTPGnCYGLIGANGAGKSTFLK----ILSGEIQPTTgvvsmgpnerlatlKQNHFDyedytvlETVIMGHKRLYEVmk 97
Cdd:cd03240 18 IEFFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNS--------------KGGAHD-------PKLIREGEVRAQV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 98 ekdaiymKEDFSDEDGiRAAELEGEFAELDgweaepEAAVLLQG-LNIPEELHDQKMSeltAGQKVKV------LLAQSL 170
Cdd:cd03240 74 -------KLAFENANG-KKYTITRSLAILE------NVIFCHQGeSNWPLLDMRGRCS---GGEKVLAsliirlALAETF 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488284819 171 FGKPDVLLLDEPTNGLDTRSINW-LEEFL------INFEntVIVVSHDRHFLNK 217
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIEEsLAEIIeerksqKNFQ--LIVITHDEELVDA 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-61 |
2.69e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 2.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIqpTTGVVSMG 61
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL--TGGGAPRG 59
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-272 |
2.88e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 18 EEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG-----------VVSMGPNERLATLKQNHFdyedytvlETVI 86
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGkvdrngevsviAISAGLSGQLTGIENIEF--------KMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 87 MGHKRlYEVMKEKDAIYmkedfsdedgiraaelegEFAELDgweaepeaavllqglnipeELHDQKMSELTAGQKVKVLL 166
Cdd:PRK13546 113 MGFKR-KEIKAMTPKII------------------EFSELG-------------------EFIYQPVKKYSSGMRAKLGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 167 AQSLFGKPDVLLLDEPTNGLDT----RSINWLEEFLiNFENTVIVVSHDRHFLNKVCTHMADLDFSKIKLYVGNYDFWLE 242
Cdd:PRK13546 155 SINITVNPDILVIDEALSVGDQtfaqKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
250 260 270
....*....|....*....|....*....|
gi 488284819 243 SSQLATKLQAQSNAKKEEQIKELQDfiARF 272
Cdd:PRK13546 234 YEAFLNDFKKKSKAEQKEFRNKLDE--SRF 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-56 |
2.95e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.85 E-value: 2.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488284819 14 RKLFEEV-NIKFT--PGNCYGLIGANGAGKSTFLKILSGEIQPTTG 56
Cdd:PRK15112 23 RQTVEAVkPLSFTlrEGQTLAIIGENGSGKSTLAKMLAGMIEPTSG 68
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-467 |
2.99e-04 |
|
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: 42.42 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNltkddkvafIADSDITT---------TTLFKVIMGEITPDTGSVRW------GVTTSQ 384
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLT---------VPEGEIVAllgrngagkTTLLKTIMGLLPPRSGSIRFdgrditGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 385 ------AYLPKDNsKDFEEpLTILDWLR--QFAGKEEDDntflRSFLGRM--LFSgeeVLK-----PVNVLSGGEkvRVM 449
Cdd:cd03224 72 raragiGYVPEGR-RIFPE-LTVEENLLlgAYARRRAKR----KARLERVyeLFP---RLKerrkqLAGTLSGGE--QQM 140
|
170 180
....*....|....*....|.
gi 488284819 450 LS---KLMlSKANVLVLDDPT 467
Cdd:cd03224 141 LAiarALM-SRPKLLLLDEPS 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
320-513 |
3.16e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 42.87 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSV----------------RWGVtts 383
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpsrarharqRVGV--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 384 qayLPK-DN-SKDFeeplTILDWLRQFAGKEEDDNTFLRSFLGRML-FSGEE--VLKPVNVLSGGEKVRVMLSKLMLSKA 458
Cdd:PRK13537 85 ---VPQfDNlDPDF----TVRENLLVFGRYFGLSAAAARALVPPLLeFAKLEnkADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 459 NVLVLDDPTNHLDLES---ITALNDGLMAFTGSILFASHDHQFIQTLANRiIAVSDKG 513
Cdd:PRK13537 158 DVLVLDEPTTGLDPQArhlMWERLRSLLARGKTILLTTHFMEEAERLCDR-LCVIEEG 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-187 |
3.46e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.01 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTG-------VVSMGPNER--LATLKQN 72
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGrimldgqDITHVPAENrhVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHKrlyevmkekdaiyMKEDFSDEDGIRAAElegefaeldgweaepeAAVLLQglniPEELHDQK 152
Cdd:PRK09452 95 YALFPHMTVFENVAFGLR-------------MQKTPAAEITPRVME----------------ALRMVQ----LEEFAQRK 141
|
170 180 190
....*....|....*....|....*....|....*
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD 187
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
440-515 |
3.46e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.73 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD-------LESITALNDglmAFTGSILFASHDHQFIQTLANRIIaVSDK 512
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRII-VMNK 220
|
...
gi 488284819 513 GVI 515
Cdd:PRK13637 221 GKC 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-187 |
3.55e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.41 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKL-FEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSM-GPNER---LATLKQNhfdy 76
Cdd:PRK13657 335 VEFDDVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRtvtRASLRRN---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 77 edytvLETVImghkrlyevmkeKDAIYM-----------KEDFSDEDGIRAAELEgefAELDGWEAEPeaavllQGLN-- 143
Cdd:PRK13657 411 -----IAVVF------------QDAGLFnrsiednirvgRPDATDEEMRAAAERA---QAHDFIERKP------DGYDtv 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488284819 144 IPEelhdqKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD 187
Cdd:PRK13657 465 VGE-----RGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
440-510 |
3.72e-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: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 440 LSGGEKV------RVMLSKLMLSKANVLVLDDPTNHLDLESIT-ALNDgLMAFTGS-----ILFASHDHQFIQtLANRII 507
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAE-IIEERKSqknfqLIVITHDEELVD-AADHIY 193
|
...
gi 488284819 508 AVS 510
Cdd:cd03240 194 RVE 196
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-225 |
3.85e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 153 MSELTAGQKVKVLLAQSLFG---KPDVLLLDEPTNGLDTRSINWLEEFLINFE---NTVIVVSHDRHFLnKVCTHMADL 225
Cdd:PRK00635 807 LSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLThqgHTVVIIEHNMHVV-KVADYVLEL 884
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
409-515 |
4.77e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 409 AGKEEDDNTFLRSFLGRMLFSGEEVLK--PVNvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLES---ITALNDGLM 483
Cdd:PRK10418 109 LGKPADDATLTAALEAVGLENAARVLKlyPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqarILDLLESIV 187
|
90 100 110
....*....|....*....|....*....|...
gi 488284819 484 AFTG-SILFASHDHQFIQTLANRiIAVSDKGVI 515
Cdd:PRK10418 188 QKRAlGMLLVTHDMGVVARLADD-VAVMSHGRI 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-219 |
5.85e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 4 VNDVSLQFPDRK-LFEEV--------NIKFT--PGNCYGLIGANGAGKST----FLKILS--GEI----QPTTGvvsMGP 62
Cdd:PRK15134 278 VEQLQVAFPIRKgILKRTvdhnvvvkNISFTlrPGETLGLVGESGSGKSTtglaLLRLINsqGEIwfdgQPLHN---LNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 63 NERLATLKQNHFDYED-YTVLetvimgHKRLyEVMKekdaiymkedfsdedgIRAAELEGEFAELDGWEAEPEAAVLLQ- 140
Cdd:PRK15134 355 RQLLPVRHRIQVVFQDpNSSL------NPRL-NVLQ----------------IIEEGLRVHQPTLSAAQREQQVIAVMEe 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 141 -GLNiPEELHdQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDtRSI-----NWLEEFLINFENTVIVVSHDRHF 214
Cdd:PRK15134 412 vGLD-PETRH-RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVqaqilALLKSLQQKHQLAYLFISHDLHV 488
|
....*
gi 488284819 215 LNKVC 219
Cdd:PRK15134 489 VRALC 493
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
322-537 |
6.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.92 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 322 VENVSVTIDGK-----KILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWGVTTSQAYLPK-DNSKDF 395
Cdd:PRK13645 9 LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 EEPLTILDWLRQ---FAGKEEDDNTFLRSFLG----RMLFSGEEVLKPVNV-----------LSGGEKVRVMLSKLMLSK 457
Cdd:PRK13645 89 RKEIGLVFQFPEyqlFQETIEKDIAFGPVNLGenkqEAYKKVPELLKLVQLpedyvkrspfeLSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 458 ANVLVLDDPTNHLD---LESITALNDGLMAFTGS-ILFASHDHQFIQTLANRIIAVSDKGVIDRAETTydEFLENPEIQK 533
Cdd:PRK13645 169 GNTLVLDEPTGGLDpkgEEDFINLFERLNKEYKKrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF--EIFSNQELLT 246
|
....
gi 488284819 534 QMDI 537
Cdd:PRK13645 247 KIEI 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-494 |
6.79e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.76 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSV--TIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIM------GEITPDtgSVRW------------G 379
Cdd:cd03289 3 MTVKDLTAkyTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQID--GVSWnsvplqkwrkafG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 380 VTTSQAYL----------PKDNSKDfEEPLTILDwlrqfagkEEDDNTFLRSFLGRMLFSgeeVLKPVNVLSGGEKVRVM 449
Cdd:cd03289 81 VIPQKVFIfsgtfrknldPYGKWSD-EEIWKVAE--------EVGLKSVIEQFPGQLDFV---LVDGGCVLSHGHKQLMC 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488284819 450 LSKLMLSKANVLVLDDPTNHLDLESITALNDGL-MAFTG-SILFASH 494
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADcTVILSEH 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-515 |
7.19e-04 |
|
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: 40.98 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 320 LQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRWG---VTTSQAYLPKDNSK--- 393
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkLTDDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 394 ---DFE--EPLTILD-------WLRQFAGKEEDDNTflRSFLGRMLFSGEEVLKPVNvLSGGEKVRVMLSKLMLSKANVL 461
Cdd:cd03262 81 vfqQFNlfPHLTVLEnitlapiKVKGMSKAEAEERA--LELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284819 462 VLDDPTNHLD-------LESITALndglmAFTG-SILFASHDHQFIQTLANRIIAVsDKGVI 515
Cdd:cd03262 158 LFDEPTSALDpelvgevLDVMKDL-----AEEGmTMVVVTHEMGFAREVADRVIFM-DDGRI 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
435-515 |
1.09e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 40.99 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 435 KPVNVLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESITALNDGLMAFTG----SILFASHDHQFIQTLANRIIAVS 510
Cdd:PRK13636 137 KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHDIDIVPLYCDNVFVMK 216
|
....*
gi 488284819 511 DKGVI 515
Cdd:PRK13636 217 EGRVI 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
440-513 |
1.10e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDL----EsitalndgLMAFTGS--------ILFASHDHQFIQTLANRII 507
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrE--------LLPYLERlareinipILYVSHSLDEILRLADRVV 200
|
....*.
gi 488284819 508 aVSDKG 513
Cdd:PRK11144 201 -VLEQG 205
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
156-211 |
1.11e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488284819 156 LTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEEFL--INFENTVIVVSHD 211
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMheLKEQYTIIIVTHN 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-519 |
1.14e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQF----PDRKLFEEVNIKFTPGNCYGLIGANGAGKS-TFLKILsgEIQPTTGVVSMGPNERLATLKQNHFD 75
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 76 yedytvletvimgHKRLYEVMKEKDAIYMKEDFSDEDGIRAaeLEGEFAEL----DGWEAEPEAAVLLQGL------NIP 145
Cdd:PRK15134 83 -------------EQTLRGVRGNKIAMIFQEPMVSLNPLHT--LEKQLYEVlslhRGMRREAARGEILNCLdrvgirQAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 146 EELHDQKmSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT----RSINWLEEFLINFENTVIVVSHDrhfLNKVcth 221
Cdd:PRK15134 148 KRLTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHN---LSIV--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 222 madldfskiklyvgnydfwlesSQLATKLQAQSNAKKEEQikelQDFIARFSANASKSKQatsrkKMLDKitlddiQPSS 301
Cdd:PRK15134 221 ----------------------RKLADRVAVMQNGRCVEQ----NRAATLFSAPTHPYTQ-----KLLNS------EPSG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 302 RRYPFVGFTPEreigndLLQVENVSV-----------TIDGKKILDNISFNLTKDDKVAFIADSDITTTT----LFKVI- 365
Cdd:PRK15134 264 DPVPLPEPASP------LLDVEQLQVafpirkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIn 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 366 -MGEITPDTGSV-RWgvtTSQAYLPKDNSKD--FEEP-------LTIL----DWLR----QFAGKEEDDntflrsflgRM 426
Cdd:PRK15134 338 sQGEIWFDGQPLhNL---NRRQLLPVRHRIQvvFQDPnsslnprLNVLqiieEGLRvhqpTLSAAQREQ---------QV 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 427 LFSGEEV-LKPVN------VLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLD---LESITALNDGL-----MAFtgsiLF 491
Cdd:PRK15134 406 IAVMEEVgLDPETrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLqqkhqLAY----LF 481
|
570 580
....*....|....*....|....*...
gi 488284819 492 ASHDHQFIQTLANRIIAVSDKGVIDRAE 519
Cdd:PRK15134 482 ISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-215 |
1.23e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284819 151 QKMSELTAGQKVKVLLAQSLF---GKPDVLLLDEPTNGLDTRSINWLEEF---LINFENTVIVVSHDRHFL 215
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQlrtLVSLGHSVIYIDHDPALL 1765
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-211 |
1.26e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 2 ITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGVVSMG--------PNER-LATLKQN 72
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmndvpPAERgVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 73 HFDYEDYTVLETVIMGHKrLYEVMKekdaiymkedfsdedgiraaelegefAELDgwEAEPEAAVLLQglniPEELHDQK 152
Cdd:PRK11000 84 YALYPHLSVAENMSFGLK-LAGAKK--------------------------EEIN--QRVNQVAEVLQ----LAHLLDRK 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284819 153 MSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT------RS-INWLEEFLinfENTVIVVSHD 211
Cdd:PRK11000 131 PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmRIeISRLHKRL---GRTMIYVTHD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
319-535 |
1.34e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGeITPD---TGSVRWgvttSQAYLPKDNSKDF 395
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYW----SGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 396 EEP--------------LTILDWLrqFAGKE--------EDDNTFLR--SFLGRMLFSGEEVLKPVNVLSGGEKVRVMLS 451
Cdd:TIGR02633 76 ERAgiviihqeltlvpeLSVAENI--FLGNEitlpggrmAYNAMYLRakNLLRELQLDADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 452 KLMLSKANVLVLDDPTNHLDLESITALND---GLMAFTGSILFASHDhqfiqtlANRIIAVSDK-GVIDRAE---TTYDE 524
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDiirDLKAHGVACVYISHK-------LNEVKAVCDTiCVIRDGQhvaTKDMS 226
|
250
....*....|.
gi 488284819 525 FLENPEIQKQM 535
Cdd:TIGR02633 227 TMSEDDIITMM 237
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-101 |
1.41e-03 |
|
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: 39.28 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 26 PGNCYGLIGANGAGKSTFLKILSGEIQPTTG---VVSMGPNERLATLKQNHFDYEDYTVLETVIMGHKRLYEVMKEKDA 101
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-190 |
1.44e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 41.37 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 32 LIGANGAGKSTFLKILSGEIqPTTGVVSMGPNE-----------RLATLKQN----HfdyedYTVLETVIMGhkrlyevm 96
Cdd:PRK11174 381 LVGPSGAGKTSLLNALLGFL-PYQGSLKINGIElreldpeswrkHLSWVGQNpqlpH-----GTLRDNVLLG-------- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 97 kekdaiymKEDFSDEDgIRAAeLE----GEFAELdgweaepeaavLLQGLNIPeeLHDQkMSELTAGQKVKVLLAQSLFG 172
Cdd:PRK11174 447 --------NPDASDEQ-LQQA-LEnawvSEFLPL-----------LPQGLDTP--IGDQ-AAGLSVGQAQRLALARALLQ 502
|
170
....*....|....*...
gi 488284819 173 KPDVLLLDEPTNGLDTRS 190
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHS 520
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
440-511 |
1.67e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.01 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLE-SITALNDGLMAF----TGSILFASHDHQFIqTLANRIIAVSD 511
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFlqddKRTLVLVTHKLQYL-PHADWIIAMKD 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-49 |
1.81e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 1.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG 49
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
163-187 |
1.91e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 39.34 E-value: 1.91e-03
10 20
....*....|....*....|....*
gi 488284819 163 KVLLAQSLFGKPDVLLLDEPTNGLD 187
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVD 136
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-211 |
2.09e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.10 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQF---PDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSGEIQPTTGvvsmgpnerlatlkqnhfdye 77
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 78 dytvlETVIMGHKRLYE-VMKEKDAIYMKEDFSD--------EDGIrAAELEGEFAELDGWEAEPEAAVLLQGLnipEEL 148
Cdd:PRK13650 63 -----QIIIDGDLLTEEnVWDIRHKIGMVFQNPDnqfvgatvEDDV-AFGLENKGIPHEEMKERVNEALELVGM---QDF 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284819 149 HDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRS----INWLEEFLINFENTVIVVSHD 211
Cdd:PRK13650 134 KEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
150-187 |
2.94e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 2.94e-03
10 20 30
....*....|....*....|....*....|....*...
gi 488284819 150 DQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLD 187
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
15-47 |
3.20e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.91 E-value: 3.20e-03
10 20 30
....*....|....*....|....*....|...
gi 488284819 15 KLFEEVNIKFTPGNCygLIGANGAGKSTFLKIL 47
Cdd:COG4637 11 KSLRDLELPLGPLTV--LIGANGSGKSNLLDAL 41
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
130-211 |
3.89e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.84 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 130 EAEPEAAVLLQGLNIPE--ELHDQKMSELTAGQKVKVLLAQSLFGKPDVLLLDEPTNGLDT-------RSINWLEEfliN 200
Cdd:PRK10261 141 EAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaqilQLIKVLQK---E 217
|
90
....*....|.
gi 488284819 201 FENTVIVVSHD 211
Cdd:PRK10261 218 MSMGVIFITHD 228
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-218 |
4.00e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 1 MITVNDVSLQFPDRKLFEEVNIKFTPGNCYGLIGANGAGKSTFLKILSG--EIQPTTGVVSMGPNERLAtlkqnhFDYED 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLE------LSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 79 YTVlETVIMGHKRLYEVMKEKDAIYMKEDFSDEDGIRAAELEGEFAELDGWEAEpeaavlLQGLNIPEELHDQKMSE-LT 157
Cdd:PRK09580 75 RAG-EGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEK------IALLKMPEDLLTRSVNVgFS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284819 158 AGQKVKVLLAQSLFGKPDVLLLDEPTNGLDTRSINWLEE---FLINFENTVIVVSHDRHFLNKV 218
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYI 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
433-509 |
4.50e-03 |
|
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: 38.32 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 433 VLKPVNV-LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLE----SITALNDGLMAFTGSILFASHDHQFIQTLANRII 507
Cdd:cd03222 64 VYKPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
..
gi 488284819 508 AV 509
Cdd:cd03222 144 VF 145
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
441-495 |
4.53e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 39.32 E-value: 4.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488284819 441 SGGEKVRVMLSKLMLSKANVLVLDDPTNHLDL----ESITALNDGLMAFTGSILFASHD 495
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
151-225 |
5.53e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 151 QKMSELTAG--QKVKvlLAQSLfGKPD----VLLLDEPTNGLDTRSINWLEEF---LINFENTVIVVSHDRHFLnKVCTH 221
Cdd:cd03271 165 QPATTLSGGeaQRIK--LAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVlqrLVDKGNTVVVIEHNLDVI-KCADW 240
|
....
gi 488284819 222 MADL 225
Cdd:cd03271 241 IIDL 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
319-378 |
6.17e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 38.75 E-value: 6.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 319 LLQVENVSVTIDGKKILDNISFNLTKDDKVAFIADSDITTTTLFKVIMGEITPDTGSVRW 378
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
436-530 |
7.34e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 38.41 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 436 PVNvLSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLE---SITALNDGLMAFTGSILFASHDHQFIQTLANRIIAVSdK 512
Cdd:PRK10619 150 PVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-Q 227
|
90
....*....|....*...
gi 488284819 513 GVIDRaETTYDEFLENPE 530
Cdd:PRK10619 228 GKIEE-EGAPEQLFGNPQ 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
440-526 |
8.85e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284819 440 LSGGEKVRVMLSKLMLSKANVLVLDDPTNHLDLESitalnDGLMAFTGSILFASHDHQFIqTLANRIIAV--SDKGVI-- 515
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-----EKLIEKTIVDIKDKADKTII-TIAHRIASIkrSDKIVVfn 1432
|
90
....*....|....*....
gi 488284819 516 --DR------AETTYDEFL 526
Cdd:PTZ00265 1433 npDRtgsfvqAHGTHEELL 1451
|
|
| |
