|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
90-655 |
3.44e-150 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 450.65 E-value: 3.44e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRLHLSGLLEVNGKPSSSKAYKL--AFVRQEDLFFSQLTVR 167
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP--KGVKGSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDA-KVRGISGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:TIGR00955 118 EHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 247 DAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGPaGKEPLTYFGNFGFLCPEHVNPAEFLA 326
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGS-PDQAVPFFSDLGHPCPENYNPADFYV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 327 DLISVDYSSSEtvySSQKRVHALVDAFSQRSssvlYATPLSMKEETKNGMRPRRKAIVERTDG------WWRQFFLLLKR 400
Cdd:TIGR00955 277 QVLAVIPGSEN---ESRERIEKICDSFAVSD----IGRDMLVNTNLWSGKAGGLVKDSENMEGigynasWWTQFYALLKR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 401 AWMQASRDGPTNKVRARMSVASAVIFGSVFWRMGKSQTSIQDRMGLLQVAAINTAMAALTKTVGVFPKERAIVDRERSKG 480
Cdd:TIGR00955 350 SWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 481 SYSLGPYLLSKTIAEIPIGAAFPLMFGAVLYPMARLNPTLSRFGKFCGIVTVESFAASAMGLTVGAMVPSTEAAMAVGPS 560
Cdd:TIGR00955 430 LYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPP 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 561 LMTVFIVFGGYYVNADNTPIIFRWIPRASLIRWAFQGLCINEFSGLK---FDHQNTFDV--QTGEQALERLSFGGRRIRE 635
Cdd:TIGR00955 510 FVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDnieCTSANTTGPcpSSGEVILETLSFRNADLYL 589
|
570 580
....*....|....*....|
gi 15226227 636 TIAAQSRILMFWYSATYLLL 655
Cdd:TIGR00955 590 DLIGLVILIFFFRLLAYFAL 609
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
67-298 |
1.80e-92 |
|
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: 285.98 E-value: 1.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 67 PVTIRWRNITCSLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlspRLHLSGLLEVNGKPSSS 146
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYK--LAFVRQEDLFFSQLTVRETLSFAAELqlpeissaeerdeyvnnlllklglvscadscvgdakvRGISGGEKKRL 224
Cdd:cd03213 78 RSFRkiIGYVPQDDILHPTLTVRETLMFAAKL-------------------------------------RGLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 225 SLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
88-601 |
1.95e-88 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 291.01 E-value: 1.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslspRLHLSGL----LEVNGKPSSSKAYKLAFVRQEDLFFSQ 163
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG------RIQGNNFtgtiLANNRKPTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVRETLSFAAELQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGpAGKEPLTYFGNFGFLCPEHVNPAE 323
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG-KGSDAMAYFESVGFSPSFPMNPAD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 324 FLADLISVDYSSSETVYSSQKRV-HALVDAF-SQRSSSVLYATPLSMKEETKNGM------RPRRKAIVERTDGWWRQFF 395
Cdd:PLN03211 314 FLLDLANGVCQTDGVSEREKPNVkQSLVASYnTLLAPKVKAAIEMSHFPQANARFvgsastKEHRSSDRISISTWFNQFS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 396 LLLKRAwMQASRDGPTNKVRARMSVASAVIFGSVFWRmgKSQTSIQDRMGLLQVAAINTAMAALTKTVGVFPKERAIVDR 475
Cdd:PLN03211 394 ILLQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVK 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 476 ERSKGSYSLGPYLLSKTIAEIPIGAAFPLMFGAVLYPMARLNPTLSRFGKFCGIVTVESFAASAMGLTVGAMVPSTEAAM 555
Cdd:PLN03211 471 ERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKAS 550
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15226227 556 AVGPSLMTVFIVFGGYYVNadNTPIIFRWIPRASLIRWAFQgLCIN 601
Cdd:PLN03211 551 TIVTVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYR-LLIN 593
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
48-598 |
2.24e-76 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 268.52 E-value: 2.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 48 DEAED--DYAETEDGGGDSIrpvtIRWRNITCSLsdKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL 125
Cdd:TIGR00956 740 DESDDvnDEKDMEKESGEDI----FHWRNLTYEV--KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 126 SLSprLHLSGLLEVNGKP-SSSKAYKLAFVRQEDLFFSQLTVRETLSFAAELQLPEISSAEERDEYVNNLLLKLGLVSCA 204
Cdd:TIGR00956 814 TTG--VITGGDRLVNGRPlDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYA 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 205 DSCVGDAKVrGISGGEKKRLSLACELIASP-SVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKF 283
Cdd:TIGR00956 892 DAVVGVPGE-GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEF 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 284 DDIVLLTEG-TLVYAGPAGKEPLT---YFGNFGFL-CPEHVNPAEFLADLISV--------DYSSSETVYSSQKRVHALV 350
Cdd:TIGR00956 971 DRLLLLQKGgQTVYFGDLGENSHTiinYFEKHGAPkCPEDANPAEWMLEVIGAapgahanqDYHEVWRNSSEYQAVKNEL 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 351 DAFSqrsssvlyaTPLSMKEETKNGMRPRRKAIvertdGWWRQFFLLLKRAWMQASRDGPTNKVRARMSVASAVIFGSVF 430
Cdd:TIGR00956 1051 DRLE---------AELSKAEDDNDPDALSKYAA-----SLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTF 1116
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 431 WRMGKSQTSIQDRMGLLQVAAI--NTAMAALtktVGVFPKERAIVD-RERSKGSYSLGPYLLSKTIAEIPigaaFPLMFG 507
Cdd:TIGR00956 1117 FKVGTSLQGLQNQMFAVFMATVlfNPLIQQY---LPPFVAQRDLYEvRERPSRTFSWLAFIAAQITVEIP----YNLVAG 1189
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 508 AV-----LYPM------ARLNPTLSRFGKFCGIVTVESFAASAMGLTVGAMVPSTEAAMAVGPSLMTVFIVFGGYYVNAD 576
Cdd:TIGR00956 1190 TIfffiwYYPVgfywnaSKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPS 1269
|
570 580
....*....|....*....|..
gi 15226227 577 NTPIIFRWIPRASLIRWAFQGL 598
Cdd:TIGR00956 1270 RMPGFWIFMYRCSPFTYLVQAL 1291
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
69-298 |
1.28e-71 |
|
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: 232.55 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 69 TIRWRNITcsLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLhlSGLLEVNGKPSSSKA 148
Cdd:cd03234 3 VLPWWDVG--LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTT--SGQILFNGQPRKPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 149 YK--LAFVRQEDLFFSQLTVRETLSFAAELQLPEISSAEERDEYVNNLLLKLglvsCADSCVGDAKVRGISGGEKKRLSL 226
Cdd:cd03234 79 FQkcVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRD----LALTRIGGNLVKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
82-612 |
8.87e-68 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 243.09 E-value: 8.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 82 KSSKSVRF-LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL-----SLSPRLHLSGLlevnGKPSSSKAYK--LAF 153
Cdd:TIGR00956 67 KFRDTKTFdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhiGVEGVITYDGI----TPEEIKKHYRgdVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 154 VRQEDLFFSQLTVRETLSFAAELQLP----EISSAEERDEYVNNLLLK-LGLVSCADSCVGDAKVRGISGGEKKRLSLAC 228
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKTPqnrpDGVSREEYAKHIADVYMAtYGLSHTRNTKVGNDFVRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGH-TVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGPAgKEPLTY 307
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPA-DKAKQY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 308 FGNFGFLCPEHVNPAEFLADLISvdysSSETVY--SSQKRVHALVDAFSQ--RSSSVlYA-------TPLSMKEETKNGM 376
Cdd:TIGR00956 302 FEKMGFKCPDRQTTADFLTSLTS----PAERQIkpGYEKKVPRTPQEFETywRNSPE-YAqlmkeidEYLDRCSESDTKE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 377 RPRRKAIVERTD----------GWWRQFFLLLKRAWMQASRDGPTNKVRARMSVASAVIFGSVFWRMGKSQTSIQDRMGL 446
Cdd:TIGR00956 377 AYRESHVAKQSKrtrpsspytvSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 447 LQVAAINTAMAALTKTVGVFpKERAIVDRERSKGSYSLGPYLLSKTIAEIPIGAAFPLMFGAVLYPMARLNPTLSRFGKF 526
Cdd:TIGR00956 457 LFFAILFNAFSSLLEIASMY-EARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFY 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 527 CGIVTVESFAASAMGLTVGAMVPSTEAAMAVGPSLMTVFIVFGGYYVNADNTPIIFRWIPRASLIRWAFQGLCINEFSGL 606
Cdd:TIGR00956 536 LLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGR 615
|
....*.
gi 15226227 607 KFDHQN 612
Cdd:TIGR00956 616 RFECSQ 621
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
90-603 |
5.72e-63 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 228.96 E-value: 5.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlHLSGLLEVNGKPSSSKAYKL--AFVRQEDLFFSQLTVR 167
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGG---YIEGDIRISGFPKKQETFARisGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 248 AFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTE-GTLVYAGPAGKEP---LTYFGNFGFL--CPEHVNP 321
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGRNShkiIEYFEAIPGVpkIKEKYNP 1131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 322 AEFLADLIS--------VDYSSSETVYSSQKRVHALVDAFS---QRSSSVLYATPLSmkeetkngmrprrkaivertDGW 390
Cdd:PLN03140 1132 ATWMLEVSSlaaevklgIDFAEHYKSSSLYQRNKALVKELStppPGASDLYFATQYS--------------------QST 1191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 391 WRQFFLLLKRAWMQASRDGPTNKVRARMSVASAVIFGSVFWRMGKSQTSIQDR---MGLLQVAAINTAMAALTKTVGVFP 467
Cdd:PLN03140 1192 WGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLtmvIGAMYAAVLFVGINNCSTVQPMVA 1271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 468 KERAIVDRERSKGSYSLGPYLLSKTIAEIPIGAAFPLMFGAVLYPMARLNPTLSRFGKFCGIVTVESFAASAMGLTVGAM 547
Cdd:PLN03140 1272 VERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSL 1351
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 548 VPSTEAAMAVGPSLMTVFIVFGGYYVNADNTP---IIFRWI-PRAslirWAFQGLCINEF 603
Cdd:PLN03140 1352 TPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPkwwVWYYWIcPVA----WTVYGLIVSQY 1407
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
67-298 |
1.48e-54 |
|
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: 185.52 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 67 PVTIRWRNITCSLSDKSSKsvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlHLSGLLEVNGKP-SS 145
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGK--RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAG---VITGEILINGRPlDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 146 SKAYKLAFVRQEDLFFSQLTVRETLSFAAELqlpeissaeerdeyvnnlllklglvscadscvgdakvRGISGGEKKRLS 225
Cdd:cd03232 76 NFQRSTGYVEQQDVHSPNLTVREALRFSALL-------------------------------------RGLSVEQRKRLT 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 226 LACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTE-GTLVYAG 298
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
397-601 |
2.21e-47 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 166.68 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 397 LLKRAWMQASRDGPTNKVRARMSVASAVIFGSVFWRMGkSQTSIQDRMGLLQVAAINTAMAALTKTVGVFPKERAIVDRE 476
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 477 RSKGSYSLGPYLLSKTIAEIPIGAAFPLMFGAVLYPMARLNPTLSRFGKFCGIVTVESFAASAMGLTVGAMVPSTEAAMA 556
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226227 557 VGPSLMTVFIVFGGYYVNADNTPIIFRWIPRASLIRWAFQGLCIN 601
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
68-298 |
3.46e-45 |
|
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: 160.51 E-value: 3.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 68 VTIRWRNItcSLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRLHLSGLLEVNGKPSSSK 147
Cdd:cd03233 2 STLSWRNI--SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE--GNVSVEGDIHYNGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYK----LAFVRQEDLFFSQLTVRETLSFAAelqlpeissaeerdeyvnnlllklglvscadSCVGDAKVRGISGGEKKR 223
Cdd:cd03233 78 AEKypgeIIYVSEEDVHFPTLTVRETLDFAL-------------------------------RCKGNEFVRGISGGERKR 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 224 LSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
90-618 |
1.00e-42 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 167.33 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRLHLSGLLEVNGK------PSSSKAYklafVRQEDLFFSQ 163
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLD--PSLKVSGEITYNGYrlnefvPRKTSAY----ISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVRETLSFAAELQ--------LPEISSAE---------ERDEYV---------NNLL----LK-LGLVSCADSCVGDAK 212
Cdd:PLN03140 254 MTVKETLDFSARCQgvgtrydlLSELARREkdagifpeaEVDLFMkatamegvkSSLItdytLKiLGLDICKDTIVGDEM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 213 VRGISGGEKKRLSLAcELIASPS-VIFADEPTTGLDAFQAEKVMETLQKLAQ-DGHTVICSIHQPRGSVYAKFDDIVLLT 290
Cdd:PLN03140 334 IRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLS 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 291 EGTLVYAGPAgKEPLTYFGNFGFLCPEHVNPAEFLADLISVDYSSSETVYSSQKRVHALVDAFSQRSSSVLYATPLSM-- 368
Cdd:PLN03140 413 EGQIVYQGPR-DHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQLENel 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 369 -----KEETKNGMRPRRKAIVERTDgwwrqfflLLK----RAWMQASRDGPTNKVRARMSVASAVIFGSVFWRMGKSQTS 439
Cdd:PLN03140 492 svpfdKSQSHKAALVFSKYSVPKME--------LLKacwdKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTRN 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 440 IQDrmGLLQVAAINTAM-----------AALTKTVGVFPKERAIVdrERSKGSYSLGPYLLsktiaEIPIGAAFPLMFGA 508
Cdd:PLN03140 564 EED--GALYIGALLFSMiinmfngfaelALMIQRLPVFYKQRDLL--FHPPWTFTLPTFLL-----GIPISIIESVVWVV 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 509 VLYPMARLNPTLSRFGK-FCGIVTVESFAASAMGLTVGA----MVPSTEAAMavgpSLMTVFIVfGGYYVNADNTPIIFR 583
Cdd:PLN03140 635 ITYYSIGFAPEASRFFKqLLLVFLIQQMAAGIFRLIASVcrtmIIANTGGAL----VLLLVFLL-GGFILPKGEIPNWWE 709
|
570 580 590
....*....|....*....|....*....|....*
gi 15226227 584 WIPRASLIRWAFQGLCINEFSGLKFDHQNTFDVQT 618
Cdd:PLN03140 710 WAYWVSPLSYGFNALAVNEMFAPRWMNKMASDNST 744
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
91-299 |
7.20e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.14 E-value: 7.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP--SSSKAYK--LAFVRQEDLFFSQLTV 166
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-----SGEVRVLGEDvaRDPAEVRrrIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFAAEL-QLPeissAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:COG1131 91 RENLRFFARLyGLP----RKEARERIDELLELFGLTDAADR-----KVGTLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226227 246 LDAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYAKFDDIVLLTEGTLVYAGP 299
Cdd:COG1131 162 LDPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
88-301 |
2.70e-39 |
|
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: 145.39 E-value: 2.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY----KLAFVRQEDLFFSQ 163
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-----SGSILIDGEDVRKEPRearrQIGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVRETLSFAAELQLPEISSAEERdeyVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:COG4555 89 LTVRENIRYFAELYGLFDEELKKR---IEELIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYAKFDDIVLLTEGTLVYAGPAG 301
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQGSLD 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
73-293 |
5.21e-39 |
|
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: 143.38 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSsksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLslsprLHLSGLLEVNGKP-SSSKAYKL 151
Cdd:cd03225 3 KNLSFSYPDGA----RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL-----GPTSGEVLVDGKDlTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 152 A----FVRQE-DLFFSQLTVRETLSFAAE-LQLPEissaEERDEYVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLS 225
Cdd:cd03225 74 RrkvgLVFQNpDDQFFGPTVEEEVAFGLEnLGLPE----EEIEERVEEALELVGLEGLRD-----RSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 226 LACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGsVYAKFDDIVLLTEGT 293
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
70-299 |
5.45e-37 |
|
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: 138.23 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLslsprLHLSGLLEVNGKPSSSKay 149
Cdd:COG1122 1 IELENLSFSYPGG-----TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL-----KPTSGEVLVDGKDITKK-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 KLAFVRQ---------EDLFFSQlTVRETLSFAAE-LQLPEissaEERDEYVNNLLLKLGLVSCADscvgdakvRGI--- 216
Cdd:COG1122 69 NLRELRRkvglvfqnpDDQLFAP-TVEEDVAFGPEnLGLPR----EEIRERVEEALELVGLEHLAD--------RPPhel 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 217 SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYAKFDDIVLLTEGTLVY 296
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDDGRIVA 214
|
...
gi 15226227 297 AGP 299
Cdd:COG1122 215 DGT 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
91-295 |
1.46e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.02 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYKLAFVRQEDL-----FF--- 161
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVLIDGQDiSSLSERELARLRRRHIgfvfqFFnll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAELQLpeiSSAEERDEYVNNLLLKLGLVSCAdscvgDAKVRGISGGEKKRLSLACELIASPSVIFADE 241
Cdd:COG1136 99 PELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRL-----DHRPSQLSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPRgsVYAKFDDIVLLTEGTLV 295
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
89-294 |
5.52e-34 |
|
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: 129.53 E-value: 5.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 89 FLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS---------KAYKLAFVRQEDL 159
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVRVDGTDISKlsekelaafRRRHIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 160 FFSQLTVRETLSFAAELQLpeiSSAEERDEYVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASPSVIFA 239
Cdd:cd03255 93 LLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLN-----HYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLA-QDGHTVICSIHQPRgsVYAKFDDIVLLTEGTL 294
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDGKI 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
91-306 |
1.24e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFV---RQEDLFFsQLTVR 167
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-----SGTVRLFGKPPRRARRRIGYVpqrAEVDWDF-PITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ET--LSFAAELQLPEISSAEERDEyVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:COG1121 96 DVvlMGRYGRRGLFRRPSRADREA-VDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 246 LDAFQAEKVMETLQKLAQDGHTVICSIHQPrGSVYAKFDDIVLLtEGTLVYAGPAgKEPLT 306
Cdd:COG1121 170 VDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLL-NRGLVAHGPP-EEVLT 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
75-298 |
3.01e-33 |
|
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: 127.24 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 75 ITCSLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK---PSSSKAYK- 150
Cdd:cd03263 2 QIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-----SGTAYINGYsirTDRKAARQs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 151 LAFVRQEDLFFSQLTVRETLSFAAELQ-LPEissaEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACE 229
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKgLPK----SEIKEEVELLLRVLGLTDKANK-----RARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 230 LIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVICSIHQPRgSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
73-306 |
5.89e-33 |
|
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: 127.47 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS-----K 147
Cdd:COG1120 5 ENLSVGYGG------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDLASlsrreL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYKLAFVRQEDLFFSQLTVRETLSFAAELQLPEISSAEERD-EYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSL 226
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDrEAVEEALERTGLEHLADRPVDE-----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 227 ACELIASPSVIFADEPTTGLD-AFQAEkVMETLQKLAQD-GHTVICSIHQP----RgsvYAkfDDIVLLTEGTLVYAGPA 300
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlAHQLE-VLELLRRLARErGRTVVMVLHDLnlaaR---YA--DRLVLLKDGRIVAQGPP 222
|
....*.
gi 15226227 301 gKEPLT 306
Cdd:COG1120 223 -EEVLT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
91-244 |
6.81e-33 |
|
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: 123.91 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK-----LAFVRQEDLFFSQLT 165
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDDERKslrkeIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 166 VRETLSFAAELQLPeisSAEERDEYVNNLLLKLGLVSCADSCVGDaKVRGISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:pfam00005 76 VRENLRLGLLLKGL---SKREKDARAEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
91-298 |
3.36e-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: 124.18 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQ--LTVRE 168
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-----SGSIRVFGKPLEKERKRIGYVPQRRSIDRDfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 169 T--LSFAAELQLPEISSAEERDEyVNNLLLKLGLVSCADSCVGDAkvrgiSGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:cd03235 90 VvlMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGEL-----SGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 247 DAFQAEKVMETLQKLAQDGHTVICSIHQPrGSVYAKFDDIVLLtEGTLVYAG 298
Cdd:cd03235 164 DPKTQEDIYELLRELRREGMTILVVTHDL-GLVLEYFDRVLLL-NRTVVASG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
70-277 |
4.10e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 120.66 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSK-- 147
Cdd:COG4133 3 LEAENLSCRRGE------RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-----AGEVLWNGEPIRDAre 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 --AYKLAFVRQEDLFFSQLTVRETLSFAAELqlpeiSSAEERDEYVNNLLLKLGLVSCAdscvgDAKVRGISGGEKKRLS 225
Cdd:COG4133 72 dyRRRLAYLGHADGLKPELTVRENLRFWAAL-----YGLRADREAIDEALEAVGLAGLA-----DLPVRQLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 226 LACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRG 277
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLE 193
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
88-293 |
4.63e-31 |
|
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: 118.89 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLafVRQEDLFFSQLtvr 167
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEE--LRRRIGYVPQL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 etlsfaaelqlpeissaeerdeyvnnlllklglvscadscvgdakvrgiSGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:cd00267 82 -------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226227 248 AFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAkFDDIVLLTEGT 293
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
66-298 |
4.00e-30 |
|
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: 125.64 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 66 RPVTIRWRNITCSLSDKssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-- 143
Cdd:COG4988 333 GPPSIELEDVSFSYPGG-----RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDls 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 144 ---SSSKAYKLAFVRQEDLFFSQlTVRETLSFAAelqlPEISSAE-----ER---DEYVNNllLKLGLvscaDSCVGDAK 212
Cdd:COG4988 403 dldPASWRRQIAWVPQNPYLFAG-TIRENLRLGR----PDASDEEleaalEAaglDEFVAA--LPDGL----DTPLGEGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 213 vRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVICSIHQPrgSVYAKFDDIVLLTEG 292
Cdd:COG4988 472 -RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL--ALLAQADRILVLDDG 547
|
....*.
gi 15226227 293 TLVYAG 298
Cdd:COG4988 548 RIVEQG 553
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
91-298 |
6.02e-30 |
|
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: 117.68 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGrLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKA----YKLAFVRQEDLFFSQLTV 166
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-----SGTIRIDGQDVLKQPqklrRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFAAELQlpEISSAEErDEYVNNLLLKLGLvscADscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:cd03264 90 REFLDYIAWLK--GIPSKEV-KARVDEVLELVNL---GD--RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 247 DAFQAEKVMETLQKLAQDgHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03264 162 DPEERIRFRNLLSELGED-RIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
91-294 |
6.74e-30 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 116.34 E-value: 6.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK----LAFVRQEDLFFSQLTV 166
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDIKKEPEEvkrrIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFaaelqlpeissaeerdeyvnnlllklglvscadscvgdakvrgiSGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:cd03230 91 RENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226227 247 DAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYAKFDDIVLLTEGTL 294
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
73-298 |
1.25e-28 |
|
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: 112.91 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS-----K 147
Cdd:cd03214 3 ENLSVGYGG------RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDLASlspkeL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYKLAFVRQedlffsQLTVRETLSFAaelqlpeissaeerDEYVNNLllklglvscadscvgdakvrgiSGGEKKRLSLA 227
Cdd:cd03214 72 ARKIAYVPQ------ALELLGLAHLA--------------DRPFNEL----------------------SGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226227 228 CELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQP-RGSVYAkfDDIVLLTEGTLVYAG 298
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLnLAARYA--DRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
91-269 |
1.27e-28 |
|
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: 114.11 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQLTVRETL 170
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAAELQLPeisSAEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQ 250
Cdd:cd03293 95 ALGLELQGV---PKAEARERAEELLELVGL-----SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180
....*....|....*....|
gi 15226227 251 AEKVMETLQKL-AQDGHTVI 269
Cdd:cd03293 167 REQLQEELLDIwRETGKTVL 186
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
70-299 |
1.41e-27 |
|
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: 111.44 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQlsLSPRlhlSGLLEVNGKP----SS 145
Cdd:cd03261 1 IELRGLTKSFGG------RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPD---SGEVLIDGEDisglSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 146 SKAYKL----AFVRQEDLFFSQLTVRETLSFA--AELQLPEissaEERDEYVnnlLLKLGLVSCADscVGDAKVRGISGG 219
Cdd:cd03261 70 AELYRLrrrmGMLFQSGALFDSLTVFENVAFPlrEHTRLSE----EEIREIV---LEKLEAVGLRG--AEDLYPAELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 220 EKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEG 219
|
.
gi 15226227 299 P 299
Cdd:cd03261 220 T 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
35-299 |
2.36e-27 |
|
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: 117.17 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 35 RLFAgpgiaLLPEDEAEDDYAETEDGGGdsirPVTIRWRNITCSLSDKSsksvRFLLKNVSGEAKPGRLLAIMGPSGSGK 114
Cdd:COG4987 308 RLNE-----LLDAPPAVTEPAEPAPAPG----GPSLELEDVSFRYPGAG----RPVLDGLSLTLPPGERVAIVGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 115 TTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK-----LAFVRQEDLFFSQlTVRETLSFAAelqlPEISSAE---- 185
Cdd:COG4987 375 STLLALLLRFLDPQ-----SGSITLGGVDLRDLDEDdlrrrIAVVPQRPHLFDT-TLRENLRLAR----PDATDEElwaa 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 186 -ER---DEYVNNLllKLGLvscaDSCVGDAKvRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKL 261
Cdd:COG4987 445 lERvglGDWLAAL--PDGL----DTWLGEGG-RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA 517
|
250 260 270
....*....|....*....|....*....|....*...
gi 15226227 262 AQdGHTVICSIHQPRGsvYAKFDDIVLLTEGTLVYAGP 299
Cdd:COG4987 518 LA-GRTVLLITHRLAG--LERMDRILVLEDGRIVEQGT 552
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
91-299 |
2.33e-26 |
|
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: 107.65 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAY-------KLAFVRQEDLFFSq 163
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVdvlelrrRVGMVFQKPNPFP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVRETLSFAaeLQLPEISSAEERDEYVNNLLLKLGLvscaDSCVGD-AKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:cd03260 95 GSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAAL----WDEVKDrLHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQDgHTVICSIHQP----RGSvyakfDDIVLLTEGTLVYAGP 299
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKE-YTIVIVTHNMqqaaRVA-----DRTAFLLNGRLVEFGP 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
70-292 |
7.27e-26 |
|
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: 104.39 E-value: 7.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSsksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-----S 144
Cdd:cd03228 1 IEFKNVSFSYPGRP----KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDlrdldL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 145 SSKAYKLAFVRQEDLFFSQlTVREtlsfaaelqlpeissaeerdeyvnNLLlklglvscadscvgdakvrgiSGGEKKRL 224
Cdd:cd03228 72 ESLRKNIAYVPQDPFLFSG-TIRE------------------------NIL---------------------SGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 225 SLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVICSIHQPrgSVYAKFDDIVLLTEG 292
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRL--STIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
46-299 |
7.79e-26 |
|
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: 113.39 E-value: 7.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 46 PEDEAEDDYAETEDGGGDsirpvtIRWRNITCSLSDKSsksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL 125
Cdd:COG2274 456 PEREEGRSKLSLPRLKGD------IELENVSFRYPGDS----PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 126 SLSprlhlSGLLEVNGKPSSS---KAY--KLAFVRQEDLFFSQlTVRETLSFAAelqlPEISSAE-ER-------DEYVN 192
Cdd:COG2274 526 EPT-----SGRILIDGIDLRQidpASLrrQIGVVLQDVFLFSG-TIRENITLGD----PDATDEEiIEaarlaglHDFIE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 193 NLllKLGLvscaDSCVGDaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVICSI 272
Cdd:COG2274 596 AL--PMGY----DTVVGE-GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIA 667
|
250 260
....*....|....*....|....*..
gi 15226227 273 HqpRGSVYAKFDDIVLLTEGTLVYAGP 299
Cdd:COG2274 668 H--RLSTIRLADRIIVLDKGRIVEDGT 692
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
100-298 |
1.03e-25 |
|
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: 105.45 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 100 PGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP--SSSKAY-------KLAFVRQEDLFFSQLTVRETL 170
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPD-----GGTIVLNGTVlfDSRKKInlppqqrKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAaelqLPEISSAEERDEyVNNLLLKLGLVScadscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQ 250
Cdd:cd03297 97 AFG----LKRKRNREDRIS-VDELLDLLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226227 251 AEKVMETLQKLAQDGH-TVICSIHQPRgSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03297 167 RLQLLPELKQIKKNLNiPVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
78-298 |
2.16e-25 |
|
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: 104.90 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 78 SLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVR-- 155
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKLSRRLRKIRrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 156 ------QeDLFFS---QLTVRETLSFAAELQLPEiSSAEERDEYVNNLLLKLGLvscaDSCVGDAKVRGISGGEKKRLSL 226
Cdd:cd03257 83 eiqmvfQ-DPMSSlnpRMTIGEQIAEPLRIHGKL-SKKEARKEAVLLLLVGVGL----PEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPrgSVYAKF-DDIVLLTEGTLVYAG 298
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDL--GVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
81-300 |
3.49e-25 |
|
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: 104.96 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 81 DKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNG------KPSSSKAY--KLA 152
Cdd:cd03256 7 SKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGtdinklKGKALRQLrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 153 FVRQEDLFFSQLTVRETLSFAAELQLPEISS------AEERDEYVNnLLLKLGLVSCADscvgdAKVRGISGGEKKRLSL 226
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRSTWRSlfglfpKEEKQRALA-ALERVGLLDKAY-----QRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQ-DGHTVICSIHQPrgsVYAK--FDDIVLLTEGTLVYAGPA 300
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQV---DLAReyADRIVGLKDGRIVFDGPP 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
70-300 |
4.51e-25 |
|
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: 109.61 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSsksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRLHLSGLLEVNGKPSSSKAY 149
Cdd:COG1123 5 LEVRDLSVRYPGGD----VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP--HGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 KL-----AFVRQE-DLFFSQLTVRETLSFAAELQLpeiSSAEERDEYVNNLLLKLGLVScadscVGDAKVRGISGGEKKR 223
Cdd:COG1123 79 ALrgrriGMVFQDpMTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLER-----RLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 224 LSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPrGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
91-269 |
4.88e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.79 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQLTVRETL 170
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-----SGEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAAELQ-LPeissAEERDEYVNNLLLKLGLVSCAdscvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAF 249
Cdd:COG1116 102 ALGLELRgVP----KAERRERARELLELVGLAGFE-----DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL 172
|
170 180
....*....|....*....|.
gi 15226227 250 QAEKVMETLQKL-AQDGHTVI 269
Cdd:COG1116 173 TRERLQDELLRLwQETGKTVL 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
90-248 |
1.69e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.79 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPRLHLSGLLEVNGK-----PSSSKAYKLAFvrQEDLFFSQL 164
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--TLSPAFSASGEVLLNGRrltalPAEQRRIGILF--QDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAaelqLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:COG4136 92 SVGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
....
gi 15226227 245 GLDA 248
Cdd:COG4136 163 KLDA 166
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
82-298 |
1.84e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 101.83 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 82 KSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYK--LAFVRQED 158
Cdd:cd03259 8 KTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-----SGEILIDGRDvTGVPPERrnIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 159 LFFSQLTVRETLSFAAELQLpeiSSAEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIF 238
Cdd:cd03259 82 ALFPHLTVAENIAFGLKLRG---VPKAEIRARVRELLELVGL-----EGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 239 ADEPTTGLDAFQAEKVMETLQKL-AQDGHTVICSIHQPrGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqRELGITTIYVTHDQ-EEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
73-300 |
3.02e-24 |
|
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: 107.30 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP------SSS 146
Cdd:COG1123 264 RNLSKRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT-----SGSILFDGKDltklsrRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAY--KLAFVRQ--EDLFFSQLTVRETLSFAaeLQLPEISSAEERDEYVNNLLLKLGLvscaDSCVGDAKVRGISGGEKK 222
Cdd:COG1123 338 RELrrRVQMVFQdpYSSLNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGL----PPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 223 RLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD-LAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
91-273 |
3.51e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.28 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS-KAYKLAFVR-------QEDLFFS 162
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT-----SGQVLVNGQDLSRlKRREIPYLRrrigvvfQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLSFAaeLQLPEISSAEERDEyVNNLLLKLGLVScadscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:COG2884 93 DRTVYENVALP--LRVTGKSRKEIRRR-VREVLDLVGLSD-----KAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
68-300 |
3.60e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 68 VTIRWRNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS- 146
Cdd:PRK13548 1 AMLEARNLSVRLGG------RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-----SGEVRLNGRPLADw 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYKLAFVR-----QEDLFFSqLTVRETLSFAAelqLPEISSAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEK 221
Cdd:PRK13548 70 SPAELARRRavlpqHSSLSFP-FTVEEVVAMGR---APHGLSRAEDDALVAAALAQVDLAHLAGR-----DYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 222 KRLSLA---CELIA---SPSVIFADEPTTGLDAFQAEKVMETLQKLA-QDGHTVICSIH------QprgsvYAkfDDIVL 288
Cdd:PRK13548 141 QRVQLArvlAQLWEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHdlnlaaR-----YA--DRIVL 213
|
250
....*....|..
gi 15226227 289 LTEGTLVYAGPA 300
Cdd:PRK13548 214 LHQGRLVADGTP 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
91-298 |
3.97e-24 |
|
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: 101.64 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK-PSSSKAyklAFVRQEDLFFSQ------ 163
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT-----SGEVRVAGLvPWKRRK---KFLRRIGVVFGQktqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 -LTVRETLSFAAEL-QLPEISSAEERDEYVNnlLLKLGLVScadscvgDAKVRGISGGEKKRLSLACELIASPSVIFADE 241
Cdd:cd03267 109 dLPVIDSFYLLAAIyDLPPARFKKRLDELSE--LLDLEELL-------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHY-MKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
88-293 |
5.87e-24 |
|
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: 99.18 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY-------KLAFVRQEDLF 160
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDelpplrrRIGMVFQDFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLSFaaelqlpeissaeerdeyvnnlllklglvscadscvgdakvrGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:cd03229 88 FPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226227 241 EPTTGLDAFQAEKVMETLQKL-AQDGHTVICSIHQPRgSVYAKFDDIVLLTEGT 293
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
91-269 |
6.49e-24 |
|
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: 100.97 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSP-RLHLSGLlEVNGKPSSsKAYKLAFVR--QEDLFFSQLTVR 167
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSgSVLFDGE-DITGLPPH-EIARLGIGRtfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQLPE-------ISSAEERDEYVNNLLLKLGLVScadscVGDAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:cd03219 94 ENVMVAAQARTGSglllaraRREEREARERAEELLERVGLAD-----LADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180
....*....|....*....|....*....
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
70-298 |
6.88e-24 |
|
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: 100.52 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNG-----KPS 144
Cdd:cd03266 2 ITADALTKRFRDVKKTVQ--AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-----AGFATVDGfdvvkEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 145 SSKAyKLAFVRQEDLFFSQLTVRETLSFAAELQLPEISSAEERdeyVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRL 224
Cdd:cd03266 75 EARR-RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTAR---LEELADRLGMEELLDR-----RVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 225 SLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
88-273 |
9.37e-24 |
|
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: 99.64 E-value: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY--KLAFVRQE--DLFFSQ 163
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-----SGSILLNGKPIKAKERrkSIGYVMQDvdYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 lTVRETLSFAAELqlpeissAEERDEYVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:cd03226 88 -SVREELLLGLKE-------LDAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190
....*....|....*....|....*....|
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
88-275 |
1.01e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.51 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSK---AY--KLAFVRQEDLFFS 162
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMpppEWrrQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QlTVRETLSFAAELQLPEISsaeerDEYVNNLLLKLGLvscADSCVgDAKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:COG4619 88 G-TVRDNLPFPFQLRERKFD-----RERALELLERLGL---PPDIL-DKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 243 TTGLDAFQAEKVMETLQKL-AQDGHTVICSIHQP 275
Cdd:COG4619 158 TSALDPENTRRVEELLREYlAEEGRAVLWVSHDP 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
91-298 |
6.30e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 97.29 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK---PSSSKAYKLAFVRQEDLFFSQLTVR 167
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-----SGEITFDGKsyqKNIEALRRIGALIEAPGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLS-FAAELQLpeissaeeRDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:cd03268 91 ENLRlLARLLGI--------RKKRIDEVLDVVGL-----KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 247 DAFQAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
91-266 |
9.78e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.40 E-value: 9.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQLTVRETL 170
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-----SGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAaeLQLPEISSAEeRDEYVNNLLLKLGLvscADscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQ 250
Cdd:COG4525 98 AFG--LRLRGVPKAE-RRARAEELLALVGL---AD--FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170
....*....|....*.
gi 15226227 251 AEKVMETLQKLAQDGH 266
Cdd:COG4525 170 REQMQELLLDVWQRTG 185
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
70-299 |
1.92e-22 |
|
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: 96.97 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQlsLSPRlhlSGLLEVNGKP-SSSKA 148
Cdd:COG1127 6 IEVRNLTKSFGDRV------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPD---SGEILVDGQDiTGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 149 YKLAFVRQE--DLF-----FSQLTVRETLSFA--AELQLPEissaEERDEYVnnlLLKLGLVSCADscVGDAKVRGISGG 219
Cdd:COG1127 75 KELYELRRRigMLFqggalFDSLTVFENVAFPlrEHTDLSE----AEIRELV---LEKLELVGLPG--AADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 220 EKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVIcsI--HQPRgSVYAKFDDIVLLTEGTLVY 296
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSV--VvtHDLD-SAFAIADRVAVLADGKIIA 222
|
...
gi 15226227 297 AGP 299
Cdd:COG1127 223 EGT 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
91-273 |
2.68e-22 |
|
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: 95.55 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQlslspRLHLSGLLEVNGKPSSS-KAYKLAFVR-------QEDLFFS 162
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVSDlRGRAIPYLRrkigvvfQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLSFAAElqlpeISSAEERD--EYVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:cd03292 92 DRNVYENVAFALE-----VTGVPPREirKRVPAALELVGLSHKHR-----ALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
91-298 |
4.52e-22 |
|
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: 95.04 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLslsprLHLSGLLEVNGKPSSSKAY-KLAFVRQEDLFFSQLTVRET 169
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII-----LPDSGEVLFDGKPLDIAARnRIGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 170 LSFAAELQLPEISSAEERDEYvnnLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAF 249
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDE---WLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226227 250 QAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
70-269 |
1.91e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 94.10 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKsvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlHLSGLLEVNGKPSSSKAY 149
Cdd:COG1124 2 LEVRNLSVSYGQGGRR--VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-----PWSGEVTFDGRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 KlAFVRQEDLFFSQ--------LTVRETLsfaAE-LQLPEISSAEERdeyVNNLLLKLGLvscadscvgDAKVRG----- 215
Cdd:COG1124 75 K-AFRRRVQMVFQDpyaslhprHTVDRIL---AEpLRIHGLPDREER---IAELLEQVGL---------PPSFLDryphq 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 216 ISGGEKKRLSLACELIASPSVIFADEPTTGLDA-FQAEkVMETLQKL-AQDGHTVI 269
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVsVQAE-ILNLLKDLrEERGLTYL 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
91-289 |
3.04e-21 |
|
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: 98.13 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-----SSSKAYKLAFVRQEDLFFSQlT 165
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPladadADSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSF----AAELQLPEISSAEERDEYVNNLLLKLglvscaDSCVGDAKvRGISGGEKKRLSLACELIASPSVIFADE 241
Cdd:TIGR02857 412 IAENIRLarpdASDAEIREALERAGLDEFVAALPQGL------DTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQdGHTVICSIHQPrgSVYAKFDDIVLL 289
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
91-304 |
3.30e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLaGQLSlSPRlhlSGLLEVNGKPSSS-KAYKLAFVRQEDL--FFSQLTVR 167
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLD-KPT---SGTYRVAGQDVATlDADALAQLRREHFgfIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQLPEI---SSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:PRK10535 99 SHLTAAQNVEVPAVyagLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 245 GLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgsVYAKFDDIVLLTEGTLVYAGPAGKEP 304
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ--VAAQAERVIEIRDGEIVRNPPAQEKV 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
91-274 |
6.25e-21 |
|
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: 91.82 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPrlHLSGLLEVNGKPSSSKAYKLAFVRQE--------DLFfS 162
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL---LEE--PDSGTIIIDGLKLTDDKKNINELRQKvgmvfqqfNLF-P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLSFAAE--LQLPEiSSAEERDEYvnnLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:cd03262 90 HLTVLENITLAPIkvKGMSK-AEAEERALE---LLEKVGLADKAD-----AYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQ 274
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
91-273 |
6.93e-21 |
|
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: 93.99 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKL----AFVRQEDLFFSQLTV 166
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT-----SGTARVAGYDVVREPRKVrrsiGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFAAELQ-LPEiSSAEERDEyvnNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:TIGR01188 84 RENLEMMGRLYgLPK-DEAEERAE---ELLELFELGEAADR-----PVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180
....*....|....*....|....*...
gi 15226227 246 LDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
91-273 |
6.95e-21 |
|
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: 90.95 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPRlhlSGLLEVNGKPSSSKAYKLAFVRQ---------EDLFF 161
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNG--LLRPQ---SGAVLIDGEPLDYSRKGLLERRQrvglvfqdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQlTVRETLSFAA-ELQLPEissaEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:TIGR01166 83 AA-DVDQDVAFGPlNLGLSE----AEVERRVREALTAVGA-----SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
73-282 |
1.03e-20 |
|
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: 90.50 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSlsdkssKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRLhlSGLLEVNGKPSSSKAYK-- 150
Cdd:TIGR01189 4 RNLACS------RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG---LLRPD--SGEVRWNGTPLAEQRDEph 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 151 --LAFVRQEDLFFSQLTVRETLSFAAElqlpeISSAEERDeyVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLAC 228
Cdd:TIGR01189 73 enILYLGHLPGLKPELSALENLHFWAA-----IHGGAQRT--IEDALAAVGLTGFED-----LPAAQLSAGQQRRLALAR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAK 282
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEAR 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
90-332 |
1.06e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRlhlSGLLEVNGKP---SSSKAY--KLAFVRQEDLFFSQL 164
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQ---SGTVFLGDKPismLSSRQLarRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELQLPEISSAEERDE-YVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:PRK11231 92 TVRELVAYGRSPWLSLWGRLSAEDNaRVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 244 TGLD-AFQAEkVMETLQKLAQDGHTVICSIHQ-PRGSVYAkfDDIVLLTEGTLVYAGpagkepltyfgnfgflCPEHVNP 321
Cdd:PRK11231 167 TYLDiNHQVE-LMRLMRELNTQGKTVVTVLHDlNQASRYC--DHLVVLANGHVMAQG----------------TPEEVMT 227
|
250
....*....|.
gi 15226227 322 AEFLADLISVD 332
Cdd:PRK11231 228 PGLLRTVFDVE 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
84-248 |
2.27e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSV--RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGllEVngkpSSSKAYKLAFVRQEDLFF 161
Cdd:COG0488 5 SKSFggRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD-----SG--EV----SIPKGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLS------FAAELQLPEISSA------------------EERDEY-----VNNLLLKLGLvscaDSCVGDAK 212
Cdd:COG0488 74 DDLTVLDTVLdgdaelRALEAELEELEAKlaepdedlerlaelqeefEALGGWeaearAEEILSGLGF----PEEDLDRP 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 15226227 213 VRGISGGEKKRLSLACELIASPSVIFADEPTTGLDA 248
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
91-298 |
2.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLnvlagqlslsprLHLSGLLE-------VNGKPSSSKAYKLAFVRQ------- 156
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLF------------LHFNGILKptsgevlIKGEPIKYDKKSLLEVRKtvgivfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 --EDLFFSQlTVRETLSFAA-ELQLPEissaEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIAS 233
Cdd:PRK13639 86 npDDQLFAP-TVEEDVAFGPlNLGLSK----EEVEKRVKEALKAVGM-----EGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 234 PSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQ-PRGSVYAkfDDIVLLTEGTLVYAG 298
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvDLVPVYA--DKVYVMSDGKIIKEG 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
89-273 |
4.86e-20 |
|
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: 89.70 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 89 FLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPRlhlSGLLEVNGK---PSSSKAYKLAFVRQEDLFFSQLT 165
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAG--FIKPD---SGKILLNGKditNLPPEKRDISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPEissAEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:cd03299 88 VYKNIAYGLKKRKVD---KKEIERKVLEIAEMLGI-----DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180
....*....|....*....|....*....
gi 15226227 246 LDAFQAEKVMETLQKLAQD-GHTVICSIH 273
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEfGVTVLHVTH 188
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
64-293 |
1.05e-19 |
|
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: 87.91 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 64 SIRPVTIRWrnitcslsDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLsprlhLSGLLEVNGkp 143
Cdd:cd03250 2 SVEDASFTW--------DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK-----LSGSVSVPG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 144 ssskayKLAFVRQEDLFFSqLTVRETLSFAAELQlpeissaEERDEYVnnlllklgLVSCA------------DSCVGDa 211
Cdd:cd03250 67 ------SIAYVSQEPWIQN-GTIRENILFGKPFD-------EERYEKV--------IKACAlepdleilpdgdLTEIGE- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 212 kvRGI--SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMET-LQKLAQDGHTVICSIHQPRGSVYAkfDDIVL 288
Cdd:cd03250 124 --KGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPHA--DQIVV 199
|
....*
gi 15226227 289 LTEGT 293
Cdd:cd03250 200 LDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
91-275 |
1.10e-19 |
|
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: 93.19 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPRlhlSGLLEVNGKPSSSK-----AYKLAFVRQEDLFFSQlT 165
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAG--LLDPL---QGEVTLDGVPVSSLdqdevRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAelqlPEISSAEERDeyvnnLLLKLGLVSCADSCVG--DAKVRG----ISGGEKKRLSLACELIASPSVIFA 239
Cdd:TIGR02868 425 VRENLRLAR----PDATDEELWA-----ALERVGLADWLRALPDglDTVLGEggarLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKlAQDGHTVICSIHQP 275
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
91-298 |
1.49e-19 |
|
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: 88.29 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqLSLSPrlhlSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQLTVRETL 170
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPT----SGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAAELQLPEISSaEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQ 250
Cdd:TIGR01184 76 ALAVDRVLPDLSK-SERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226227 251 AEKVMETLQKLAQDGH-TVICSIHQPRGSVYAKfDDIVLLTEGTLVYAG 298
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRvTVLMVTHDVDEALLLS-DRVVMLTNGPAANIG 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
91-273 |
1.66e-19 |
|
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: 87.81 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLS-LSPRLHLSGLlEVNGKPSSSKAyKLAFVRQEDLFFSQLTVRET 169
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGH-DVVREPREVRR-RIGIVFQDLSVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 170 LSFAAELQ-LPeissAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDA 248
Cdd:cd03265 94 LYIHARLYgVP----GAERRERIDELLDFVGLLEAADR-----LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180
....*....|....*....|....*.
gi 15226227 249 FQAEKVMETLQKL-AQDGHTVICSIH 273
Cdd:cd03265 165 QTRAHVWEYIEKLkEEFGMTILLTTH 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
88-306 |
2.64e-19 |
|
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: 87.83 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL--SLSPRLHLSG-------LLEVngKPssskayKLAFV--RQ 156
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRLFGerrggedVWEL--RK------RIGLVspAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 EDLFFSQLTVRET-LS-FAAELQLPEISSAEERDEyVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASP 234
Cdd:COG1119 88 QLRFPRDETVLDVvLSgFFDSIGLYREPTDEQRER-ARELLELLGLAHLAD-----RPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 235 SVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVIcsihqprgsVY---------AKFDDIVLLTEGTLVYAGPAgKEPL 305
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTL---------VLvthhveeipPGITHVLLLKDGRVVAAGPK-EEVL 231
|
.
gi 15226227 306 T 306
Cdd:COG1119 232 T 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
49-298 |
3.01e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.22 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 49 EAEDDYAETEDGGGDSIRPVTIRWRN-ITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSL 127
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIEAEDlEILSPDGKT------LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 128 SprlhlsGLLEVNGKPSSS---KAY--KLAFVRQEDLFFSQlTVRETLSFA-AELQLPEISSAEER---DEYVNnlLLKL 198
Cdd:PRK11174 403 Q------GSLKINGIELREldpESWrkHLSWVGQNPQLPHG-TLRDNVLLGnPDASDEQLQQALENawvSEFLP--LLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 199 GLvscaDSCVGDAKVrGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVICSIHQPrgS 278
Cdd:PRK11174 474 GL----DTPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQL--E 545
|
250 260
....*....|....*....|
gi 15226227 279 VYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK11174 546 DLAQWDQIWVMQDGQIVQQG 565
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
90-289 |
3.07e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlHLSGLLEVNGkpssskAYKLAFVRQE----DLFfsQLT 165
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-----PTSGTVRRAG------GARVAYVPQRsevpDSL--PLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRE--TLSFAAELQLPEISSAEERDEyVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:NF040873 74 VRDlvAMGRWARRGLWRRLTRDDRAA-VDDALERVGLADLAG-----RQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSIHQPrgSVYAKFDDIVLL 289
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDL--ELVRRADPCVLL 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
90-299 |
6.10e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPRlhlSGLLEVNGKPSSSKAYK-----LAFVRQEDLFFSQL 164
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING--TLTPT---AGTVLVAGDDVEALSARaasrrVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELQLPEISSAEERDE-YVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:PRK09536 93 DVRQVVEMGRTPHRSRFDTWTETDRaAVERAMERTGVAQFADR-----PVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSIHQPrgSVYAKF-DDIVLLTEGTLVYAGP 299
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIHDL--DLAARYcDELVLLADGRVRAAGP 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
70-298 |
1.42e-18 |
|
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: 83.90 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKsvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPRlhlSGLLEVNGKPSS---- 145
Cdd:cd03247 1 LSINNVSFSYPEQEQQ----VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSdlek 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 146 SKAYKLAFVRQEDLFFSQlTVRetlsfaaelqlpeissaeerdeyvNNLLLKLglvscadscvgdakvrgiSGGEKKRLS 225
Cdd:cd03247 72 ALSSLISVLNQRPYLFDT-TLR------------------------NNLGRRF------------------SGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226227 226 LACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDgHTVICSIHQPRGsvYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
88-277 |
1.82e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRLHlsGLLEVNGKPS--SSKAYKLAFVRQEDLFFSQLT 165
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG---LLPPAA--GTIKLDGGDIddPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPEISSAEERDEYVNnlllkLGLvscadscVGDAKVRGISGGEKKRLSLAcELIASPSVIFA-DEPTT 244
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAVG-----LAP-------LAHLPFGYLSAGQKRRVALA-RLLVSNRPIWIlDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 245 GLDAFQAEKVMETLQ-KLAQDGhTVICSIHQPRG 277
Cdd:PRK13539 157 ALDAAAVALFAELIRaHLAQGG-IVIAATHIPLG 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
88-298 |
2.05e-18 |
|
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: 84.97 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagqlslsPRLH--LSGLLEVNGkpSSSKAYKL-------AFVRQED 158
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI-------PRFYdvDSGRILIDG--HDVRDYTLaslrrqiGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 159 LFFSQlTVRETLSFAAelqlPEISSAEERD--------EYVNNllLKLGLvscaDSCVGDakvRGI--SGGEKKRLSLAC 228
Cdd:cd03251 86 FLFND-TVAENIAYGR----PGATREEVEEaaraanahEFIME--LPEGY----DTVIGE---RGVklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDgHTVICSIHqpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAH--RLSTIENADRIVVLEDGKIVERG 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
90-300 |
2.27e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.19 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLL---NVLAGQLSLSPRLhlsGLLEVNGKPSSSKAYKL--------AFVRQED 158
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLEQPEAGTIRV---GDITIDTARSLSQQKGLirqlrqhvGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 159 LFFSQLTVRETLsfaaeLQLPEISSAEERDEYV---NNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPS 235
Cdd:PRK11264 95 NLFPHRTVLENI-----IEGPVIVKGEPKEEATaraRELLAKVGL-----AGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQprgSVYAK--FDDIVLLTEGTLVYAGPA 300
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE---MSFARdvADRAIFMDQGRIVEQGPA 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
91-300 |
3.65e-18 |
|
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: 84.31 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK---LAFVRQEDLFFSQLTVR 167
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-----SGTILFGGEDATDVPVQernVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQ-LPEISSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:cd03296 93 DNVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 247 DAFQAEKVMETLQKLAQD-GHTVICSIH-QPRGSVYAkfDDIVLLTEGTL--------VYAGPA 300
Cdd:cd03296 168 DAKVRKELRRWLRRLHDElHVTTVFVTHdQEEALEVA--DRVVVMNKGRIeqvgtpdeVYDHPA 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
91-292 |
5.76e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.37 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQLTVRETL 170
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-----HGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAaeLQLPEISSAeERDEYVNNLLLKLGLVScadscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQ 250
Cdd:PRK11248 92 AFG--LQLAGVEKM-QRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15226227 251 AEKVMETLQKLAQD-GHTVICSIHQPRGSVYAKfDDIVLLTEG 292
Cdd:PRK11248 164 REQMQTLLLKLWQEtGKQVLLITHDIEEAVFMA-TELVLLSPG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
70-299 |
5.91e-18 |
|
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: 83.82 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAgqlslspRLH--LSGLLEVNGKP---- 143
Cdd:cd03253 1 IEFENVTFAYDPG-----RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-------RFYdvSSGSILIDGQDirev 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 144 -SSSKAYKLAFVRQEDLFFSQlTVRETLSF----AAELQLPEISSAEERDEYVNNLLLKLglvscaDSCVGDakvRG--I 216
Cdd:cd03253 69 tLDSLRRAIGVVPQDTVLFND-TIGYNIRYgrpdATDEEVIEAAKAAQIHDKIMRFPDGY------DTIVGE---RGlkL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 217 SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVICSIHqpRGSVYAKFDDIVLLTEGTLVY 296
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH--RLSTIVNADKIIVLKDGRIVE 215
|
...
gi 15226227 297 AGP 299
Cdd:cd03253 216 RGT 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
88-247 |
6.49e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 83.36 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSL-SPRLHLSGLlEVNGKPSSSKAYK-LAFVRQEDLFFSQLT 165
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQ-DITKLPMHKRARLgIGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPeisSAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:cd03218 92 VEENILAVLEIRGL---SKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
..
gi 15226227 246 LD 247
Cdd:cd03218 164 VD 165
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
89-264 |
7.67e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 85.92 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 89 FLLkNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqLsLSPRlhlSGLLEVNGKP--SSSK-----AYK--LAFVRQEDL 159
Cdd:COG4148 14 FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG-L-ERPD---SGRIRLGGEVlqDSARgiflpPHRrrIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 160 FFSQLTVRETLSFAAElQLPEISSAEERDEYVNnlLLKLG--LvscadscvgDAKVRGISGGEKKRLSLACELIASPSVI 237
Cdd:COG4148 88 LFPHLSVRGNLLYGRK-RAPRAERRISFDEVVE--LLGIGhlL---------DRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180
....*....|....*....|....*..
gi 15226227 238 FADEPTTGLDAFQAEKVMETLQKLAQD 264
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDE 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
91-300 |
8.60e-18 |
|
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: 82.87 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYK-----LAFVRQEDLFFSQL 164
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR-----SGSIRFDGRDiTGLPPHEraragIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELQLPeiSSAEERDEYVNNLLLKLGLVScadscvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:cd03224 91 TVEENLLLGAYARRR--AKRKARLERVYELFPRLKERR-------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 245 GLDAFQAEKVMETLQKLAQDGHTVICsIHQprgsvYAKF-----DDIVLLTEGTLVYAGPA 300
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILL-VEQ-----NARFaleiaDRAYVLERGRVVLEGTA 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
82-276 |
1.09e-17 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 83.09 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 82 KSSKSvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYKLA-----FVR 155
Cdd:TIGR04406 9 KSYKK-RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILIDGQDiTHLPMHERArlgigYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 156 QEDLFFSQLTVRETLSfaAELQLPEISSAEERDEYVNNLLLKLGLVScadscVGDAKVRGISGGEKKRLSLACELIASPS 235
Cdd:TIGR04406 83 QEASIFRKLTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISH-----LRDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPR 276
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR 196
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
101-298 |
1.42e-17 |
|
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: 82.16 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 101 GRLLAIMGPSGSGKTTLLNVLAG-QLSLSPRLHLSGlLEVNGKPSSSKAYKLAFvrQEDLFFSQLTVRETLSFAAElqlP 179
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLING-VDVTAAPPADRPVSMLF--QENNLFAHLTVEQNVGLGLS---P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 180 EISSAEERDEYVNNLLLKLGLVSCadscvgDAKVRG-ISGGEKKRLSLACELIASPSVIFADEPTTGLD-AFQAEKVMET 257
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGL------EKRLPGeLSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226227 258 LQKLAQDGHTVICSIHQPRGSVyAKFDDIVLLTEGTLVYAG 298
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
73-303 |
1.47e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslSPRLHL-SGLLEVNGK-----PSSS 146
Cdd:COG0396 4 KNLHVSVEGKE------ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG----HPKYEVtSGSILLDGEdilelSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYK---LAF---VRqedlfFSQLTVRETLSFAAELQLPEISSAEERDEYVNNLLLKLGL-VSCADSCVGDakvrGISGG 219
Cdd:COG0396 74 RARAgifLAFqypVE-----IPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNE----GFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 220 EKKRLSLACELIASPSVIFADEPTTGLD--AFQaeKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYA 297
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDidALR--IVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHVLVDGRIVKS 222
|
....*.
gi 15226227 298 GpaGKE 303
Cdd:COG0396 223 G--GKE 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
70-298 |
1.58e-17 |
|
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: 82.27 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNItcSLSDKSSKSVrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlHLSGLLEVNGKPSSS--- 146
Cdd:cd03254 3 IEFENV--NFSYDEKKPV---LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-----PQKGQILIDGIDIRDisr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAY--KLAFVRQEDLFFSQlTVRETLSFaaelqlpeiSSAEERDEYVNNLLLKLG-------LVSCADSCVGDAKvRGIS 217
Cdd:cd03254 73 KSLrsMIGVVLQDTFLFSG-TIMENIRL---------GRPNATDEEVIEAAKEAGahdfimkLPNGYDTVLGENG-GNLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 218 GGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLaQDGHTVICSIHQPRGSVYAkfDDIVLLTEGTLVYA 297
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEE 218
|
.
gi 15226227 298 G 298
Cdd:cd03254 219 G 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
88-273 |
1.91e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.70 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY----KLAFVRQEDLFFSQ 163
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD-----AGSISLCGEPVPSRARharqRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVRETLS-FAAELQLpeiSSAEERdEYVNNLLLKLGLVSCADscvgdAKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:PRK13537 95 FTVRENLLvFGRYFGL---SAAAAR-ALVPPLLEFAKLENKAD-----AKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190
....*....|....*....|....*....|..
gi 15226227 243 TTGLDAfQAEKVM-ETLQKLAQDGHTVICSIH 273
Cdd:PRK13537 166 TTGLDP-QARHLMwERLRSLLARGKTILLTTH 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
64-273 |
2.04e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 64 SIRPVTIRWRNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP 143
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKA------VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-----AGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 144 SSSKA----YKLAFVRQEDLFFSQLTVRETL-SFAAELQLpeisSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISG 218
Cdd:PRK13536 105 VPARArlarARIGVVPQFDNLDLEFTVRENLlVFGRYFGM----STREIEAVIPSLLEFARLESKADARVSD-----LSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 219 GEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
91-267 |
2.36e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 81.71 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS---------KAYKLAFVRQEDLFF 161
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT-----SGTVRLAGQDLFAldedararlRARHVGFVFQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAELQlpEISSAEERDEyvnNLLLKLGLVSCAdscvgDAKVRGISGGEKKRLSLACELIASPSVIFADE 241
Cdd:COG4181 103 PTLTALENVMLPLELA--GRRDARARAR---ALLERVGLGHRL-----DHYPAQLSGGEQQRVALARAFATEPAILFADE 172
|
170 180
....*....|....*....|....*.
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQDGHT 267
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFELNRERGT 198
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
70-299 |
3.42e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKssksvrFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK-----PS 144
Cdd:COG4604 2 IEIKNVSKRYGGK------VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLVDGLdvattPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 145 SSKAYKLAFVRQEDLFFSQLTVRETLSFA------AELqlpeisSAEERdEYVNNLLLKLGLVSCADscvgdakvRGI-- 216
Cdd:COG4604 71 RELAKRLAILRQENHINSRLTVRELVAFGrfpyskGRL------TAEDR-EIIDEAIAYLDLEDLAD--------RYLde 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 217 -SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPR-GSVYAkfDDIVLLTEGT 293
Cdd:COG4604 136 lSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINfASCYA--DHIVAMKDGR 213
|
....*.
gi 15226227 294 LVYAGP 299
Cdd:COG4604 214 VVAQGT 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
70-294 |
4.45e-17 |
|
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: 80.98 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY 149
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLV---LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 K-----LAFVRQEDLFFSQlTVRETLSFAaeLQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVRgISGGEKKRL 224
Cdd:cd03248 84 KylhskVSLVGQEPVLFAR-SLQDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQ-LSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 225 SLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDgHTVICSIHqpRGSVYAKFDDIVLLTEGTL 294
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAH--RLSTVERADQILVLDGGRI 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
90-249 |
4.91e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 83.27 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqLsLSPRlhlSGLLEVNGKP----SSSKAYKLAFVRQEDLFFSQLT 165
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-L-ETPD---SGRIVLNGRDlftnLPPRERRVGFVFQHYALFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPeisSAEERDEYVNNLLLKLGLVSCAdscvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:COG1118 92 VAENIAFGLRVRPP---SKAEIRARVEELLELVQLEGLA-----DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
....
gi 15226227 246 LDAF 249
Cdd:COG1118 164 LDAK 167
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
90-310 |
7.36e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVL-------AGQLSLSPR-LHL----SGLLEVNGKPS-SSKAYKLAFVRQ 156
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQtINLvrdkDGQLKVADKNQlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 EDLFFSQLTVRETLsFAAELQLPEISSAEERDEYVNnLLLKLGLvscadscvgDAKVRG-----ISGGEKKRLSLACELI 231
Cdd:PRK10619 100 HFNLWSHMTVLENV-MEAPIQVLGLSKQEARERAVK-YLAKVGI---------DERAQGkypvhLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 232 ASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKfDDIVLLTEGTLVYAGPagkePLTYFGN 310
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVS-SHVIFLHQGKIEEEGA----PEQLFGN 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
73-288 |
1.10e-16 |
|
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: 79.07 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSlsdkssKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRLhlSGLLEVNGKP----SSSKA 148
Cdd:cd03231 4 DELTCE------RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG---LSPPL--AGRVLLNGGPldfqRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 149 YKLAFVRQEDLFFSQLTVRETLSFAAelqlpeissAEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLAC 228
Cdd:cd03231 73 RGLLYLGHAPGIKTTLSVLENLRFWH---------ADHSDEQVEEALARVGL-----NGFEDRPVAQLSAGQQRRVALAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVL 288
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
91-299 |
1.17e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlHLSGLLEVNGKPSSSKAY-KLAFVRQEDLFFSQLTVRET 169
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILA-----PDSGEVLWDGEPLDPEDRrRIGYLPEERGLYPKMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 170 LSFAAEL-QLPEiSSAEERDEYvnnLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDA 248
Cdd:COG4152 92 LVYLARLkGLSK-AEAKRRADE---WLERLGLGDRANK-----KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15226227 249 FQAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAGP 299
Cdd:COG4152 163 VNVELLKDVIRELAAKGTTVIFSSHQ-MELVEELCDRIVIINKGRKVLSGS 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
90-294 |
1.46e-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: 78.03 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS---KAYK--LAFVRQEDLFFSQl 164
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-----SGRVRLDGADISQwdpNELGdhVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVREtlsfaaelqlpeissaeerdeyvnNLLlklglvscadscvgdakvrgiSGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:cd03246 91 SIAE------------------------NIL---------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15226227 245 GLDAFQAEKVMETLQKLAQDGHTVICSIHQPrgSVYAKFDDIVLLTEGTL 294
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
70-274 |
1.89e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 79.16 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAG-QLSLSPRLHLSG--LLEVNGKPSSS 146
Cdd:cd03258 2 IELKNVSKVFGDTGGKVT--ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPTSGSVLVDGtdLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYKLAFVRQEDLFFSQLTVRETLSFAAELqlpEISSAEERDEYVNNLLLKLGLvscADScvGDAKVRGISGGEKKRLSL 226
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEI---AGVPKAEIEERVLELLELVGL---EDK--ADAYPAQLSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQ 274
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHE 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
88-298 |
2.05e-16 |
|
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: 79.07 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAgqlslspRLHL--SGLLEVNGK--PSSSKAY---KLAFVRQEDLF 160
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQ-------RFYVpeNGRVLVDGHdlALADPAWlrrQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQlTVRETLSFAAELQLPE--ISSAEERDEYVNNLLLKLGLvscaDSCVGDAKVrGISGGEKKRLSLACELIASPSVIF 238
Cdd:cd03252 88 FNR-SIRDNIALADPGMSMErvIEAAKLAGAHDFISELPEGY----DTIVGEQGA-GLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 239 ADEPTTGLDaFQAEK-VMETLQKLAqDGHTVICSIHqpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03252 162 FDEATSALD-YESEHaIMRNMHDIC-AGRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
91-264 |
2.09e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.43 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYKLAFVRQE-DLFFSQ-----L 164
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLRKEiGMVFQQpnpfpM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAaeLQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVrGISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:PRK14239 101 SIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSAL-GLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180
....*....|....*....|
gi 15226227 245 GLDAFQAEKVMETLQKLAQD 264
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDD 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
70-329 |
2.16e-16 |
|
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: 79.27 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITcslsdKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAgqlslspRL--HLSGLLEVNGKPSSSK 147
Cdd:cd03295 1 IEFENVT-----KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN-------RLiePTSGEIFIDGEDIREQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 A-----YKLAFVRQEDLFFSQLTVRETLSFaaelqLPEIS--SAEERDEYVNNLllkLGLVSCADSCVGDAKVRGISGGE 220
Cdd:cd03295 69 DpvelrRKIGYVIQQIGLFPHMTVEENIAL-----VPKLLkwPKEKIRERADEL---LALVGLDPAEFADRYPHELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHqprgSVYAKF---DDIVLLTEGTLVY 296
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTH----DIDEAFrlaDRIAIMKNGEIVQ 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 15226227 297 AGpagkepltyfgnfgflCPEHV--NPA-EFLADLI 329
Cdd:cd03295 217 VG----------------TPDEIlrSPAnDFVAEFV 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
73-269 |
2.37e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.30 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKssksvrFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYK- 150
Cdd:COG3842 9 ENVSKRYGDV------TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-----SGRILLDGRDvTGLPPEKr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 151 -LAFVRQEDLFFSQLTVRETLSFAAELQ-LPeissAEERDEYVNNLLLKLGLVScadscVGDAKVRGISGGEKKRLSLAC 228
Cdd:COG3842 78 nVGMVFQDYALFPHLTVAENVAFGLRMRgVP----KAEIRARVAELLELVGLEG-----LADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVI 269
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFI 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
101-298 |
2.59e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 101 GRLLAIMGPSGSGKTTLLNVLAGQLS--LSPRLHLSGL---LEVNGKPS----SSKAYKLAFVRQEDLFfSQLTVRETLS 171
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLITgdKSAGSHIELLgrtVQREGRLArdirKSRANTGYIFQQFNLV-NRLSVLENVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 172 FAAELQLPEISS-----AEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:PRK09984 109 IGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAHQ-----RVSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 247 DAFQAEKVMETLQKLAQ-DGHTVICSIHQPRgsvYA--KFDDIVLLTEGTLVYAG 298
Cdd:PRK09984 184 DPESARIVMDTLRDINQnDGITVVVTLHQVD---YAlrYCERIVALRQGHVFYDG 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
91-295 |
2.71e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.52 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagqlslsPRLHL--SGLLEVNGKPssSKAYKL-------AFVRQEDLFF 161
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLL-------LRFYDptSGRILIDGVD--IRDLTLeslrrqiGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SqLTVRETLSFAAelqlPEISSAE-ER-------DEYVNNllLKLGLvscaDSCVGDakvRGI--SGGEKKRLSLACELI 231
Cdd:COG1132 427 S-GTIRENIRYGR----PDATDEEvEEaakaaqaHEFIEA--LPDGY----DTVVGE---RGVnlSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 232 ASPSVIFADEPTTGLDAFQAEKVMETLQKLAQdGHTVIcSI-HqpRGSVYAKFDDIVLLTEGTLV 295
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK-GRTTI-VIaH--RLSTIRNADRILVLDDGRIV 553
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
91-298 |
3.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQ---------EDLFF 161
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS-----SGRILFDGKPIDYSRKGLMKLREsvgmvfqdpDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQlTVRETLSFAA-ELQLPEissaEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:PRK13636 97 SA-SVYQDVSFGAvNLKLPE----DEVRKRVDNALKRTGI-----EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHD-IDIVPLYCDNVFVMKEGRVILQG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
91-300 |
6.32e-16 |
|
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: 77.71 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYK-----LAFVRQEDLFFSQL 164
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-----SGSIRFDGEDiTGLPPHRiarlgIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELqLPEISSAEERDEYVNNL---LLKLglvscadscvgdAKVRG--ISGGEKKRLSLACELIASPSVIFA 239
Cdd:COG0410 94 TVEENLLLGAYA-RRDRAEVRADLERVYELfprLKER------------RRQRAgtLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLAQDGHTVICsIHQprgsvYAKF-----DDIVLLTEGTLVYAGPA 300
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILL-VEQ-----NARFaleiaDRAYVLERGRIVLEGTA 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
91-295 |
6.74e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 77.24 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRlhlSGLLEVNG------KPSSSKAyKLAFVRQE-DLFFSq 163
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK--PT---SGSVLLDGtdirqlDPADLRR-NIGYVPQDvTLFYG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 lTVRETLSFAAelqlPEISSAE-----ER---DEYVNNLllKLGLvscaDSCVGDaKVRGISGGEKKRLSLACELIASPS 235
Cdd:cd03245 93 -TLRDNITLGA----PLADDERilraaELagvTDFVNKH--PNGL----DLQIGE-RGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKLAQDgHTVICSIHQPrgSVYAKFDDIVLLTEGTLV 295
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRP--SLLDLVDRIIVMDSGRIV 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
61-298 |
7.13e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 7.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 61 GGDSIRPVTIRWRNITCSLSDKSSKsvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVN 140
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQPQP----VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-----QGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 141 GKPSSskAYKLAFVRQEDLFFSQL------TVRETLSFAAelqlPEISsaeerDEYVNNLLLKLGLVSCADSCVG-DAKV 213
Cdd:PRK11160 401 GQPIA--DYSEAALRQAISVVSQRvhlfsaTLRDNLLLAA----PNAS-----DEALIEVLQQVGLEKLLEDDKGlNAWL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 214 ----RGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDgHTVICSIHQPRGsvYAKFDDIVLL 289
Cdd:PRK11160 470 geggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-KTVLMITHRLTG--LEQFDRICVM 546
|
....*....
gi 15226227 290 TEGTLVYAG 298
Cdd:PRK11160 547 DNGQIIEQG 555
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
91-274 |
8.50e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.44 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLL---NVL----AGQLslsprlhLSGLLEVNGKPSSSKAYKL--AFVRQEDLFF 161
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLeeitSGDL-------IVDGLKVNDPKVDERLIRQeaGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAeLQLPEISSAEERDEyVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADE 241
Cdd:PRK09493 90 PHLTALENVMFGP-LRVRGASKEEAEKQ-ARELLAKVGLAERAHHYPSE-----LSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQ 274
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
90-306 |
1.44e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.26 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKpsssKAYKLAFV---RQEDLFFS---- 162
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQ----DIFKMDVIelrRRVQMVFQipnp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 --QLTVRETLSFAAELQLPeISSAEERDEYVNNLLLKLGLVSCADSCVgDAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:PRK14247 94 ipNLSIFENVALGLKLNRL-VKSKKELQERVRWALEKAQLWDEVKDRL-DAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDgHTVICSIHQPRGSvyAKFDDIV-LLTEGTLVYAGPAgKEPLT 306
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQA--ARISDYVaFLYKGQIVEWGPT-REVFT 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
91-298 |
1.48e-15 |
|
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: 76.51 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYKLAF--VRQEDLFFSQLTVR 167
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-----SGEILLDGKDiTNLPPHKRPVntVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAaeLQLPEISSAEERDEyVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:cd03300 91 ENIAFG--LRLKKLPKAEIKER-VAEALDLVQLEGYANR-----KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 248 AFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03300 163 LKLRKDMQLELKRLQKElGITFVFVTHD-QEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
97-302 |
1.53e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 76.33 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 97 EAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKA-YK--LAFVRQEDLFFSQLTVRET--LS 171
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPD-----SGRILWNGQDLTALPpAErpVSMLFQENNLFPHLTVAQNigLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 172 FAAELQLpeisSAEERDEyVNNLLLKLGLVSCadscvGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD-AFQ 250
Cdd:COG3840 96 LRPGLKL----TAEQRAQ-VEQALERVGLAGL-----LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 251 AEkvMETL-QKLAQD-GHTVICSIHQPRGSvyAKF-DDIVLLTEGTLVYAGPAGK 302
Cdd:COG3840 166 QE--MLDLvDELCRErGLTVLMVTHDPEDA--ARIaDRVLLVADGRIAADGPTAA 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
90-248 |
2.11e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.20 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlHLSGLLEVNGKPSS---SKAYKLAFVRQEDLFFSQLTV 166
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH-----QTSGHIRFHGTDVSrlhARDRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFAAELqLP--EISSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:PRK10851 92 FDNIAFGLTV-LPrrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLLDEPFG 165
|
....
gi 15226227 245 GLDA 248
Cdd:PRK10851 166 ALDA 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
91-299 |
3.11e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK-PSSSKAyklAFVRQEDLFFSQ------ 163
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT-----SGEVRVLGYvPFKRRK---EFARRIGVVFGQrsqlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 -LTVRETLSFAAEL-QLPEISSAEERDEYVNnlLLKLG--LvscadscvgDAKVRGISGGEKKRlslaCELIAS----PS 235
Cdd:COG4586 110 dLPAIDSFRLLKAIyRIPDAEYKKRLDELVE--LLDLGelL---------DTPVRQLSLGQRMR----CELAAAllhrPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKL-AQDGHTVICSIHqprgsvYakFDDI-------VLLTEGTLVYAGP 299
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSH------D--MDDIealcdrvIVIDHGRIIYDGS 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
88-299 |
3.24e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.59 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY-----KLAFVRQE-DLFF 161
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-----AGTITVGGMVLSEETVwdvrrQVGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAElqlpeiSSAEERDEYVNNLLLKLGLVSCADscVGDAKVRGISGGEKKRLSLACELIASPSVIFADE 241
Cdd:PRK13635 95 VGATVQDDVAFGLE------NIGVPREEMVERVDQALRQVGMED--FLNREPHRLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 242 PTTGLDAFQAEKVMETLQKL-AQDGHTVICSIHQPRGSvyAKFDDIVLLTEGTLVYAGP 299
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEA--AQADRVIVMNKGEILEEGT 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
90-294 |
4.83e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS---------KAYKLAFVRQEDLF 160
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-----SGEVSLVGQPLHQmdeearaklRAKHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLsfaaelQLPEI----SSAEERDEYVNnLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSV 236
Cdd:PRK10584 100 IPTLNALENV------ELPALlrgeSSRQSRNGAKA-LLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 237 IFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPRgsVYAKFDDIVLLTEGTL 294
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQ--LAARCDRRLRLVNGQL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
73-300 |
5.33e-15 |
|
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: 74.10 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslsprlhLSGLLEVNGKpssskayklA 152
Cdd:cd03217 4 KDLHVSVGGKE------ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---------HPKYEVTEGE---------I 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 153 FVRQEDLffSQLTVRE------TLSFAAELQLPEISsaeerdeyVNNLLLKLGLvscadscvgdakvrGISGGEKKRLSL 226
Cdd:cd03217 60 LFKGEDI--TDLPPEErarlgiFLAFQYPPEIPGVK--------NADFLRYVNE--------------GFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
73-275 |
6.75e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRlhLSGLLEVNGKPssskaykLA 152
Cdd:PRK13538 5 RNLACERDE------RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG---LARP--DAGEVLWQGEP-------IR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 153 FVRQE---DLFF--------SQLTVRETLSFAAELqlpeisSAEERDEYVNNLLLKLGLVScadscVGDAKVRGISGGEK 221
Cdd:PRK13538 67 RQRDEyhqDLLYlghqpgikTELTALENLRFYQRL------HGPGDDEALWEALAQVGLAG-----FEDVPVRQLSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 222 KRLSLACELIASPSVIFADEPTTGLDAfQAEKVMETL--QKLAQDGhTVICSIHQP 275
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDK-QGVARLEALlaQHAEQGG-MVILTTHQD 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
86-269 |
7.13e-15 |
|
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: 73.24 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 86 SVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP----SSSKAYK--LAFV---RQ 156
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-----SGEITLDGKPvtrrSPRDAIRagIAYVpedRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 EDLFFSQLTVREtlsfaaelqlpeissaeerdeyvnNLLLKLGLvscadscvgdakvrgiSGGEKKRLSLACELIASPSV 236
Cdd:cd03215 86 REGLVLDLSVAE------------------------NIALSSLL----------------SGGNQQKVVLARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 237 IFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
91-269 |
7.92e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 76.65 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK---LAFVRQEDLFFSQLTVR 167
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT-----SGEILIGGRDVTDLPPKdrnIAMVFQSYALYPHMTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQ-LPeissAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGL 246
Cdd:COG3839 94 ENIAFPLKLRkVP----KAEIDRRVREAAELLGLEDLLDR-----KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180
....*....|....*....|....
gi 15226227 247 DAFQAEKVMETLQKLAQD-GHTVI 269
Cdd:COG3839 165 DAKLRVEMRAEIKRLHRRlGTTTI 188
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
90-261 |
9.53e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.08 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-----SSSKA----YKLAFVRQEDLF 160
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT-----SGDVIFNGQPmsklsSAAKAelrnQKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLSfaaelqLPEISSAEERDEYVNNLLLKLGLVSCADScvGDAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:PRK11629 99 LPDFTALENVA------MPLLIGKKKPAEINSRALEMLAAVGLEHR--ANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180
....*....|....*....|.
gi 15226227 241 EPTTGLDAFQAEKVMETLQKL 261
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGEL 191
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
91-273 |
1.08e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 74.26 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPrlHLSGLLEVNGKPSSSKAYKLAFVRQE--------DLfFS 162
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL---LEE--PDSGTITVDGEDLTDSKKDINKLRRKvgmvfqqfNL-FP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLSFAaelqlPEIS---SAEERDEYVNNLLLKLGLvscADSCvgDAKVRGISGGEKKRLSLACELIASPSVIFA 239
Cdd:COG1126 91 HLTVLENVTLA-----PIKVkkmSKAEAEERAMELLERVGL---ADKA--DAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 15226227 240 DEPTTGLDafqAEKVME---TLQKLAQDGHTVICSIH 273
Cdd:COG1126 161 DEPTSALD---PELVGEvldVMRDLAKEGMTMVVVTH 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-273 |
1.10e-14 |
|
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: 78.52 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 46 PEDEAEDDYAETED---GGGDsiRPVTIRWRNITCSLSDKSSKSVRFLLKNVsgeaKPGRLLAIMGPSGSGKTTLLNVLA 122
Cdd:TIGR01257 1913 PIFDEDDDVAEERQriiSGGN--KTDILRLNELTKVYSGTSSPAVDRLCVGV----RPGECFGLLGVNGAGKTTTFKMLT 1986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 123 GQLSLSprlhlSGLLEVNGKP---SSSKAYK-LAFVRQEDLFFSQLTVRETLSFAAELQ-LPeissAEERDEYVNNLLLK 197
Cdd:TIGR01257 1987 GDTTVT-----SGDATVAGKSiltNISDVHQnMGYCPQFDAIDDLLTGREHLYLYARLRgVP----AEEIEKVANWSIQS 2057
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 198 LGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLDAfQAEKVM-ETLQKLAQDGHTVICSIH 273
Cdd:TIGR01257 2058 LGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP-QARRMLwNTIVSIIREGRAVVLTSH 2128
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
90-318 |
1.36e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.11 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYKLAFVRQE--DLF-----FS 162
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRREvgMVFqypnpFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLSFAAELQlPEISSAEERDEYVNNLLLKLGLVSCADSCVGDaKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:PRK14267 99 HLTIYDNVAIGVKLN-GLVKSKKELDERVEWALKKAALWDEVKDRLND-YPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQDgHTVICSIHQPRGSvyAKFDDIV-LLTEGTLVYAGPAGKepltYFGNfgflcPEH 318
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQA--ARVSDYVaFLYLGKLIEVGPTRK----VFEN-----PEH 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
69-274 |
2.41e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 69 TIRWRNITCSLSDKSSksvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagQLSLSPRlhlSGLLEVNG------- 141
Cdd:COG4161 2 SIQLKNINCFYGSHQA------LFDINLECPSGETLVLLGPSGAGKSSLLRVL--NLLETPD---SGQLNIAGhqfdfsq 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 142 KPSSSKAYKLafvRQE-DLFFSQ------LTVRETLsFAAELQLPEISSAEERDEyVNNLLLKLGLVSCADscvgdAKVR 214
Cdd:COG4161 71 KPSEKAIRLL---RQKvGMVFQQynlwphLTVMENL-IEAPCKVLGLSKEQAREK-AMKLLARLRLTDKAD-----RFPL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 215 GISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQ 274
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
91-273 |
2.74e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 72.29 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK---PSSSKAYKLAFVRQEDLFFSQLTVR 167
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-----SGRIYIGGRdvtDLPPKDRDIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQlpeISSAEERDEYVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:cd03301 91 DNIAFGLKLR---KVPKDEIDERVREVAELLQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180
....*....|....*....|....*..
gi 15226227 248 AFQAEKVMETLQKLAQD-GHTVICSIH 273
Cdd:cd03301 163 AKLRVQMRAELKRLQQRlGTTTIYVTH 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
97-258 |
3.23e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 97 EAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK-----PSSSKAYKLAFvrQEDLFFSQLTVRET-- 169
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPA-----SGSLTLNGQdhtttPPSRRPVSMLF--QENNLFSHLTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 170 LSFAAELQLpeisSAEERDEyVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLD-A 248
Cdd:PRK10771 94 LGLNPGLKL----NAAQREK-LHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDEPFSALDpA 163
|
170
....*....|
gi 15226227 249 FQAEkvMETL 258
Cdd:PRK10771 164 LRQE--MLTL 171
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
88-299 |
3.38e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLH---LSGLLEVNGKP-SSSKAYKLAFVR-------Q 156
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarVTGDVTLNGEPlAAIDAPRLARLRavlpqaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 EDLFFSqltVRETLSFAAELQLPEISSAEERDEYVNNLLLKLglvSCADSCVGdAKVRGISGGEKKRLSLACEL------ 230
Cdd:PRK13547 94 PAFAFS---AREIVLLGRYPHARRAGALTHRDGEIAWQALAL---AGATALVG-RDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 231 ---IASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHT-VICSIHQPR-GSVYAkfDDIVLLTEGTLVYAGP 299
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHA--DRIAMLADGAIVAHGA 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
88-260 |
3.47e-14 |
|
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: 70.17 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlhlsgllEVNGKPSSSKAYKLAfvrqedlFFSQLtvr 167
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE-----------PDEGIVTWGSTVKIG-------YFEQL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 etlsfaaelqlpeissaeerdeyvnnlllklglvscadscvgdakvrgiSGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:cd03221 72 -------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170
....*....|...
gi 15226227 248 AFQAEKVMETLQK 260
Cdd:cd03221 103 LESIEALEEALKE 115
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
55-275 |
4.77e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.61 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 55 AETEDGGGDSIRPV---TIRWRNITCSLSDKssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPrl 131
Cdd:COG4178 345 ADALPEAASRIETSedgALALEDLTLRTPDG-----RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---LWP-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 132 HLSGLLEVngkPSSSKAyklafvrqedLFFSQL------TVRETLSF-AAELQLPeissaeerDEYVNNLLLKLGLVSCA 204
Cdd:COG4178 415 YGSGRIAR---PAGARV----------LFLPQRpylplgTLREALLYpATAEAFS--------DAELREALEAVGLGHLA 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 205 DSCvgDAKV---RGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGhTVIcSI-HQP 275
Cdd:COG4178 474 ERL--DEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVI-SVgHRS 544
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
88-276 |
4.82e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRLhlSGLLEVNGK-----PSSSKAYK-LAFVRQEDLFF 161
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG---IVPRD--AGNIIIDDEdisllPLHARARRgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLsfAAELQLPEISSAEERDEYVNNLLLKLGLVSCADScVGDAkvrgISGGEKKRLSLACELIASPSVIFADE 241
Cdd:PRK10895 91 RRLSVYDNL--MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDS-MGQS----LSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190
....*....|....*....|....*....|....*
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPR 276
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
105-300 |
8.45e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.61 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 105 AIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK--PSSSKAY-------KLAFVRQEDLFFSQLTVRETLSFAAE 175
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPD-----EGEIVLNGRtlFDSRKGIflppekrRIGYVFQEARLFPHLSVRGNLRYGMK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 176 LQLPEisSAEERDEYVNNLLlklGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVM 255
Cdd:TIGR02142 102 RARPS--ERRISFERVIELL---GIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15226227 256 ETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
85-298 |
1.16e-13 |
|
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: 71.03 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 85 KSVRF---------LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAgqlslspRLH--LSGLLEVNGKPSSS---KAY- 149
Cdd:cd03249 4 KNVSFrypsrpdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-------RFYdpTSGEILLDGVDIRDlnlRWLr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 -KLAFVRQEDLFFSQlTVRETLSF----AAELQLPEISSAEERDEYVNNLLLKLglvscaDSCVGDakvRG--ISGGEKK 222
Cdd:cd03249 77 sQIGLVSQEPVLFDG-TIAENIRYgkpdATDEEVEEAAKKANIHDFIMSLPDGY------DTLVGE---RGsqLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 223 RLSLACELIASPSVIFADEPTTGLDAfQAEK-VMETLQKLAQdGHTVICSIHqpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDA-ESEKlVQEALDRAMK-GRTTIVIAH--RLSTIRNADLIAVLQNGQVVEQG 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
70-273 |
1.47e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTL---LNVLagqlsLSPRlhlSGLLEVNGKPSSS 146
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELK-ALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNAL-----LLPD---TGTIEWIFKDEKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYKLAFVRQEDLFFSQLTVRETLSFA-------------AELQLPE-----------IS---SAEERDEYVNNLLLKLG 199
Cdd:PRK13651 74 KKKTKEKEKVLEKLVIQKTRFKKIKKIkeirrrvgvvfqfAEYQLFEqtiekdiifgpVSmgvSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 200 LvscaDSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:PRK13651 154 L----DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
68-299 |
1.60e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 68 VTIRWRNITCSLSDKSSKsvrfllknVSGeakpGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSsK 147
Cdd:PRK15056 12 VTVTWRNGHTALRDASFT--------VPG----GSIAALVGVNGSGKSTLFKALMGFVRLA-----SGKISILGQPTR-Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYK---LAFVRQE---DLFFSQLtVRETLSFAAELQLPEISSAEERD-EYVNNLLLKLGLVSCADSCVGDakvrgISGGE 220
Cdd:PRK15056 74 ALQknlVAYVPQSeevDWSFPVL-VEDVVMMGRYGHMGWLRRAKKRDrQIVTAALARVDMVEFRHRQIGE-----LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQpRGSVyAKFDDIVLLTEGTLVYAGP 299
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN-LGSV-TEFCDYTVMVKGTVLASGP 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
84-261 |
2.03e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSV--RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLsprlhLSGLLEVngkpssSKAYKLAFVRQE-DLF 160
Cdd:COG0488 322 SKSYgdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP-----DSGTVKL------GETVKIGYFDQHqEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLSFAAElqlpeissaEERDEYVNNLLLKLGLvSCADScvgDAKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:COG0488 391 DPDKTVLDELRDGAP---------GGTEQEVRGYLGRFLF-SGDDA---FKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180
....*....|....*....|.
gi 15226227 241 EPTTGLDafqaekvMETLQKL 261
Cdd:COG0488 458 EPTNHLD-------IETLEAL 471
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
69-298 |
3.85e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.69 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 69 TIRWRNITCSLSDKSSKsvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagQLSLSPRlhlSGLLEVNGK-----P 143
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQG-----VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDPQ---SGRILIDGTdirtvT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 144 SSSKAYKLAFVRQEDLFFSQlTVRETLSFAAELQLP-EISSAEERDEYVNNLLLKLGlvsCADSCVGDakvRG--ISGGE 220
Cdd:PRK13657 404 RASLRRNIAVVFQDAGLFNR-SIEDNIRVGRPDATDeEMRAAAERAQAHDFIERKPD---GYDTVVGE---RGrqLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSiHqpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA-H--RLSTVRNADRILVFDNGRVVESG 551
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
91-295 |
4.29e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 69.06 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY-----KLAFVRQEDLFFSQlT 165
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDISKIGLhdlrsRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPEISSAEER---DEYVNNLLLKLGLVSCADSCvgdakvrGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:cd03244 94 IRSNLDPFGEYSDEELWQALERvglKEFVESLPGGLDTVVEEGGE-------NLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15226227 243 TTGLDAFQAEKVMETLQKlAQDGHTVICSIHqpRGSVYAKFDDIVLLTEGTLV 295
Cdd:cd03244 167 TASVDPETDALIQKTIRE-AFKDCTVLTIAH--RLDTIIDSDRILVLDKGRVV 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
84-273 |
4.59e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSV---RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlhlsgllEVNGKPSSSKAYKLAFVRQEDLF 160
Cdd:TIGR03719 11 SKVVppkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----------DFNGEARPQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLSFA-AELQ-----LPEISS--AEERDEY------------------VNNLLLKLGLVSCADSC-VGDAKV 213
Cdd:TIGR03719 80 DPTKTVRENVEEGvAEIKdaldrFNEISAkyAEPDADFdklaaeqaelqeiidaadAWDLDSQLEIAMDALRCpPWDADV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 214 RGISGGEKKRLSLACELIASPSVIFADEPTTGLDafqAEKVMETLQKLAQDGHTVICSIH 273
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
88-275 |
6.16e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlhlsgllevnGKPSSSKayklaFVRQEDLFFSQLTVR 167
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--------------GTPVAGC-----VDVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 EtlsfaaelQLPEISSAEERDEYVNNlllkLGLvscADSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:COG2401 104 D--------AIGRKGDFKDAVELLNA----VGL---SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*....
gi 15226227 248 AFQAEKVMETLQKLAQD-GHTVICSIHQP 275
Cdd:COG2401 169 RQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
91-269 |
6.51e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP----SSSKAYKL--AFVRQEDLFFSQL 164
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD-----SGEILIDGKPvrirSPRDAIALgiGMVHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAE-LQLPEISSAEERDEyVNNLLLKLGL-VSCadscvgDAKVRGISGGEKKR------LSLACELIaspsv 236
Cdd:COG3845 96 TVAENIVLGLEpTKGGRLDRKAARAR-IRELSERYGLdVDP------DAKVEDLSVGEQQRveilkaLYRGARIL----- 163
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 237 IFaDEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:COG3845 164 IL-DEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
88-247 |
6.84e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKA-YK-----LAFVRQEDLFF 161
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGRIFLDGEDITHLPmHKrarlgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAELQLPeisSAEERDEYVNNLLLKLGLVSCADScvgdakvRGI--SGGEKKRLSLACELIASPSVIFA 239
Cdd:COG1137 91 RKLTVEDNILAVLELRKL---SKKEREERLEELLEEFGITHLRKS-------KAYslSGGERRRVEIARALATNPKFILL 160
|
....*...
gi 15226227 240 DEPTTGLD 247
Cdd:COG1137 161 DEPFAGVD 168
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
70-298 |
9.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNvlagqlslsprlHLSGLLEVN-GKPSSSKA 148
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELV-ALNNISYTFEKNKIYFIIGNSGSGKSTLVT------------HFNGLIKSKyGTIQVGDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 149 Y---KLAFVRQEDLFFSQLT-----VRETLSFAaeLQLPEIS-------------------SAEERDEYVNNLLLKLGLv 201
Cdd:PRK13631 89 YigdKKNNHELITNPYSKKIknfkeLRRRVSMV--FQFPEYQlfkdtiekdimfgpvalgvKKSEAKKLAKFYLNKMGL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 202 scaDSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYA 281
Cdd:PRK13631 166 ---DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLE 241
|
250
....*....|....*..
gi 15226227 282 KFDDIVLLTEGTLVYAG 298
Cdd:PRK13631 242 VADEVIVMDKGKILKTG 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
88-275 |
1.08e-12 |
|
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: 66.41 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPrlHLSGLLevnGKPSSSkayKLAFVRQEDlFFSQLTVR 167
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG---LWP--WGSGRI---GMPEGE---DLLFLPQRP-YLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQLpeissaeerdeyvnnlllklglvscadscvgdakvrgiSGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:cd03223 82 EQLIYPWDDVL--------------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*....
gi 15226227 248 AFQAEKVMETLQKLaqdGHTVIcSI-HQP 275
Cdd:cd03223 124 EESEDRLYQLLKEL---GITVI-SVgHRP 148
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
91-269 |
1.12e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK------PSSSKAYKLAFVRQEDLFFSQL 164
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-----SGEILLDGEpvrfrsPRDAQAAGIAIIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAEL-QLPEISSAEERDEyVNNLLLKLGL-VScadscvGDAKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:COG1129 95 SVAENIFLGREPrRGGLIDWRAMRRR-ARELLARLGLdID------PDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180
....*....|....*....|....*..
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:COG1129 168 TASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
91-299 |
1.23e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLnvlagqlslsprLHLSGL-------LEVNGKPSSSKAYK-------LAFVRQ 156
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLL------------LHLNGIylpqrgrVKVMGREVNAENEKwvrskvgLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 EDLFFSQlTVRETLSFAA-ELQLpeisSAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPS 235
Cdd:PRK13647 89 DDQVFSS-TVWDDVAFGPvNMGL----DKDEVERRVEEALKAVRMWDFRDK-----PPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSV-YAkfDDIVLLTEG-TLVYAGP 299
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAeWA--DQVIVLKEGrVLAEGDK 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
91-269 |
1.46e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 68.14 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYKLAFVRQE-DLFFSQ-----L 164
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDVDVVELRRRvGMVFQKpnpfpK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELQlpEISSAEERDEYVNNLLLKLGL---VscadscvgdaKVR------GISGGEKKRLSLACELIASPS 235
Cdd:COG1117 107 SIYDNVAYGLRLH--GIKSKSELDEIVEESLRKAALwdeV----------KDRlkksalGLSGGQQQRLCIARALAVEPE 174
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKLAQDgHTVI 269
Cdd:COG1117 175 VLLMDEPTSALDPISTAKIEELILELKKD-YTIV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
70-298 |
1.67e-12 |
|
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: 70.60 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAG-------------QLSLSPRLHLSGL 136
Cdd:TIGR03269 1 IEVKNLTKKFDGKE------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyHVALCEKCGYVER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 137 LEVNGKP-----SSSKAYKLAFVRQEDLFFSQLTVRETLSFAAELQLPE--------ISSAEE----RDEYVNNLLLKLG 199
Cdd:TIGR03269 75 PSKVGEPcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddtvldnvLEALEEigyeGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 200 LVSCADSCVGDAkvRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPRgs 278
Cdd:TIGR03269 155 MVQLSHRITHIA--RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPE-- 230
|
250 260
....*....|....*....|.
gi 15226227 279 VYAKFDD-IVLLTEGTLVYAG 298
Cdd:TIGR03269 231 VIEDLSDkAIWLENGEIKEEG 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-328 |
2.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 100 PGR-LLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYKLAFVRQEDLFFSQ-----LTVRETLsfA 173
Cdd:PRK14271 45 PARaVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRpnpfpMSIMDNV--L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 174 AELQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVRgISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEK 253
Cdd:PRK14271 123 AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 254 VMETLQKLAqDGHTVICSIHQPRGSVYAKfDDIVLLTEGTLVYAGPAgkEPLtyfgnfgFLCPEHVNPAEFLADL 328
Cdd:PRK14271 202 IEEFIRSLA-DRLTVIIVTHNLAQAARIS-DRAALFFDGRLVEEGPT--EQL-------FSSPKHAETARYVAGL 265
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
91-295 |
5.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.16 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK----PSSSKAYK-------LAFVRQEDL 159
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS-----SGTITIAGYhitpETGNKNLKklrkkvsLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 160 FFSQlTVRETLSFAAelqLPEISSAEERDEYVNNLLLKLGLvscaDSCVGDAKVRGISGGEKKRLSLACELIASPSVIFA 239
Cdd:PRK13641 98 LFEN-TVLKDVEFGP---KNFGFSEDEAKEKALKWLKKVGL----SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRG-SVYAkfDDIVLLTEGTLV 295
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDvAEYA--DDVLVLEHGKLI 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
102-298 |
5.18e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 102 RLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSK----AYKLAFVRQEDLFFSQLTVRETLSFAAELQ 177
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPT-----SGTVLVGGKDIETNldavRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 178 LpeiSSAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMET 257
Cdd:TIGR01257 1032 G---RSWEEAQLEMEAMLEDTGLHHKRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226227 258 LQKLaQDGHTVICSIHQPRGSVYAKfDDIVLLTEGTLVYAG 298
Cdd:TIGR01257 1104 LLKY-RSGRTIIMSTHHMDEADLLG-DRIAIISQGRLYCSG 1142
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
82-299 |
5.30e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 82 KSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP----SSSKAYKLA--FVR 155
Cdd:PRK15439 19 KQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-----SGTLEIGGNPcarlTPAKAHQLGiyLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 156 QEDLFFSQLTVRETLSFAaelqLPEISSAEERdeyVNNLLLKLGL-----VSCADSCVGDAKVRGISGGekkrlslaceL 230
Cdd:PRK15439 93 QEPLLFPNLSVKENILFG----LPKRQASMQK---MKQLLAALGCqldldSSAGSLEVADRQIVEILRG----------L 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 231 IASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYAKFDDIVLLTEGTLVYAGP 299
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGK 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
90-300 |
6.64e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPrlhLSG--------LLEVNGKPSSSKAYKLAF-------- 153
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKI---LEGdilfkgesILDLEPEERAHLGIFLAFqypieipg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 154 VRQEDlfFSQLTVRETLSFaaeLQLPEISSAEERdEYVNNlllKLGLVSCADSCVGDAKVRGISGGEKKR---LSLAcel 230
Cdd:CHL00131 99 VSNAD--FLRLAYNSKRKF---QGLPELDPLEFL-EIINE---KLKLVGMDPSFLSRNVNEGFSGGEKKRneiLQMA--- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 231 IASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDA 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
91-299 |
6.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.99 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQE-DLFFS----QL- 164
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-----SGKIIIDGVDITDKKVKLSDIRKKvGLVFQypeyQLf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 --TVRETLSFAAelqlpeISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:PRK13637 98 eeTIEKDIAFGP------INLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQPRGsvYAKF-DDIVLLTEGTLVYAGP 299
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMED--VAKLaDRIIVMNKGKCELQGT 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
91-247 |
7.84e-12 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 66.13 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS---------KAYKLAFVRQEDLFF 161
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT-----SGKVLIDGQDIAAmsrkelrelRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAELQ-LPEissaEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:cd03294 115 PHRTVLENVAFGLEVQgVPR----AEREERAAEALELVGLEGWEHK-----YPDELSGGMQQRVGLARALAVDPDILLMD 185
|
....*..
gi 15226227 241 EPTTGLD 247
Cdd:cd03294 186 EAFSALD 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
49-294 |
8.75e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 49 EAEDDYAETEDGGGDSIRPVTIRWRNITcslsDKSSKSVRfllkNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLS 128
Cdd:PRK09700 245 ELQNRFNAMKENVSNLAHETVFEVRNVT----SRDRKKVR----DISFSVCRGEILGFAGLVGSGRTELMNCLFG---VD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 129 PRLhlSGLLEVNGK---PSSS-KAYK--LAFV---RQEDLFFSQLTVRETLSFAAELQLPEISSA----EERDE--YVNN 193
Cdd:PRK09700 314 KRA--GGEIRLNGKdisPRSPlDAVKkgMAYItesRRDNGFFPNFSIAQNMAISRSLKDGGYKGAmglfHEVDEqrTAEN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 194 LLLKLGLvSCADScvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI-CSI 272
Cdd:PRK09700 392 QRELLAL-KCHSV---NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSS 467
|
250 260
....*....|....*....|..
gi 15226227 273 HQPRgsVYAKFDDIVLLTEGTL 294
Cdd:PRK09700 468 ELPE--IITVCDRIAVFCEGRL 487
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
89-298 |
1.12e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.93 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 89 FLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK-------LAFVRQEDLFF 161
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-----SGEIFYNNQAITDDNFEklrkhigIVFQNPDNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQlTVRETLSFAAELQLpeiSSAEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADE 241
Cdd:PRK13648 98 GS-IVKYDVAFGLENHA---VPYDEMHRRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 242 PTTGLDAFQAEKVMETLQKLAQDGHTVICSI-HQPRGSVYAkfDDIVLLTEGTLVYAG 298
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISItHDLSEAMEA--DHVIVMNKGTVYKEG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
90-302 |
1.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSL-SPRLHLSGLLEVNGKPS-SSKAYKL----AFVRQEDLFFSQ 163
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYFGKDIfQIDAIKLrkevGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVRETLSFAaeLQLPEISSAEERDEYVNNLLLKLGLVSCADSCVgDAKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:PRK14246 105 LSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSiHQPRGSVYAKfDDIVLLTEGTLVYAGPAGK 302
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVA-DYVAFLYNGELVEWGSSNE 238
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
91-283 |
1.28e-11 |
|
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: 63.88 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagqLSLSPRLHLSGLLEVNGKPssskayKLAFVRQedlffsqltvretL 170
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKFSRN------KLIFIDQ-------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAAELQLpeissaeerdEYvnnllLKLGlvscadscvgdAKVRGISGGEKKRLSLACELIASP--SVIFADEPTTGLDA 248
Cdd:cd03238 69 QFLIDVGL----------GY-----LTLG-----------QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQ 122
|
170 180 190
....*....|....*....|....*....|....*
gi 15226227 249 FQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKF 283
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADW 157
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
85-274 |
1.75e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.59 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 85 KSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK-------LAFVRQE 157
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT-----SGSVLIRGEPITKENIRevrkfvgLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 158 DLFFSQlTVRETLSFA-AELQLPEISSAEErdeyVNNLLLKLGLvscadSCVGDAKVRGISGGEKKRLSLACELIASPSV 236
Cdd:PRK13652 89 DQIFSP-TVEQDIAFGpINLGLDEETVAHR----VSSALHMLGL-----EELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 15226227 237 IFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQ 274
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
91-295 |
1.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAyKLAFVRQ------------ED 158
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-----TGTVTVDDITITHKT-KDKYIRPvrkrigmvfqfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 159 LFFSQLTVRETLSFAAELQLPeissAEERDEYVNNLLLKLGLvscaDSCVGDAKVRGISGGEKKRLSLACELIASPSVIF 238
Cdd:PRK13646 97 QLFEDTVEREIIFGPKNFKMN----LDEVKNYAHRLLMDLGF----SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 239 ADEPTTGLDAFQAEKVMETLQKLA-QDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLV 295
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSIV 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
70-298 |
2.00e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITcslsdKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY 149
Cdd:PRK09700 6 ISMAGIG-----KSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-----KGTITINNINYNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 KLA------FVRQEDLFFSQLTVRETLsFAAELQ------LPEISSAEERdEYVNNLLLKLGLVSCADSCVGDakvrgIS 217
Cdd:PRK09700 75 KLAaqlgigIIYQELSVIDELTVLENL-YIGRHLtkkvcgVNIIDWREMR-VRAAMMLLRVGLKVDLDEKVAN-----LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 218 GGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGhTVICSIHQPRGSVYAKFDDIVLLTEGTLVYA 297
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEG-TAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
|
.
gi 15226227 298 G 298
Cdd:PRK09700 227 G 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
71-298 |
2.87e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 63.71 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 71 RWRNITCSLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYK 150
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-----SGTVTVRGRVSSLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 151 LAFVrqedlffSQLTVRETLSF-AAELQLpeisSAEERDEYVNnlllklglvSCADSC----VGDAKVRGISGGEKKRLS 225
Cdd:cd03220 93 GGFN-------PELTGRENIYLnGRLLGL----SRKEIDEKID---------EIIEFSelgdFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226227 226 LACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgSVYAKFDDIVLLTEGTLVYAG 298
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS-SIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
91-269 |
2.89e-11 |
|
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: 62.45 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK------PSSSKAYKLAFVrqedlffSQL 164
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-----SGEILVDGKevsfasPRDARRAGIAMV-------YQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVretlsfaAELQLPEIssaeerdeyvnnlllklglvscADSCVGDAKVrgisggekkrlslaceliaspsVIFaDEPTT 244
Cdd:cd03216 84 SV-------GERQMVEI----------------------ARALARNARL----------------------LIL-DEPTA 111
|
170 180
....*....|....*....|....*
gi 15226227 245 GLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVI 136
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
70-325 |
2.91e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.62 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKsvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLlnvlagqlslspRLHLSGLLEVN--------- 140
Cdd:PRK13644 2 IRLENVSYSYPDGTPA-----LENINLVIKKGEYIGIIGKNGSGKSTL------------ALHLNGLLRPQkgkvlvsgi 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 141 --GKPSS----SKAYKLAFVRQEDLFFSQlTVRETLSFAAE-LQLPEIssaeERDEYVNNLLLKLGLvscadscvgdAKV 213
Cdd:PRK13644 65 dtGDFSKlqgiRKLVGIVFQNPETQFVGR-TVEEDLAFGPEnLCLPPI----EIRKRVDRALAEIGL----------EKY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 214 R-----GISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAkfDDIVL 288
Cdd:PRK13644 130 RhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA--DRIIV 207
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15226227 289 LTEGTLVYAGpagkEPLTYFGN-----FGFLCPEHVNPAEFL 325
Cdd:PRK13644 208 MDRGKIVLEG----EPENVLSDvslqtLGLTPPSLIELAENL 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
91-247 |
2.93e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAG----QlslsprlhlSGLLEVNGKPSSSKAY------KLAFVRQ---E 157
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiQ---------QGRVEVLGGDMADARHrravcpRIAYMPQglgK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 158 DLFFSqLTVRETLSFAAEL--QlpeisSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPS 235
Cdd:NF033858 88 NLYPT-LSVFENLDFFGRLfgQ-----DAAERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPD 156
|
170
....*....|..
gi 15226227 236 VIFADEPTTGLD 247
Cdd:NF033858 157 LLILDEPTTGVD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
86-269 |
3.38e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 86 SVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRlhLSGLLEVNGK------PSSSKAYKLAFV---RQ 156
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG---ADPA--DSGEIRLDGKpvrirsPRDAIRAGIAYVpedRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 157 EDLFFSQLTVRETLSFAAelqLPE------ISSAEER---DEYVNNLLLKlglvsCADScvgDAKVRGISGGEKKRLSLA 227
Cdd:COG1129 338 GEGLVLDLSIRENITLAS---LDRlsrgglLDRRRERalaEEYIKRLRIK-----TPSP---EQPVGNLSGGNQQKVVLA 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15226227 228 CELIASPSVIFADEPTTGLD--AfQAEkVMETLQKLAQDGHTVI 269
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDvgA-KAE-IYRLIRELAAEGKAVI 448
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
70-298 |
3.42e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagqlslsprLHL----SGLLEVNGKPSS 145
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPV---LKGLTFTLHPGEVVALVGPSGSGKSTVAALL---------QNLyqptGGQVLLDGVPLV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 146 SKAY-----KLAFVRQEDLFFSQlTVRET----LSFAAELQLPEISSAEERDEYVNnlllklGLVSCADSCVGDAKVRgI 216
Cdd:TIGR00958 547 QYDHhylhrQVALVGQEPVLFSG-SVRENiaygLTDTPDEEIMAAAKAANAHDFIM------EFPNGYDTEVGEKGSQ-L 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 217 SGGEKKRLSLACELIASPSVIFADEPTTGLDAfQAEKVMETLQKLAqdGHTVICSIHqpRGSVYAKFDDIVLLTEGTLVY 296
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDA-ECEQLLQESRSRA--SRTVLLIAH--RLSTVERADQILVLKKGSVVE 693
|
..
gi 15226227 297 AG 298
Cdd:TIGR00958 694 MG 695
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
91-314 |
4.39e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslsprLHL--SGLLEVNGK--PSSSKAYKLAFVRQE-DLFF---- 161
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNG-------LHVptQGSVRVDDTliTSTSKNKDIKQIRKKvGLVFqfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQL---TVRETLSFAAELQLPEISSAEERDEYvnnlllKLGLVSCADSCVGDAKVRgISGGEKKRLSLACELIASPSVIF 238
Cdd:PRK13649 96 SQLfeeTVLKDVAFGPQNFGVSQEEAEALARE------KLALVGISESLFEKNPFE-LSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 239 ADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH-QPRGSVYAkfDDIVLLTEGTLVYAGpagkEPLTYFGNFGFL 314
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYA--DFVYVLEKGKLVLSG----KPKDIFQDVDFL 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
69-274 |
4.93e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 69 TIRWRNITCSLSDKSSksvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLagQLSLSPRlhlSGLLEVNG------K 142
Cdd:PRK11124 2 SIQLNGINCFYGAHQA------LFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLLEMPR---SGTLNIAGnhfdfsK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 143 PSSSKAYKLafVRQE-DLFFSQ------LTVRETLsFAAELQLPEISSAEERDEyVNNLLLKLGLVSCADscvgdAKVRG 215
Cdd:PRK11124 71 TPSDKAIRE--LRRNvGMVFQQynlwphLTVQQNL-IEAPCRVLGLSKDQALAR-AEKLLERLRLKPYAD-----RFPLH 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 216 ISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQ 274
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
88-300 |
5.83e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 65.54 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPrlhLSGLLEVNGkpssskayklAFVRQ---EDL----- 159
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG--VWPP---TAGSVRLDG----------ADLSQwdrEELgrhig 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 160 -------FFSQlTVRETLSfaaelQLPEISSAE-----------ErdeyvnnLLLKL--GLvscaDSCVGDAKVRgISGG 219
Cdd:COG4618 410 ylpqdveLFDG-TIAENIA-----RFGDADPEKvvaaaklagvhE-------MILRLpdGY----DTRIGEGGAR-LSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 220 EKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPrgSVYAKFDDIVLLTEGTLVYAGP 299
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP--SLLAAVDKLLVLRDGRVQAFGP 549
|
.
gi 15226227 300 A 300
Cdd:COG4618 550 R 550
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
93-264 |
6.94e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 64.30 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 93 NVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqLsLSPRLHLSGLLEVNGKP---SSSKAY------KLAFVRQEDlfFSQ 163
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILG-L-LPPPGITSGEILFDGEDllkLSEKELrkirgrEIQMIFQDP--MTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 L----TVRETLsfaAE-LQLPEISSAEERDEYVNNLLLKLGLvscadscvGDAKVRG------ISGGEKKRLSLACELIA 232
Cdd:COG0444 99 LnpvmTVGDQI---AEpLRIHGGLSKAEARERAIELLERVGL--------PDPERRLdrypheLSGGMRQRVMIARALAL 167
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 233 SPSVIFADEPTTGLDA-FQAEkVMETLQKLAQD 264
Cdd:COG0444 168 EPKLLIADEPTTALDVtIQAQ-ILNLLKDLQRE 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
90-298 |
8.07e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGllEVNGKPSsskaykLAFVRQEDLFFSQlTVRET 169
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-----EG--RVWAERS------IAYVPQQAWIMNA-TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 170 LSF-----AAELQLPEISSAEERDeyvnnlLLKLGlvSCADSCVGDAKVrGISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:PTZ00243 741 ILFfdeedAARLADAVRVSQLEAD------LAQLG--GGLETEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15226227 245 GLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgsVYAKFDDIVLLTEGTLVYAG 298
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGALAGKTRVLATHQVH--VVPRADYVVALGDGRVEFSG 863
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
100-247 |
8.70e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 100 PGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS--KAYKLAFVRQEDLFFSQLTVRETLSFAAELQ 177
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE-----SGQIQIDGKTATRgdRSRFMAYLGHLPGLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 178 lpeissAEERDEYVNNLLLKLGLVSCADSCvgdakVRGISGGEKKRLSLAcELIASPSVIF-ADEPTTGLD 247
Cdd:PRK13543 111 ------GRRAKQMPGSALAIVGLAGYEDTL-----VRQLSAGQKKRLALA-RLWLSPAPLWlLDEPYANLD 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
73-300 |
1.13e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslsprlhlsglLEvngKPSSSKAykla 152
Cdd:PRK11432 10 KNITKRFGSNT------VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG-------------LE---KPTEGQI---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 153 FVRQEDLFFSQLTVRET-LSFAAELQLPEIS--------------SAEERDEYVNNlllKLGLVSCADscVGDAKVRGIS 217
Cdd:PRK11432 64 FIDGEDVTHRSIQQRDIcMVFQSYALFPHMSlgenvgyglkmlgvPKEERKQRVKE---ALELVDLAG--FEDRYVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 218 GGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDDIVLLTEGTLVY 296
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHD-QSEAFAVSDTVIVMNKGKIMQ 217
|
....
gi 15226227 297 AGPA 300
Cdd:PRK11432 218 IGSP 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
92-249 |
1.15e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 92 KNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYKLAFvrQEDLFFSQLTVRETLS 171
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVF--QSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 172 FAaeLQLPEISSAEeRDEYVNNL--LLKLG-LVscadscvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDA 248
Cdd:PRK11000 98 FG--LKLAGAKKEE-INQRVNQVaeVLQLAhLL--------DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
.
gi 15226227 249 F 249
Cdd:PRK11000 167 A 167
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
63-298 |
1.59e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.32 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 63 DSIRPVTIRWRNITCSLSDksskSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlSLSPrlhLSGLLEVNGK 142
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPN----SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG--LLKP---QSGEIKIDGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 143 PSSSKAY-----KLAFVRQE-DLFFSQLTVRETLSFAAE-LQLPEissaEERDEYVNNLLLKLGLVSCADScvgdaKVRG 215
Cdd:PRK13632 72 TISKENLkeirkKIGIIFQNpDNQFIGATVEDDIAFGLEnKKVPP----KKMKDIIDDLAKKVGMEDYLDK-----EPQN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 216 ISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSI-HQPRGSVYAkfDDIVLLTEGTL 294
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAILA--DKVIVFSEGKL 220
|
....
gi 15226227 295 VYAG 298
Cdd:PRK13632 221 IAQG 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
90-266 |
1.89e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.03 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKP-SSSKAYK----LAFVRQEDLF--FS 162
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-----SGSILIDGKDvTKLPEYKrakyIGRVFQDPMMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLSFAAE------LQLPeiSSAEERDEYVNnLLLKLGLvscadscvG-----DAKVRGISGGEKKRLSLACELI 231
Cdd:COG1101 96 SMTIEENLALAYRrgkrrgLRRG--LTKKRRELFRE-LLATLGL--------GlenrlDTKVGLLSGGQRQALSLLMATL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 15226227 232 ASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGH 266
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
84-294 |
1.91e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPrlhlSGLLEVNGKpssskaykLAFVRQEDLFFSQ 163
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----TSSVVIRGS--------VAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 lTVRETLSFAAELQlpeiSSAEERDEYVNNLLLKLGLVSCAD-SCVGDAKVRgISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:PLN03232 694 -TVRENILFGSDFE----SERYWRAIDVTALQHDLDLLPGRDlTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgsVYAKFDDIVLLTEGTL 294
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLH--FLPLMDRIILVSEGMI 817
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
91-268 |
2.38e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQlslsPRLHlSGLLEVNGKPSSSkaYKLAFVRQEDL--------FFS 162
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD----PRAT-SGRIVFDGKDITD--WQTAKIMREAVaivpegrrVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QLTVRETLS---FAAELQlpeisSAEERDEYVNNLLLKLglvscADSCVGDAKVrgISGGEKKRLSLACELIASPSVIFA 239
Cdd:PRK11614 94 RMTVEENLAmggFFAERD-----QFQERIKWVYELFPRL-----HERRIQRAGT--MSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180
....*....|....*....|....*....
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLAQDGHTV 268
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTI 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
90-264 |
2.45e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRlhlSGLLEVNGKPSSS---KAYK--LAFVRQEDLFFSQl 164
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PT---SGTLLFEGEDISTlkpEIYRqqVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAEL--QLPE---ISSAEERDEYVNNLLLKlglvscadscvgdaKVRGISGGEKKRLSLACELIASPSVIFA 239
Cdd:PRK10247 96 TVYDNLIFPWQIrnQQPDpaiFLDDLERFALPDTILTK--------------NIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180
....*....|....*....|....*
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLAQD 264
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVRE 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
92-306 |
2.45e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 92 KNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLS-LSPRLHLSGLlEVNGKPSSSKAYKLAFVRQEDLFFSQLTVRETL 170
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGE-HIQHYASKEVARRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAAELQLPEISSAEERDE-YVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAF 249
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKEDEeAVTKAMQATGITHLADQ-----SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 250 QAEKVMETLQKLAQD-GHTVICSIHQ-PRGSVYAKfdDIVLLTEGTLVYAGpAGKEPLT 306
Cdd:PRK10253 178 HQIDLLELLSELNREkGYTLAAVLHDlNQACRYAS--HLIALREGKIVAQG-APKEIVT 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
91-264 |
2.97e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTT----LLNVLAGQlslsprlhlsGLLEVNGKP--SSSKAYKLAFVRQEDLFFS-- 162
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ----------GEIWFDGQPlhNLNRRQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 ------QLTVRETLSFAAELQLPEISsAEERDEYVNNLLLKLGLvscadscvgDAKVR-----GISGGEKKRLSLACELI 231
Cdd:PRK15134 372 nsslnpRLNVLQIIEEGLRVHQPTLS-AAQREQQVIAVMEEVGL---------DPETRhrypaEFSGGQRQRIAIARALI 441
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 232 ASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD 264
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
93-247 |
3.02e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 93 NVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL-----SLSPRLHLSGLLEVNGKPSSSKAYKL----AFVRQ--EDLFF 161
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLapdagEVHYRMRDGQLRDLYALSEAERRRLLrtewGFVHQhpRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLT----VRETLSFAAELQLPEIssaeeRDEYVNnlllKLGLVSCADSCVGDAKvRGISGGEKKRLSLACELIASPSVI 237
Cdd:PRK11701 104 MQVSaggnIGERLMAVGARHYGDI-----RATAGD----WLERVEIDAARIDDLP-TTFSGGMQQRLQIARNLVTHPRLV 173
|
170
....*....|
gi 15226227 238 FADEPTTGLD 247
Cdd:PRK11701 174 FMDEPTGGLD 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
94-300 |
3.47e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 94 VSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLsgllevNGKP-SSSKAYKLAFVRQedlFFSQltvRETLSF 172
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQF------AGQPlEAWSAAELARHRA---YLSQ---QQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 173 AA------ELQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLA--CeLIASPSV------IF 238
Cdd:PRK03695 83 AMpvfqylTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRLAavV-LQVWPDInpagqlLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226227 239 ADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD-LNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
91-298 |
3.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRLHLSGLLEVNGKPSSSKAY-----KLAFVRQE-DLFFSQL 164
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL--PDDNPNSKITVDGITLTAKTVwdireKVGIVFQNpDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAE-LQLPEissaEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:PRK13640 101 TVGDDVAFGLEnRAVPR----PEMIKIVRDVLADVGMLDYIDS-----EPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 244 TGLDAFQAEKVMETLQKLAQDGHTVICSI-HQPRGSVYAkfDDIVLLTEGTLVYAG 298
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISItHDIDEANMA--DQVLVLDDGKLLAQG 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
99-269 |
4.25e-10 |
|
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: 62.88 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 99 KPGRLLAIMGPSGSGKTTLLNVLAGQlsLSPRL-----------------------HLSGLLEVNGKPssskAYKLAFVR 155
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGE--LKPNLgdydeepswdevlkrfrgtelqdYFKKLANGEIKV----AHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 156 QEDLFFSqLTVRETLsfaaelqlpeiSSAEER---DEYVNnlllKLGLVScadscVGDAKVRGISGGEKKRLSLACELIA 232
Cdd:COG1245 171 LIPKVFK-GTVRELL-----------EKVDERgklDELAE----KLGLEN-----ILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190
....*....|....*....|....*....|....*..
gi 15226227 233 SPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
88-298 |
6.34e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNvlagqlslsprlHLSGLLevngKPSS-------------SKAYKLAFV 154
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQ------------HLNGLL----QPTSgtvtigervitagKKNKKLKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 155 RQE-DLFF----SQL---TVRETLSFA-AELQLPEiSSAEERDEYvnnlLLKLglvscadscVG-DAKVRG-----ISGG 219
Cdd:PRK13634 84 RKKvGIVFqfpeHQLfeeTVEKDICFGpMNFGVSE-EDAKQKARE----MIEL---------VGlPEELLArspfeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 220 EKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQ-PRGSVYAkfDDIVLLTEGTLVYA 297
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSmEDAARYA--DQIVVMHKGTVFLQ 227
|
.
gi 15226227 298 G 298
Cdd:PRK13634 228 G 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
86-247 |
6.89e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 86 SVRF--LL--KNVSGEAKPGRLLAIMGPSGSGKTTLLNVL-------AGQLSLSPRlHLSGLlevngkpSSSKAYKLAFV 154
Cdd:PRK11300 12 MMRFggLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptGGTILLRGQ-HIEGL-------PGHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 155 R--QEDLFFSQLTVRETLSFAAELQL-----------PEISSAE-ERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGE 220
Cdd:PRK11300 84 RtfQHVRLFREMTVIENLLVAQHQQLktglfsgllktPAFRRAEsEALDRAATWLERVGLLEHANRQAGN-----LAYGQ 158
|
170 180
....*....|....*....|....*..
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLN 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
70-298 |
7.71e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNvlagqlslsprlHLSGLLevngKPSSSKAY 149
Cdd:PRK13633 5 IKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAK------------HMNALL----IPSEGKVY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 KLAF----------VRQE-DLFF----SQLT---VRETLSFAAE-LQLPeissAEERDEYVNNLLLKLGLVSCADScvgd 210
Cdd:PRK13633 69 VDGLdtsdeenlwdIRNKaGMVFqnpdNQIVatiVEEDVAFGPEnLGIP----PEEIRERVDESLKKVGMYEYRRH---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 211 aKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKL-AQDGHTVICSIHQPRGSVYAkfDDIVLL 289
Cdd:PRK13633 141 -APHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEA--DRIIVM 217
|
....*....
gi 15226227 290 TEGTLVYAG 298
Cdd:PRK13633 218 DSGKVVMEG 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
91-269 |
7.79e-10 |
|
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: 59.76 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLL-----NVLAGQLSLSPRlHLSGLLEVngkpSSSKAYKLAFVRQEDL-FFSQ- 163
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLkciygNYLPDSGSILVR-HDGGWVDL----AQASPREILALRRRTIgYVSQf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 LTVR---ETLSFAAE-LQLPEISSAEERDEyVNNLLLKLGL------VSCADscvgdakvrgISGGEKKRLSLACELIAS 233
Cdd:COG4778 102 LRVIprvSALDVVAEpLLERGVDREEARAR-ARELLARLNLperlwdLPPAT----------FSGGEQQRVNIARGFIAD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 15226227 234 PSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
91-299 |
8.51e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.04 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSS-----SKAYKLAFVRQEDLFFSQlt 165
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTklqldSWRSRLAVVSQTPFLFSD-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 vretlSFAAELQLPEISSAEERDEYVNNL------LLKL--GLvscaDSCVGDakvRGI--SGGEKKRLSLACELIASPS 235
Cdd:PRK10789 404 -----TVANNIALGRPDATQQEIEHVARLasvhddILRLpqGY----DTEVGE---RGVmlSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 236 VIFADEPTTGLDAfQAEKvmETLQKLAQ--DGHTVICSIHqpRGSVYAKFDDIVLLTEGTLVYAGP 299
Cdd:PRK10789 472 ILILDDALSAVDG-RTEH--QILHNLRQwgEGRTVIISAH--RLSALTEASEILVMQHGHIAQRGN 532
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
84-359 |
8.78e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLslsprlhlsgllevngkPSSSKAY-----KLAFVRQED 158
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL-----------------PPRSDASvvirgTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 159 LFFSQlTVRETLSFAAELQlpeiSSAEERDEYVNNLLLKLGLVSCAD-SCVGDAKVrGISGGEKKRLSLACELIASPSVI 237
Cdd:PLN03130 689 WIFNA-TVRDNILFGSPFD----PERYERAIDVTALQHDLDLLPGGDlTEIGERGV-NISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 238 FADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRgsVYAKFDDIVLLTEGTLvyagpagKEPLTY--FGNFGFLC 315
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLH--FLSQVDRIILVHEGMI-------KEEGTYeeLSNNGPLF 833
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15226227 316 PEHVNPAEFLADLISVDYSSSETVYSSQKRVHALVDAFSQRSSS 359
Cdd:PLN03130 834 QKLMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSS 877
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
68-300 |
8.98e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 68 VTIRWRNITCSLSDkssksvRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSK 147
Cdd:PRK10575 10 TTFALRNVSFRVPG------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYKlAFVRQEDLFFSQL------TVRETLSFAaelQLPEISS-----AEERdEYVNNLLLKLGLVSCADSCVGDakvrgI 216
Cdd:PRK10575 79 SSK-AFARKVAYLPQQLpaaegmTVRELVAIG---RYPWHGAlgrfgAADR-EKVEEAISLVGLKPLAHRLVDS-----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 217 SGGEKKRLSLACELIASPSVIFADEPTTGLD-AFQAEkVMETLQKLAQD-GHTVICSIHQPrgSVYAKF-DDIVLLTEGT 293
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVD-VLALVHRLSQErGLTVIAVLHDI--NMAARYcDYLVALRGGE 225
|
....*..
gi 15226227 294 LVYAGPA 300
Cdd:PRK10575 226 MIAQGTP 232
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
99-273 |
9.34e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 99 KPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRLhlsgllevnGKPSSSKAYK--LAFVRQEDL--FFSQLtVRETLSFAA 174
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLK--PNL---------GKFDDPPDWDeiLDEFRGSELqnYFTKL-LEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 175 ELQ----LPE---------ISSAEER---DEYVNNLLLKlGLVscadscvgDAKVRGISGGEKKRLSLACELIASPSVIF 238
Cdd:cd03236 92 KPQyvdlIPKavkgkvgelLKKKDERgklDELVDQLELR-HVL--------DRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190
....*....|....*....|....*....|....*
gi 15226227 239 ADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
73-298 |
1.19e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQ-----LSLSPRLHLSGLLEVNGKPSSSK 147
Cdd:PRK09580 5 KDLHVSVEDKA------ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyevTGGTVEFKGKDLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYKLAFVRQEDL------FFSQLTVRETLSFAAELQLpeissaeERDEYVNNLLLKLGLVSCADSCVGDAKVRGISGGEK 221
Cdd:PRK09580 79 GIFMAFQYPVEIpgvsnqFFLQTALNAVRSYRGQEPL-------DRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 222 KRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
70-256 |
1.38e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.73 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSL-SPRLHLSGlLEVNGKPSSSKA 148
Cdd:PRK09452 15 VELRGISKSFDGKE------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIMLDG-QDITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 149 YKLAFvrQEDLFFSQLTVRETLSFAAELQ-LPEissaEERDEYVNNLLLKLGLVSCADScvgdaKVRGISGGEKKRLSLA 227
Cdd:PRK09452 88 VNTVF--QSYALFPHMTVFENVAFGLRMQkTPA----AEITPRVMEALRMVQLEEFAQR-----KPHQLSGGQQQRVAIA 156
|
170 180
....*....|....*....|....*....
gi 15226227 228 CELIASPSVIFADEPTTGLDaFQAEKVME 256
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALD-YKLRKQMQ 184
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
79-300 |
1.43e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 79 LSDKSSKSVRFL-LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVrqe 157
Cdd:COG1134 29 LRRRRTRREEFWaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT-----SGRVEVNGRVSALLELGAGFH--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 158 dlffSQLTVRETLSFAAELQ---LPEIssaEERDEYVnnlllklglVSCADscVG---DAKVRGISGGEKKRLSLACELI 231
Cdd:COG1134 101 ----PELTGRENIYLNGRLLglsRKEI---DEKFDEI---------VEFAE--LGdfiDQPVKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226227 232 ASPSVIFADEPT-TGLDAFQaEKVMETLQKLAQDGHTVI-CSiHQPrGSVyAKF-DDIVLLTEGTLVYAGPA 300
Cdd:COG1134 163 VDPDILLVDEVLaVGDAAFQ-KKCLARIRELRESGRTVIfVS-HSM-GAV-RRLcDRAIWLEKGRLVMDGDP 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
91-293 |
1.50e-09 |
|
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: 58.50 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL-SLSPRLHLSGLLEVNGKPSSSKA---YKLAFVRQEDLFFSQlTV 166
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqTLEGKVHWSNKNESEPSFEATRSrnrYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFAAELQlpeissaEERDEYVNN---LLLKLGLVSCADSC-VGDakvRGI--SGGEKKRLSLACELIASPSVIFAD 240
Cdd:cd03290 96 EENITFGSPFN-------KQRYKAVTDacsLQPDIDLLPFGDQTeIGE---RGInlSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 241 EPTTGLDAFQAEKVMET--LQKLAQDGHTVICSIHQPRGSVYAkfDDIVLLTEGT 293
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPHA--DWIIAMKDGS 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
91-274 |
1.86e-09 |
|
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: 59.17 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLN-VLAGqlSLSPRLHLSG-----------------LLEVNGKP------SSS 146
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYP--ALARRLHLKKeqpgnhdrieglehidkVIVIDQSPigrtprSNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYKLAFVRQEDLFFSQLT----VRETL-------SFAAELQLPeISSAEERDEYVNNLLLKL-GLVScadscVGDAKVR 214
Cdd:cd03271 89 ATYTGVFDEIRELFCEVCKgkryNRETLevrykgkSIADVLDMT-VEEALEFFENIPKIARKLqTLCD-----VGLGYIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 215 ------GISGGEKKRLSLACELiASPS----VIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQ 274
Cdd:cd03271 163 lgqpatTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
70-260 |
1.91e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNIT---CSLSDKSSKSVrfllKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVN------ 140
Cdd:TIGR03269 280 IKVRNVSkryISVDRGVVKAV----DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-----SGEVNVRvgdewv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 141 -----GKPSSSKAYK-LAFVRQEDLFFSQLTVRETLSFAAELQLPE----------ISSAEERDEYVNNLLLKLglvscA 204
Cdd:TIGR03269 351 dmtkpGPDGRGRAKRyIGILHQEYDLYPHRTVLDNLTEAIGLELPDelarmkavitLKMVGFDEEKAEEILDKY-----P 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 205 DScvgdakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQK 260
Cdd:TIGR03269 426 DE---------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK 472
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
91-247 |
1.98e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAFVRQEDLF---FSQLTVR 167
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-----SGELLIDDHPLHFGDYSYRSQRIRMIFqdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLS--FAAELQLPEISSAEERDEYVNNLLLKLGLVSCADSCVGDAkvrgISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:PRK15112 104 QRISqiLDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM----LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
..
gi 15226227 246 LD 247
Cdd:PRK15112 180 LD 181
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
88-295 |
2.99e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSS-KAYKLAFVR-QEDLFFSQLT 165
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS-----AGKIWFSGHDITRlKNREVPFLRrQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPEI---SSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIiagASGDDIRRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLV 295
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHD-IGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
70-298 |
3.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 70 IRWRNITCSLSDKSSKSVRFLLkNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNgkpSSSKAY 149
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVS---STSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 150 KLAFVRQ---------EDLFFSQlTVRETLSFAAElqlpEISSAEERDEYVnnLLLKLGLVSCADSCVGDAKVRgISGGE 220
Cdd:PRK13643 78 EIKPVRKkvgvvfqfpESQLFEE-TVLKDVAFGPQ----NFGIPKEKAEKI--AAEKLEMVGLADEFWEKSPFE-LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
84-261 |
3.20e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK--P--SSSKAY----KLAFVR 155
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-----HGEILFDGEniPamSRSRLYtvrkRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 156 QEDLFFSQLTVRETLSFA--AELQLPE--ISSAeerdeyvnnLLLKLGLVSCAdscvGDAKVR--GISGGEKKRLSLACE 229
Cdd:PRK11831 91 QSGALFTDMNVFDNVAYPlrEHTQLPAplLHST---------VMMKLEAVGLR----GAAKLMpsELSGGMARRAALARA 157
|
170 180 190
....*....|....*....|....*....|..
gi 15226227 230 LIASPSVIFADEPTTGLDAFqaekVMETLQKL 261
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPI----TMGVLVKL 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
44-315 |
5.41e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 44 LLPEDEAEDDYAE---TEDGGGDSIrpvTIRWRNITCSLSDKSSksvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNV 120
Cdd:TIGR00957 613 FLSHEELEPDSIErrtIKPGEGNSI---TVHNATFTWARDLPPT------LNGITFSIPEGALVAVVGQVGCGKSSLLSA 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 121 LAGQLS-LSPRLHLSGllevngkpssskayKLAFVRQEdLFFSQLTVRETLSFAAELQLPEISSAEErdeyVNNLLLKLG 199
Cdd:TIGR00957 684 LLAEMDkVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLRENILFGKALNEKYYQQVLE----ACALLPDLE 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 200 LVSCADSCVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETL--QKLAQDGHTVICSIHQPrg 277
Cdd:TIGR00957 745 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigPEGVLKNKTRILVTHGI-- 822
|
250 260 270
....*....|....*....|....*....|....*....
gi 15226227 278 SVYAKFDDIVLLTEGTLVYAGPAgKEPLTYFGNFG-FLC 315
Cdd:TIGR00957 823 SYLPQVDVIIVMSGGKISEMGSY-QELLQRDGAFAeFLR 860
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
66-301 |
7.44e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.02 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 66 RPVTIRWRNITCSlsdksskSVRFLLKNVSGEAKPGRLLAIMGPSGSGKT----TLLNVL-AGQLSLSPRLHLSGlleVN 140
Cdd:PRK10418 1 MPQQIELRNIALQ-------AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTAGRVLLDG---KP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 141 GKPSSSKAYKLAFVRQ--EDLFFSQLT----VRETLSfaaelqlpeiSSAEERDEYVnnlllklgLVSCADScVGDAKVR 214
Cdd:PRK10418 71 VAPCALRGRKIATIMQnpRSAFNPLHTmhthARETCL----------ALGKPADDAT--------LTAALEA-VGLENAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 215 GI--------SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIHQpRGSVYAKFDD 285
Cdd:PRK10418 132 RVlklypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHD-MGVVARLADD 210
|
250
....*....|....*.
gi 15226227 286 IVLLTEGTLVYAGPAG 301
Cdd:PRK10418 211 VAVMSHGRIVEQGDVE 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
88-247 |
8.80e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKpssskaYKLAFVRQedlffsQLTVR 167
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-----EGVIKRNGK------LRIGYVPQ------KLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAE--LQL-PEISSAEerdeyvnnLLLKLGLVSCADscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:PRK09544 80 TTLPLTVNrfLRLrPGTKKED--------ILPALKRVQAGH--LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
...
gi 15226227 245 GLD 247
Cdd:PRK09544 150 GVD 152
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
84-248 |
8.95e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 84 SKSV---RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlhlsgllEVNGKPSSSKAYKLAFVRQEDLF 160
Cdd:PRK11819 13 SKVVppkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----------EFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLS------FAAELQLPEISSA-EERDEYVNNLLLKLGLVSCA---------DSCV-----------GDAKV 213
Cdd:PRK11819 82 DPEKTVRENVEegvaevKAALDRFNEIYAAyAEPDADFDALAAEQGELQEIidaadawdlDSQLeiamdalrcppWDAKV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 15226227 214 RGISGGEKKRLSLACELIASPSVIFADEPTTGLDA 248
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
91-266 |
9.52e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.54 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTL-LNVLagqlslspRLHLS-GLLEVNGKP-SSSKAYKLAFVRQE------DLFF 161
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLgLALL--------RLIPSeGEIRFDGQDlDGLSRRALRPLRRRmqvvfqDPFG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 S---QLTVRETLSFAAELQLPEISsAEERDEYVNNLLLKLGLvscadscvgDAKVRG-----ISGGEKKRLSLACELIAS 233
Cdd:COG4172 374 SlspRMTVGQIIAEGLRVHGPGLS-AAERRARVAEALEEVGL---------DPAARHrypheFSGGQRQRIAIARALILE 443
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 234 PSVIFADEPTTGLD-AFQAEkVMETLQKLaQDGH 266
Cdd:COG4172 444 PKLLVLDEPTSALDvSVQAQ-ILDLLRDL-QREH 475
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
88-298 |
9.64e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 58.68 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLnvlagqlslspRLhLSGLLEVNG-------------KPSSSKAYkLAFV 154
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLA-----------RL-LFRFYDVTSgrilidgqdirdvTQASLRAA-IGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 155 RQEDLFFSQlTVRETLSFAAelqlPEISSAEER--------DEYVNNllLKLGLvscaDSCVGDakvRG--ISGGEKKRL 224
Cdd:COG5265 438 PQDTVLFND-TIAYNIAYGR----PDASEEEVEaaaraaqiHDFIES--LPDGY----DTRVGE---RGlkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 225 SLACELIASPSVIFADEPTTGLDAfQAEK-VMETLQKLAQdGHTVICSIHqpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDS-RTERaIQAALREVAR-GRTTLVIAH--RLSTIVDADEILVLEAGRIVERG 574
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
91-247 |
1.24e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslsprlhL----SGLLEVNGKP-SSSKAYKLAFVRQE-------- 157
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---------LerptSGSVLVDGVDlTALSERELRAARRKigmifqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 158 DLfFSQLTVRETLSFaaelqlP-EIS--SAEERDEYVNNLllkLGLVSCADScvGDAKVRGISGGEKKRLSLACELIASP 234
Cdd:COG1135 92 NL-LSSRTVAENVAL------PlEIAgvPKAEIRKRVAEL---LELVGLSDK--ADAYPSQLSGGQKQRVGIARALANNP 159
|
170
....*....|...
gi 15226227 235 SVIFADEPTTGLD 247
Cdd:COG1135 160 KVLLCDEATSALD 172
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
74-321 |
1.40e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 74 NITCSLSDKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVL-------AGQLSLSPRLHLSGLLEVNGKPSSS 146
Cdd:PRK13645 11 NVSYTYAKKTPFEFK-ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTngliiseTGQTIVGDYAIPANLKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYKLAFVRQEDLFFsQLTVRETLSFAAelqlpeISSAEERDEYVNNLLLKLGLVSCADSCVGDAKVRgISGGEKKRLSL 226
Cdd:PRK13645 90 KEIGLVFQFPEYQLF-QETIEKDIAFGP------VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFE-LSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGpagkEPLT 306
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG----SPFE 237
|
250
....*....|....*
gi 15226227 307 YFGNFGFLCPEHVNP 321
Cdd:PRK13645 238 IFSNQELLTKIEIDP 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
73-273 |
1.56e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.15 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITCSLSDKSSksvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAG-QLSLSPRLHLSGlLEVNGKPSSSKAYKL 151
Cdd:PRK11607 23 RNLTKSFDGQHA------VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDG-VDLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 152 AFvrQEDLFFSQLTVRETLSFAaeLQLPEISSAEERDEyVNNLllkLGLVSCADscVGDAKVRGISGGEKKRLSLACELI 231
Cdd:PRK11607 96 MF--QSYALFPHMTVEQNIAFG--LKQDKLPKAEIASR-VNEM---LGLVHMQE--FAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15226227 232 ASPSVIFADEPTTGLDAFQAEKV-METLQKLAQDGHTVICSIH 273
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTH 208
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
444-598 |
1.87e-08 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 55.21 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 444 MGLLQVAAINTAMAaltktvgvfpkeraiVDRERSKGSY--------SLGPYLLSKTIAEIPIGAAFPLMFGAVLYPMAR 515
Cdd:COG0842 12 MSLLFTALMLTALS---------------IAREREQGTLerllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 516 LNPTLSRFGKFCGIVTVESFAASAMGLTVGAMVPSTEAAMAVGPSLMTVFIVFGGYYVNADNTPIIFRWIPRASLIRWAF 595
Cdd:COG0842 77 VPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFV 156
|
...
gi 15226227 596 QGL 598
Cdd:COG0842 157 EAL 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
66-262 |
2.04e-08 |
|
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: 57.49 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 66 RPVTIRWRNITCSLSDkssksvrFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL-----SLSPRLHLSgllevn 140
Cdd:COG1245 338 EETLVEYPDLTKSYGG-------FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLkpdegEVDEDLKIS------ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 141 gkpssskaYKLAFVRQEdlffSQLTVRETLSFAAElqlPEISSAEERDEYVNNLLLKLGLvscadscvgDAKVRGISGGE 220
Cdd:COG1245 405 --------YKPQYISPD----YDGTVEEFLRSANT---DDFGSSYYKTEIIKPLGLEKLL---------DKNVKDLSGGE 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLA 262
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
216-273 |
2.46e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.92 E-value: 2.46e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 216 ISGGEKKRLSLACELIAS---PSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIH 273
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
90-261 |
3.93e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYKLAFVRQE--------DLFf 161
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQvsmvhpkpNLF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 sQLTVRETLSFAAEL-------QLPEI-----SSAEERDEyVNNLLLKLGLvscadscvgdakvrGISGGEKKRLSLACE 229
Cdd:PRK14258 101 -PMSVYDNVAYGVKIvgwrpklEIDDIvesalKDADLWDE-IKHKIHKSAL--------------DLSGGQQQRLCIARA 164
|
170 180 190
....*....|....*....|....*....|..
gi 15226227 230 LIASPSVIFADEPTTGLDAFQAEKVMETLQKL 261
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSL 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
56-298 |
4.55e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 56 ETE-DGGGDSIRPVT--IRWRNITCSLSDKSSKSvrflLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAgqlslspRLH 132
Cdd:PRK11176 325 EQEkDEGKRVIERAKgdIEFRNVTFTYPGKEVPA----LRNINFKIPAGKTVALVGRSGSGKSTIANLLT-------RFY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 133 --LSGLLEVNGkpSSSKAYKLAFVRQEDLFFSQL------TVRETLSFAAElqlpEISSAEE-----RDEYVNNLLLKL- 198
Cdd:PRK11176 394 diDEGEILLDG--HDLRDYTLASLRNQVALVSQNvhlfndTIANNIAYART----EQYSREQieeaaRMAYAMDFINKMd 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 199 -GLvscaDSCVGDAKVRgISGGEKKRLSLACELIASPSVIFADEPTTGLD-----AFQAekVMETLQKlaqdGHTVICSI 272
Cdd:PRK11176 468 nGL----DTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATSALDteserAIQA--ALDELQK----NRTSLVIA 536
|
250 260
....*....|....*....|....*.
gi 15226227 273 HqpRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK11176 537 H--RLSTIEKADEILVVEDGEIVERG 560
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
90-302 |
5.04e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRlhlSGLLEVNGKPSSSKAYKLAFVRQE----------DL 159
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLR--PQ---KGAVLWQGKPLDYSKRGLLALRQQvatvfqdpeqQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 160 FFSQLTVRETLSFAaELQLPEISSAEERDEyvnnlllKLGLVscadscvgDAK------VRGISGGEKKRLSLACELIAS 233
Cdd:PRK13638 91 FYTDIDSDIAFSLR-NLGVPEAEITRRVDE-------ALTLV--------DAQhfrhqpIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 234 PSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPrGSVYAKFDDIVLLTEGTLVYAGPAGK 302
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
91-295 |
5.72e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsprlHLSGLLEVNGKPSSSKAY-----KLAFVRQE-DLFFSQL 164
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAENVwnlrrKIGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELQ-LPEissaEERDEYVNNLLLKLGLVscadscvgDAKVRG---ISGGEKKRLSLACELIASPSVIFAD 240
Cdd:PRK13642 98 TVEDDVAFGMENQgIPR----EEMIKRVDEALLAVNML--------DFKTREparLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVyAKFDDIVLLTEGTLV 295
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEII 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
63-262 |
5.99e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 63 DSIRPVTIRWRNITCSLSDkssksvrFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLslsprlhlsgllevngK 142
Cdd:PRK13409 334 ESERETLVEYPDLTKKLGD-------FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVL----------------K 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 143 PSSSK-------AYKLAFVRQEdlffSQLTVRETLSFAAelqlPEISSaeerdEYVNNLLLK-LGLVSCADScvgdaKVR 214
Cdd:PRK13409 391 PDEGEvdpelkiSYKPQYIKPD----YDGTVEDLLRSIT----DDLGS-----SYYKSEIIKpLQLERLLDK-----NVK 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226227 215 GISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLA 262
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
99-264 |
6.53e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 99 KPGRLLAIMGPSGSGKTTLLNVLAGQlsLSPRLhlsGllEVNGKPSSSKAYKlAFVRQEdLF--FSQL------------ 164
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGE--LIPNL---G--DYEEEPSWDEVLK-RFRGTE-LQnyFKKLyngeikvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 -----------TVRETLsfaaelqlpeiSSAEER---DEYVNNLLLKLGLvscadscvgDAKVRGISGGEKKRLSLACEL 230
Cdd:PRK13409 168 yvdlipkvfkgKVRELL-----------KKVDERgklDEVVERLGLENIL---------DRDISELSGGELQRVAIAAAL 227
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 231 IASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD 264
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAEG 261
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
100-275 |
6.68e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.75 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 100 PGRLLAIMGPSGSGKTTLLnvlagqlslsprlhlsgllevngkpsssKAYKLAFVRQedlffsqltvretlsfaaelqlp 179
Cdd:cd03227 20 EGSLTIITGPNGSGKSTIL----------------------------DAIGLALGGA----------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 180 eiSSAEERDEYVnnlllKLGLVSCADSCVGDAKVRGISGGEKKRLSLA-----CELIASPSVIFaDEPTTGLDAFQAEKV 254
Cdd:cd03227 49 --QSATRRRSGV-----KAGCIVAAVSAELIFTRLQLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|.
gi 15226227 255 METLQKLAQDGHTVICSIHQP 275
Cdd:cd03227 121 AEAILEHLVKGAQVIVITHLP 141
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
91-269 |
7.69e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPssskaykLAFVRQEDlffsqltvretl 170
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-----AGSILIDGQE-------MRFASTTA------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAA-------ELQL-PEISSAEerdeyvnNLLL-----KLGLV--SCADSCVG------------DAKVRGISGGEKKR 223
Cdd:PRK11288 76 ALAAgvaiiyqELHLvPEMTVAE-------NLYLgqlphKGGIVnrRLLNYEAReqlehlgvdidpDTPLKYLSIGQRQM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15226227 224 LSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVIL 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
91-298 |
1.04e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.65 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVL-------AGQLSLS----PRLHLSGLLEVNGKpssskayKLAFVRQEDL 159
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptRGQVLIDgvdiAKISDAELREVRRK-------KIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 160 FFSQLTVRETLSFAAELQLpeiSSAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFA 239
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAG---INAEERREKALDALRQVGLENYAHSYPDE-----LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
90-274 |
1.20e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQlsLSPRlhlSGLLEVNG----KPSSSKAYKLAFVRQEDLFFSQLT 165
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL--LNPE---KGEILFERqsikKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFaaelQLPEISSAEERDEYVNnlLLKLGLVScadscvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:PRK13540 91 LRENCLY----DIHFSPGAVGITELCR--LFSLEHLI-------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 15226227 246 LDAFQAEKVMETLQKLAQDGHTVICSIHQ 274
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
91-267 |
1.24e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqLSlSPRlhlSGLLEVNGKPSS--SKAYKLAFVRQEDLFFS------ 162
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LE-SPS---QGNVSWRGEPLAklNRAQRKAFRRDIQMVFQdsisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 --QLTVRETLsfaAE-----LQLpeisSAEERDEYVNNLLLKLGL-VSCADSCVGDakvrgISGGEKKRLSLACELIASP 234
Cdd:PRK10419 103 npRKTVREII---REplrhlLSL----DKAERLARASEMLRAVDLdDSVLDKRPPQ-----LSGGQLQRVCLARALAVEP 170
|
170 180 190
....*....|....*....|....*....|....
gi 15226227 235 SVIFADEPTTGLD-AFQAEkVMETLQKLAQDGHT 267
Cdd:PRK10419 171 KLLILDEAVSNLDlVLQAG-VIRLLKKLQQQFGT 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
217-271 |
1.53e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.53e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 217 SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICS 271
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
88-273 |
1.72e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSS-----SKAYKLAFVRQE-DLFF 161
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGQIIIDGDLLTeenvwDIRHKIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAELQLPEISSAEERdeyVNNLLLKLGLVscadscvgDAKVRG---ISGGEKKRLSLACELIASPSVIF 238
Cdd:PRK13650 95 VGATVEDDVAFGLENKGIPHEEMKER---VNEALELVGMQ--------DFKEREparLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 15226227 239 ADEPTTGLDAFQAEKVMETLQKLAQD-GHTVICSIH 273
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITH 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
89-250 |
2.33e-07 |
|
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: 52.41 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 89 FLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAYklafvrqedlffSQLTVRE 168
Cdd:cd03237 13 FTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD------------YEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 169 TLSfaaelqlpEISSAEERDEYVNNLLLK-LGLVSCADScvgdaKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:cd03237 81 LLS--------SITKDFYTHPYFKTEIAKpLQIEQILDR-----EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
...
gi 15226227 248 AFQ 250
Cdd:cd03237 148 VEQ 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
91-299 |
2.43e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.03 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAY-----KLAFVRQEDLFFSQlT 165
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDISTIPLedlrsSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAELQLPEISSAEERDEYVNNLllklglvscadscvgdakvrgiSGGEKKRLSLACELIASPSVIFADEPTTG 245
Cdd:cd03369 98 IRSNLDPFDEYSDEEIYGALRVSEGGLNL----------------------SQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 246 LDAFQAEKVMETLQKLAQDGhTVICSIHqpRGSVYAKFDDIVLLTEGTLV-YAGP 299
Cdd:cd03369 156 IDYATDALIQKTIREEFTNS-TILTIAH--RLRTIIDYDKILVMDAGEVKeYDHP 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
65-294 |
2.56e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 65 IRPVTIRWRNITC-SLSDKSSKSVrfllKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLslsPRLHlSGLLEVNGKP 143
Cdd:TIGR02633 253 IGDVILEARNLTCwDVINPHRKRV----DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY---PGKF-EGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 144 SSSK------AYKLAFV---RQEDLFFSQLTVRETL------SFAAELQLPEISSAEERDEYVNNLLLKlglvscadSCV 208
Cdd:TIGR02633 325 VDIRnpaqaiRAGIAMVpedRKRHGIVPILGVGKNItlsvlkSFCFKMRIDAAAELQIIGSAIQRLKVK--------TAS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 209 GDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICsIHQPRGSVYAKFDDIVL 288
Cdd:TIGR02633 397 PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIV-VSSELAEVLGLSDRVLV 475
|
....*.
gi 15226227 289 LTEGTL 294
Cdd:TIGR02633 476 IGEGKL 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
91-269 |
3.24e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQlslspRLHLSGLLEVNGKP----SSSKAYK--LAFV---RQEDLFF 161
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL-----RPPASGSIRLDGEDitglSPRERRRlgVAYIpedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLsfaaelqlpeISSAEERDEYVNNLLLKLGL-------------VSCADScvgDAKVRGISGGEKKRLSLAC 228
Cdd:COG3845 349 PDMSVAENL----------ILGRYRRPPFSRGGFLDRKAirafaeelieefdVRTPGP---DTPARSLSGGNQQKVILAR 415
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVL 456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
88-261 |
4.25e-07 |
|
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: 53.40 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSlsPRlhlSGLLEVngkpssSKAYKLAFVRQE-DLFFSQLTV 166
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQ--PD---SGTIEI------GETVKLAYVDQSrDALDPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 167 RETLSFAAE-LQLP--EISSAEerdeYVNNLLLKlGlvscADScvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPT 243
Cdd:TIGR03719 404 WEEISGGLDiIKLGkrEIPSRA----YVGRFNFK-G----SDQ---QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170
....*....|....*...
gi 15226227 244 TGLDafqaekvMETLQKL 261
Cdd:TIGR03719 472 NDLD-------VETLRAL 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
81-246 |
4.36e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 81 DKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGK------PSSSKAYKLAFV 154
Cdd:PRK10762 11 DKAFPGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD-----AGSILYLGKevtfngPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 155 RQEDLFFSQLTVRETLSFAAELQLP--EISSAEERDEyVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIA 232
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVNRfgRIDWKKMYAE-ADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSF 158
|
170
....*....|....
gi 15226227 233 SPSVIFADEPTTGL 246
Cdd:PRK10762 159 ESKVIIMDEPTDAL 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
78-264 |
5.02e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 78 SLSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKT-TLLNVLaGQLSLSPRLHLSGLLEVNGKP---------SSSK 147
Cdd:PRK15134 12 SVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPPVVYPSGDIRFHGESllhaseqtlRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 148 AYKLAFVRQEDLffSQLTVRETLsfaaELQLPEISSAEE-------RDEyvnnlllklgLVSCADScVG--DAKVR---- 214
Cdd:PRK15134 91 GNKIAMIFQEPM--VSLNPLHTL----EKQLYEVLSLHRgmrreaaRGE----------ILNCLDR-VGirQAAKRltdy 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15226227 215 --GISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQD 264
Cdd:PRK15134 154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQE 205
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
98-133 |
1.17e-06 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 49.42 E-value: 1.17e-06
10 20 30
....*....|....*....|....*....|....*.
gi 15226227 98 AKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHL 133
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVF 37
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
91-300 |
1.25e-06 |
|
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: 51.75 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRLHLSGLLEVNGKP------SSSKAYKLAFVRQEDLFFSQL 164
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG---VYPHGTWDGEIYWSGSPlkasniRDTERAGIVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TVRETLSFAAELQLP-EISSAEERDEYVNNLLLKLGLVSCADS-CVGDakvrgISGGEKKRLSLACELIASPSVIFADEP 242
Cdd:TIGR02633 94 SVAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTrPVGD-----YGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15226227 243 TTGLDAFQAEKVMETLQKLAQdgHTVIC-SIHQPRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKA--HGVACvYISHKLNEVKAVCDTICVIRDGQHVATKDM 225
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
273-343 |
1.81e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 51.06 E-value: 1.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226227 273 HQPRGSVYAKFDDIVLLTEGTL-VYAGPAgKEPLTYFGNFGFLCPEHVNPAEFLADLIS--VDYSSSETVYSSQ 343
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLtVYHGPV-KKVEEYFAGLGINVPERVNPPDHFIDILEgiVKPSTSSGVDYKQ 73
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
91-275 |
1.82e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.56 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTL-LNVL--AGQL----SLSP----RLHLSGLLEV-----------------NGK 142
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIyaEGQRryveSLSAyarqFLGQMDKPDVdsieglspaiaidqkttSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 143 PSS---SKAYKLAFVRqedLFFSQLTVRETLSFAAELQLPEISSAEErdeyvnnlllklglvscadscvgdakVRGISGG 219
Cdd:cd03270 91 PRStvgTVTEIYDYLR---LLFARVGIRERLGFLVDVGLGYLTLSRS--------------------------APTLSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15226227 220 EKKRLSLACELIAS-PSVIFA-DEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQP 275
Cdd:cd03270 142 EAQRIRLATQIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
90-298 |
2.13e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.86 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPS--SSKAYKLAFVRQEDLFFSqLTVR 167
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS-----EGKIKHSGRISfsSQFSWIMPGTIKENIIFG-VSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 E--TLSFAAELQLPE-ISSAEERDeyvNNLLLKLGLVscadscvgdakvrgISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:cd03291 126 EyrYKSVVKACQLEEdITKFPEKD---NTVLGEGGIT--------------LSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 245 GLDAFQAEKVMET-LQKLAQDGHTVICS--IHQPRgsvyaKFDDIVLLTEGTLVYAG 298
Cdd:cd03291 189 YLDVFTEKEIFEScVCKLMANKTRILVTskMEHLK-----KADKILILHEGSSYFYG 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
91-273 |
2.25e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNGK--------PSSSKAyKLAFVRQEDLFFS 162
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKnlyapdvdPVEVRR-RIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 QlTVRETLSFAAELQlpeiSSAEERDEYVNNLLLKLGLvscADSCVGDAKVRG--ISGGEKKRLSLACELIASPSVIFAD 240
Cdd:PRK14243 105 K-SIYDNIAYGARIN----GYKGDMDELVERSLRQAAL---WDEVKDKLKQSGlsLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|...
gi 15226227 241 EPTTGLDAFQAEKVMETLQKLAQDgHTVICSIH 273
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQ-YTIIIVTH 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
74-261 |
3.30e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 74 NITCSLSDKSsksvrfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQL-SLSPRLHLSGLLEVngkpssskAYkla 152
Cdd:PRK11147 324 NVNYQIDGKQ------LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLqADSGRIHCGTKLEV--------AY--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 153 fvrqedlfFSQLtvRETLSfaaelqlPEISS----AEERDEYVNNlllklGLVSCADSCVGD---------AKVRGISGG 219
Cdd:PRK11147 387 --------FDQH--RAELD-------PEKTVmdnlAEGKQEVMVN-----GRPRHVLGYLQDflfhpkramTPVKALSGG 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15226227 220 EKKRLSLACELIASPSVIFADEPTTGLDafqaekvMETLQKL 261
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLD-------VETLELL 479
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
91-269 |
3.60e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTTLLN-----VLAGQL-----------SLSPRLHLSGLLEVNGKP------SSSKA 148
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANRLngaktvpgrytSIEGLEHLDKVIHIDQSPigrtprSNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 149 YKLAF--VRQ--------------------------------------EDLFFSQLTV-----------RETL------- 170
Cdd:TIGR00630 704 YTGVFdeIRElfaetpeakvrgytpgrfsfnvkggrceacqgdgvikiEMHFLPDVYVpcevckgkrynRETLevkykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 SFAAELQLpeisSAEERDEYVNN---------LLLKLGLvscadscvGDAK----VRGISGGEKKRLSLACELIA---SP 234
Cdd:TIGR00630 784 NIADVLDM----TVEEAYEFFEAvpsisrklqTLCDVGL--------GYIRlgqpATTLSGGEAQRIKLAKELSKrstGR 851
|
250 260 270
....*....|....*....|....*....|....*
gi 15226227 235 SVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:TIGR00630 852 TLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
105-264 |
4.33e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 105 AIMGPSGSGKTTLLNVLAGqLSlSPRlhlSGLLEVNGK---PSSSKAY------KLAFVRQEDLFFSQLTVRETLSFAAe 175
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISG-LT-RPQ---KGRIVLNGRvlfDAEKGIClppekrRIGYVFQDARLFPHYKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 176 lqlpeissAEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVM 255
Cdd:PRK11144 102 --------AKSMVAQFDKIVALLGIEPLLDRYPGS-----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
....*....
gi 15226227 256 ETLQKLAQD 264
Cdd:PRK11144 169 PYLERLARE 177
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
85-247 |
5.88e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 85 KSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlsgllevNGKPSSSKAYKLAFVRQEDLFFSQL 164
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISAD-----------GGSYTFPGNWQLAWVNQETPALPQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 165 TV-------RETLSFAAELQlpeisSAEERDE--YVNNLLLKLGLV------SCADSCVG---------DAKVRGISGGE 220
Cdd:PRK10636 80 ALeyvidgdREYRQLEAQLH-----DANERNDghAIATIHGKLDAIdawtirSRAASLLHglgfsneqlERPVSDFSGGW 154
|
170 180
....*....|....*....|....*..
gi 15226227 221 KKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
79-274 |
6.32e-06 |
|
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: 49.91 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 79 LSDKSSKSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGlleVNGKPSSSKAYKLAF-VRQE 157
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDG---VSWNSVTLQTWRKAFgVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 158 DLFFSQLTVRETLSFAAELQLPEI-SSAEE--RDEYVNNLLLKLGLVSCADSCVgdakvrgISGGEKKRLSLACELIASP 234
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEEIwKVAEEvgLKSVIEQFPDKLDFVLVDGGYV-------LSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15226227 235 SVIFADEPTTGLDAFQAEKVMETLQKLAQDGhTVICSIHQ 274
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEHR 1411
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
42-273 |
8.00e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 42 IALLPEdEAEDDYAE------TEDGGGDsirpVTIRWRNITCslsdkssksvRF----LLKNVSGEAKPGRLLAIMGPSG 111
Cdd:NF033858 238 IALLPE-EKRRGHQPvvipprPADDDDE----PAIEARGLTM----------RFgdftAVDHVSFRIRRGEIFGFLGSNG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 112 SGKTTLLNVLagqlslsprlhlSGLLEvngkPSSSKAyKLaF---VRQEDL-------FFSQ-------LTVRETLSFAA 174
Cdd:NF033858 303 CGKSTTMKML------------TGLLP----ASEGEA-WL-FgqpVDAGDIatrrrvgYMSQafslygeLTVRQNLELHA 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 175 EL-QLPEissaEERDEYVNNLLLKLGLVSCADSCVGDakvrgISGGEKKRLSLACELIASPSVIFADEPTTGLD-----A 248
Cdd:NF033858 365 RLfHLPA----AEIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvardM 435
|
250 260
....*....|....*....|....*.
gi 15226227 249 FqaekvMETLQKLA-QDGHTVICSIH 273
Cdd:NF033858 436 F-----WRLLIELSrEDGVTIFISTH 456
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
90-298 |
8.02e-06 |
|
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: 49.52 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVNGKPSSSKAYKLAF---VRQEDLF-FSQLT 165
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS-----EGKIKHSGRISFSPQTSWIMpgtIKDNIIFgLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETlSFAAELQLPE-ISSAEERDEYVnnlllklglvscadscVGDAKVRgISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:TIGR01271 516 YRYT-SVIKACQLEEdIALFPEKDKTV----------------LGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 245 GLDAFQAEKVMET-LQKLAQDGHTVICSihqPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:TIGR01271 578 HLDVVTEKEIFEScLCKLMSNKTRILVT---SKLEHLKKADKILLLHEGVCYFYG 629
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
217-298 |
8.28e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 217 SGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGsVYAKFDDIVLltegtLVY 296
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG-VVAGICDKVL-----VMY 236
|
..
gi 15226227 297 AG 298
Cdd:PRK09473 237 AG 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
90-274 |
1.20e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGlleVNGKPSSSKAYKLAF--VRQEDLFFSQlTVR 167
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDG---VSWNSVPLQKWRKAFgvIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSFAAELQLPEI-SSAEE--RDEYVNNLLLKLGLVSCADSCVgdakvrgISGGEKKRLSLACELIASPSVIFADEPTT 244
Cdd:cd03289 95 KNLDPYGKWSDEEIwKVAEEvgLKSVIEQFPGQLDFVLVDGGCV-------LSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190
....*....|....*....|....*....|
gi 15226227 245 GLDAFQAEKVMETLqKLAQDGHTVICSIHQ 274
Cdd:cd03289 168 HLDPITYQVIRKTL-KQAFADCTVILSEHR 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
90-261 |
2.25e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlsgllevNGKPSSSKAYKLAFVRQ--EDLFFSQLTVR 167
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD-----------SGTVKWSENANIGYYAQdhAYDFENDLTLF 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 168 ETLSfaaelqlpEISSAEERDEYVNNLLLKLgLVSCADScvgDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:PRK15064 403 DWMS--------QWRQEGDDEQAVRGTLGRL-LFSQDDI---KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170
....*....|....
gi 15226227 248 afqaekvMETLQKL 261
Cdd:PRK15064 471 -------MESIESL 477
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
217-269 |
2.29e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.10 E-value: 2.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 217 SGGEKKRLSLACEL--IASPSVIFA-DEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:COG0178 828 SGGEAQRVKLASELskRSTGKTLYIlDEPTTGLHFHDIRKLLEVLHRLVDKGNTVV 883
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
105-299 |
2.73e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 105 AIMGPSGSGKTTLLNVLAGQLSLsprlhLSGllevngkpssskayklafVRQEDlfFSQLTvreTLSFAaelQLPEISSA 184
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPL-----LSG------------------ERQSQ--FSHIT---RLSFE---QLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 185 EERDEyvNNLLLKLGL--------------VSCADSCVGDAKVRGI-----------SGGEKKRLSLACELIASPSVIFA 239
Cdd:PRK10938 82 EWQRN--NTDMLSPGEddtgrttaeiiqdeVKDPARCEQLAQQFGItalldrrfkylSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 240 DEPTTGLDAFQAEKVMETLQKLAQDGHTVICsihqprgsVYAKFDDI-------VLLTEGTLVYAGP 299
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGITLVL--------VLNRFDEIpdfvqfaGVLADCTLAETGE 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
161-276 |
3.25e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 161 FSQLTVRETLSFAAELQLPEISSAEERDEYVNNL--LLKLGLVSCADscvgDAKVRGISGGEKKRLSLACELIASPSVI- 237
Cdd:PRK00635 424 FQQMSLQELFIFLSQLPSKSLSIEEVLQGLKSRLsiLIDLGLPYLTP----ERALATLSGGEQERTALAKHLGAELIGIt 499
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15226227 238 -FADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPR 276
Cdd:PRK00635 500 yILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ 539
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
88-261 |
4.79e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSGLLEVngkpssSKAYKLAFVRQ--EDLFFSQlT 165
Cdd:PRK11819 337 RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD-----SGTIKI------GETVKLAYVDQsrDALDPNK-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 VRETLSFAAE-LQLP--EISSaeeRdEYVNNLLLKlGlvscadscvGD--AKVRGISGGEKKRLSLACELIASPSVIFAD 240
Cdd:PRK11819 405 VWEEISGGLDiIKVGnrEIPS---R-AYVGRFNFK-G---------GDqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170 180
....*....|....*....|.
gi 15226227 241 EPTTGLDafqaekvMETLQKL 261
Cdd:PRK11819 471 EPTNDLD-------VETLRAL 484
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
88-292 |
7.75e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 45.05 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 88 RFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlslsprlhlsglLEvngKPSS----SKAYKLAFVRQED-LFFS 162
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-------------LE---TPSAgellAGTAPLAEAREDTrLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 163 Q--------------LTVRETLSFAAELQLPEISSAEERDEYVNNLllklglvscadscvgdakvrgiSGGEKKRLSLAC 228
Cdd:PRK11247 89 DarllpwkkvidnvgLGLKGQWRDAALQALAAVGLADRANEWPAAL----------------------SGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 229 ELIASPSVIFADEPTTGLDAFQAEKVMETLQKL-AQDGHTVICSIHQPRGSVyAKFDDIVLLTEG 292
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEG 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
100-125 |
8.32e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 8.32e-05
10 20
....*....|....*....|....*.
gi 15226227 100 PGRLLAIMGPSGSGKTTLLNVLAGQL 125
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL 26
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
91-298 |
8.94e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTT-------LLNVLAGQLSLSPRLHLSGLLEVNGKPSSSKAyKLAFVRQEDL--FF 161
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAA-QMRHVRGADMamIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 162 SQLTVRETLSFAAELQLPE---ISSAEERDEYVNNLLLKLGLVSCADSCVGDAKV-RGISGGEKKRLSLACELIASPSVI 237
Cdd:PRK10261 111 QEPMTSLNPVFTVGEQIAEsirLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYpHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 238 FADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAG 298
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
91-264 |
2.42e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 91 LKNVSGEAKPGRLLAIMGPSGSGKTT----LLNVLAGQlslsprlhlSGLLEVNGKPSSS-KAYKLAFVRQEDLFFSQ-- 163
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQ---------GGEIIFNGQRIDTlSPGKLQALRRDIQFIFQdp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 164 ---LTVRETL--SFAAELQLPEISSAEERDEYVNNLLLKLGLVScadscvgDAKVR---GISGGEKKRLSLACELIASPS 235
Cdd:PRK10261 411 yasLDPRQTVgdSIMEPLRVHGLLPGKAAAARVAWLLERVGLLP-------EHAWRyphEFSGGQRQRICIARALALNPK 483
|
170 180
....*....|....*....|....*....
gi 15226227 236 VIFADEPTTGLDAFQAEKVMETLQKLAQD 264
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRD 512
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-306 |
2.57e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 151 LAFVRQEDLFFSqLTVRETLSFAAELQLPE----ISSAEERDEYVNNLLLKLglvscaDSCVGDAKvRGISGGEKKRLSL 226
Cdd:PTZ00265 1298 FSIVSQEPMLFN-MSIYENIKFGKEDATREdvkrACKFAAIDEFIESLPNKY------DTNVGPYG-KSLSGGQKQRIAI 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 227 ACELIASPSVIFADEPTTGLDAfQAEKVME-TLQKLAQDGHTVICSIHQPRGSVyAKFDDIVLLTE----GTLVYAGPAG 301
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDS-NSEKLIEkTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNNpdrtGSFVQAHGTH 1447
|
....*
gi 15226227 302 KEPLT 306
Cdd:PTZ00265 1448 EELLS 1452
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
85-166 |
3.15e-04 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 42.25 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 85 KSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEvnGKPSSSKAYKLAFVRQEDLFFSQL 164
Cdd:pfam03215 29 KDVQEWLDAMFLENAKHRILLISGPSGCGKSTVIKELSKELGPKYREWSNPTSF--RSPPNQVTDFRGDCIVNSRFLSQM 106
|
..
gi 15226227 165 TV 166
Cdd:pfam03215 107 ES 108
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
86-264 |
4.75e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 43.52 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 86 SVRF--------LLKNVSGEAKPGRLLAIMGPSGSGKT-TLLNVL----------------AGQ--LSLSPRlhlsGLLE 138
Cdd:COG4172 13 SVAFgqgggtveAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpdpaahpsgsilfDGQdlLGLSER----ELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 139 VNGKpssskayKLAFVRQEDLffSQLT--------VRETLSF-------AAE------LQLPEISSAEER-DEYVNNLll 196
Cdd:COG4172 89 IRGN-------RIAMIFQEPM--TSLNplhtigkqIAEVLRLhrglsgaAARaralelLERVGIPDPERRlDAYPHQL-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226227 197 klglvscadscvgdakvrgiSGGEKKR----LSLACEliasPSVIFADEPTTGLDA-FQAEkVMETLQKLAQD 264
Cdd:COG4172 158 --------------------SGGQRQRvmiaMALANE----PDLLIADEPTTALDVtVQAQ-ILDLLKDLQRE 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
101-261 |
6.86e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.39 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 101 GRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlSG--------LLEVNGKPSSSKAYKLAFVRQEDLffSQLTVRETLS- 171
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKAT-----DGevawlgkdLLGMKDDEWRAVRSDIQMIFQDPL--ASLNPRMTIGe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 172 -FAAELQL--PEISSAEERDEyVNNLLLKLGLVSCadscVGDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD- 247
Cdd:PRK15079 120 iIAEPLRTyhPKLSRQEVKDR-VKAMMLKVGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDv 194
|
170
....*....|....
gi 15226227 248 AFQAEkVMETLQKL 261
Cdd:PRK15079 195 SIQAQ-VVNLLQQL 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
73-269 |
1.10e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 73 RNITcslsdKSSKSVRfLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGqlsLSPRLHLSGLLEVNGKP------SSS 146
Cdd:PRK13549 9 KNIT-----KTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYPHGTYEGEIIFEGEElqasniRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 147 KAYKLAFVRQEDLFFSQLTVRETLSFAAELQLPEISSAEERDEYVNNLLLKLGLvscaDSCVgDAKVRGISGGEKKRLSL 226
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKL----DINP-ATPVGNLGLGQQQLVEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15226227 227 ACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACI 197
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
101-127 |
1.12e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.60 E-value: 1.12e-03
10 20
....*....|....*....|....*..
gi 15226227 101 GRLLAIMGPSGSGKTTLLNVLAGQLSL 127
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDL 132
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
100-142 |
1.15e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 40.82 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15226227 100 PGRLLAIMGPSGSGKTTLLNVLagqLSLSPRLHLS----------GllEVNGK 142
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKAL---LERDPDLRFSvsattrpprpG--EVDGV 48
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
217-269 |
1.30e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15226227 217 SGGEKKRLSLACELIASP---SVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVV 887
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
90-247 |
1.32e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 90 LLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSprlhlsgllevNGKpssskayklaFVRQEDLFFSQLT---- 165
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD-----------DGR----------IIYEQDLIVARLQqdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 166 ----------VRETLSFAAEL------------------QLPEISSAEER---------DEYVNNLLLKLGLVscadscv 208
Cdd:PRK11147 77 rnvegtvydfVAEGIEEQAEYlkryhdishlvetdpsekNLNELAKLQEQldhhnlwqlENRINEVLAQLGLD------- 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 15226227 209 GDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLD 247
Cdd:PRK11147 150 PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
101-127 |
1.40e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 1.40e-03
10 20
....*....|....*....|....*..
gi 15226227 101 GRLLAIMGPSGSGKTTLLNVLAGQLSL 127
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVL 111
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
444-591 |
1.79e-03 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 41.22 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 444 MGLLQVAAINTAMAAltktvgVFPKERAIVDRERSKGsYSLGPYLLSKTIAE-----IPIGAAFPLMFGAVLypmarlnp 518
Cdd:pfam12698 169 MIIILIGAAIIAVSI------VEEKESRIKERLLVSG-VSPLQYWLGKILGDflvglLQLLIILLLLFGIGI-------- 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226227 519 TLSRFGKFCGIVTVESFAASAMGLTVGAMVPSTEAAMAVGPSLMTVFIVFGGYYVNADNTP----IIFRWIPRASLI 591
Cdd:pfam12698 234 PFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPsflqWIFSIIPFFSPI 310
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
209-298 |
2.16e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 209 GDAKVRGISGGEKKRLSLACELIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICsihqprgsVYAKFDDIVL 288
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF--------ISSDLEEIEQ 468
|
90
....*....|
gi 15226227 289 LTEGTLVYAG 298
Cdd:PRK15439 469 MADRVLVMHQ 478
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
85-137 |
2.28e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129690 [Multi-domain] Cd Length: 637 Bit Score: 41.48 E-value: 2.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15226227 85 KSVRFLLKNVSGEAKPGRLLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLL 137
Cdd:TIGR00602 94 EEVETWLKAQVLENAPKRILLITGPSGCGKSTTIKILSKELGIQVQEWSNPTL 146
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-269 |
2.37e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 154 VRQEDLFFSQLTVRETLSFAAELQLPEISsaeERDEYVNNLLLK-LGLVSCADScvgdakvrgISGGEKKRLSLACELIA 232
Cdd:TIGR00630 438 IREAHEFFNQLTLTPEEKKIAEEVLKEIR---ERLGFLIDVGLDyLSLSRAAGT---------LSGGEAQRIRLATQIGS 505
|
90 100 110
....*....|....*....|....*....|....*....
gi 15226227 233 SPS-VIFA-DEPTTGLDAFQAEKVMETLQKLAQDGHTVI 269
Cdd:TIGR00630 506 GLTgVLYVlDEPSIGLHQRDNRRLINTLKRLRDLGNTLI 544
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
103-141 |
4.00e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 36.55 E-value: 4.00e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15226227 103 LLAIMGPSGSGKTTLLNVLAGQLSLSPRLHLSGLLEVNG 141
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVLDEIVILEG 39
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
93-300 |
4.35e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 93 NVSGEAKPGRLLAIMGPSGSGKttllnvlagqlSLSpRLHLSGLLEVNGKPSsskAYKLAFVRQEDLFFSQLTVRETL-- 170
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGK-----------SVS-SLAIMGLIDYPGRVM---AEKLEFNGQDLQRISEKERRNLVga 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226227 171 ---------------SFAAELQLPEI------SSAEERDEYVNNLLLKLGLVSCADSCvgDAKVRGISGGEKKRLSLACE 229
Cdd:PRK11022 90 evamifqdpmtslnpCYTVGFQIMEAikvhqgGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226227 230 LIASPSVIFADEPTTGLDAFQAEKVMETLQKLAQDGHTVICSIHQPRGSVYAKFDDIVLLTEGTLVYAGPA 300
Cdd:PRK11022 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
102-126 |
4.77e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 39.05 E-value: 4.77e-03
10 20
....*....|....*....|....*
gi 15226227 102 RLLAIMGPSGSGKTTLLNVLAGQLS 126
Cdd:COG0572 8 RIIGIAGPSGSGKTTFARRLAEQLG 32
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
105-124 |
6.10e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.21 E-value: 6.10e-03
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
102-152 |
6.41e-03 |
|
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.
Pssm-ID: 468038 Cd Length: 149 Bit Score: 37.86 E-value: 6.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15226227 102 RLLAIMGPSGSGKTTLLNVLAGQLSLSP---RLHLS-GLLEVngkPSSSKAYKLA 152
Cdd:NF033453 17 KLILLVGPPGSGKTALLRELAAKRGAPVinvNLELSrRLLEL---PEKQRALRAP 68
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
99-124 |
8.51e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 8.51e-03
10 20
....*....|....*....|....*.
gi 15226227 99 KPGRLLAIMGPSGSGKTTLLNVLAGQ 124
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVNALLGE 218
|
|
| |
