|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-532 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 671.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDKVTVFE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 ETMKAFEEVTQMQKELDELNEQLtirtdyetDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQTSE 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKL--------AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 164 FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIYDYKA 243
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 244 KYSHYLQLRADRRIHQLKAYEEQQRFIADNQEFIDRFRGTYSKTLQVQSRVKMLEKLEVIEIDEVDtSALRLKFPPSPRS 323
Cdd:COG0488 233 NYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRD-KTVEIRFPPPERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 324 GQYPVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKVGHNAKIGYFAQNQAAlL 402
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGtVKLGETVKIGYFDQHQEE-L 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 403 DENLTVFETIDQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDI 482
Cdd:COG0488 391 DPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1525942895 483 IKDALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREHFEDIKGFLAY 532
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-536 |
5.22e-112 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 343.03 E-value: 5.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDKVT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMQKELDEL--NEQLTirtdyeTDDYMKlierVSELSEKFysIEETNYDAEVE--KVLKGLGFERKD 156
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIyaLPEMS------EEDGMK----VADLEVKF--AEMDGYTAEARagELLLGVGIPEEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 157 FTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLiNSAKAVMV-ISHDRAFVDNITNRTIEVTM 235
Cdd:PRK15064 149 HYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL-NERNSTMIiISHDRHFLNSVCTHMADLDY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 236 GRIYDYKAKYSHYLQLRADRRIHQLKAYEEQQRFIADNQEFIDRFRGTYSKTLQVQSRVKMLEKlevIEIDEVDtsalrl 315
Cdd:PRK15064 228 GELRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDK---IKLEEVK------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 316 kfpPSPRsgQYP--------------VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDF-E 380
Cdd:PRK15064 299 ---PSSR--QNPfirfeqdkklhrnaLEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPdS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 381 GGLKVGHNAKIGYFAQNQAALLDENLTVFETIDQ-IPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLL 459
Cdd:PRK15064 374 GTVKWSENANIGYYAQDHAYDFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIKDALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVrehfEDIKG----FLAYKKM 535
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV----VDFSGtyeeYLRSQGI 529
|
.
gi 1525942895 536 D 536
Cdd:PRK15064 530 E 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-534 |
2.56e-106 |
|
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: 329.20 E-value: 2.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 12 GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDKVTVFEETMKAFEE 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 92 VTQMQKELDELNEQLTirtdYETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDftRQTSEFSGGWRMR 171
Cdd:TIGR03719 96 IKDALDRFNEISAKYA----EPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWD--ADVTKLSGGERRR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 172 IELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIYDYKAKYSHYLQL 251
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 252 RADRRIHQLKAYEEQQRFIADNQEFID---RFRGTYSKtlqvqSRVKMLEKLEVIEIDEVDTSAlRLKFPPSPRSGQYPV 328
Cdd:TIGR03719 250 KQKRLEQEEKEESARQKTLKRELEWVRqspKGRQAKSK-----ARLARYEELLSQEFQKRNETA-EIYIPPGPRLGDKVI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 329 MVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-NEIDFEGGLKVGHNAKIGYFAQNQAAlLDENLT 407
Cdd:TIGR03719 324 EAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITgQEQPDSGTIEIGETVKLAYVDQSRDA-LDPNKT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 VFETI----DQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDII 483
Cdd:TIGR03719 403 VWEEIsgglDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 484 KDALKDFDGTLILVSHDRDFLDGLVQKVFEF-GNKRVrEHFE-DIKGFLAYKK 534
Cdd:TIGR03719 483 EEALLNFAGCAVVISHDRWFLDRIATHILAFeGDSHV-EWFEgNFSEYEEDKK 534
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-505 |
4.60e-102 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 318.22 E-value: 4.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFggttlFSDVtfsinendKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQH-LLTQDKvTVFEE 84
Cdd:PRK11819 25 DISLSF-----FPGA--------KIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpQLDPEK-TVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 85 TMKAFEEVTQMQKELDELNEQLTirtdyETDDYM-KLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDftRQTSE 163
Cdd:PRK11819 91 VEEGVAEVKAALDRFNEIYAAYA-----EPDADFdALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWD--AKVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 164 FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIYDYKA 243
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 244 KYSHYLQLRADRRIHQLKAYEEQQRFIADNQEFID---RFRGTYSK-------TLQVQSRVKMLEKLEvIEIdevdtsal 313
Cdd:PRK11819 244 NYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRqspKARQAKSKarlaryeELLSEEYQKRNETNE-IFI-------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 314 rlkfPPSPRSGQYPVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-EIDFEGGLKVGHNAKIG 392
Cdd:PRK11819 315 ----PPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGqEQPDSGTIKIGETVKLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 393 YFAQNQAAlLDENLTVFETI----DQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLIL 468
Cdd:PRK11819 391 YVDQSRDA-LDPNKTVWEEIsgglDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
490 500 510
....*....|....*....|....*....|....*..
gi 1525942895 469 DEPTNHLDMKTKDIIKDALKDFDGTLILVSHDRDFLD 505
Cdd:PRK11819 470 DEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLD 506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-504 |
1.34e-100 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 317.11 E-value: 1.34e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDkVT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP-QP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMQKELDELNEQltirtdyeTDDYMklierVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQ 160
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQLHDANER--------NDGHA-----IATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIYD 240
Cdd:PRK10636 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 241 YKAKYSHYLQLRADRRIHQLKAYEEQQRFIADNQEFIDRFRGTYSKTLQVQSRVKMLEKLEVIEIDEVDtSALRLKFpPS 320
Cdd:PRK10636 227 YTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVD-NPFHFSF-RA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 321 PRSGQYPVM-VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVGHNAKIGYFAQNQ 398
Cdd:PRK10636 305 PESLPNPLLkMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELApVSGEIGLAKGIKLGYFAQHQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AALLDENLTVFETIDQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMK 478
Cdd:PRK10636 385 LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
490 500
....*....|....*....|....*.
gi 1525942895 479 TKDIIKDALKDFDGTLILVSHDRDFL 504
Cdd:PRK10636 465 MRQALTEALIDFEGALVVVSHDRHLL 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-521 |
5.12e-85 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 276.06 E-value: 5.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDKVT 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMQKELDELNEQLtirtdyETDDYMKLIERVSELSEKfysIEETN---YDAEVEKVLKGLGFerkDF 157
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLV------ETDPSEKNLNELAKLQEQ---LDHHNlwqLENRINEVLAQLGL---DP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 158 TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGR 237
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 238 IYDYKAKYSHYLQLRADrrihQLKAYEEQqrfiadNQEFiDR---------FRGTYSKTLQVQSRVKMLEKL--EVIEID 306
Cdd:PRK11147 231 LVSYPGNYDQYLLEKEE----ALRVEELQ------NAEF-DRklaqeevwiRQGIKARRTRNEGRVRALKALrrERSERR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 307 EVDTSAlRLKFPPSPRSGQYPVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKV 385
Cdd:PRK11147 300 EVMGTA-KMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrIHC 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 386 GHNAKIGYFAQNQAAlLDENLTVFETidqipLTDGSIKI------KDLLG---AFMFSGDDTTKKVKVLSGGEKTRLAMI 456
Cdd:PRK11147 379 GTKLEVAYFDQHRAE-LDPEKTVMDN-----LAEGKQEVmvngrpRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLA 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 457 KLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDFDGTLILVSHDRDFLDGLVQK--VFEfGNKRVRE 521
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFE-GNGKIGR 518
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-535 |
7.42e-73 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 245.92 E-value: 7.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAkpttgnVTG-PKEAVIAYLPQHLLTqDKVT 80
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHA------IDGiPKNCQILHVEQEVVG-DDTT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQ-MQKELDELNEQLTIRTDYET-DDYMKLI---------ERVSELSEKFYSIEETNYDAEVEKVLKG 149
Cdd:PLN03073 251 ALQCVLNTDIERTQlLEEEAQLVAQQRELEFETETgKGKGANKdgvdkdavsQRLEEIYKRLELIDAYTAEARAASILAG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNR 229
Cdd:PLN03073 331 LSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 230 TIEVTMGRIYDYKAKYSHYLQLRADRRIHQLKAYEEQQRFIADNQEFIDRFRGTYSKTLQVQSRVKMLEKLEviEIDEV- 308
Cdd:PLN03073 411 ILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLG--HVDAVv 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 309 DTSALRLKFP-PSPRSGQYPVMVEELTKTY-GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVG 386
Cdd:PLN03073 489 NDPDYKFEFPtPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG-TVF 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 387 HNAK--IGYFAQNQAALLDEN----LTVFETIDQIPltdgSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLL 460
Cdd:PLN03073 568 RSAKvrMAVFSQHHVDGLDLSsnplLYMMRCFPGVP----EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 461 EPVNVLILDEPTNHLDMKTKDIIKDALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREHFediKGFLAYKKM 535
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFH---GTFHDYKKT 715
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-250 |
2.60e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 199.52 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHlltqdkvt 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 vfeetmkafeevtqmqkeLDELNEQLTirtdyetddymkLIERVSELSEKfysieetNYDAEVEKVLKGLGFERKDFTRQ 160
Cdd:COG0488 387 ------------------QEELDPDKT------------VLDELRDGAPG-------GTEQEVRGYLGRFLFSGDDAFKP 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIYD 240
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
250
....*....|
gi 1525942895 241 YKAKYSHYLQ 250
Cdd:COG0488 510 YPGGYDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
330-518 |
3.65e-53 |
|
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: 176.87 E-value: 3.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEI-DFEGGLKVGHNAKIGYFAQnqaalldenltv 408
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELePDEGIVTWGSTVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 409 fetidqipltdgsikikdllgafmfsgddttkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALK 488
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 1525942895 489 DFDGTLILVSHDRDFLDGLVQKVFEFGNKR 518
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-234 |
8.28e-49 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 165.31 E-value: 8.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQhlltqdkvtv 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 feetmkafeevtqmqkeldelneqltirtdyetddymkliervselsekfysieetnydaevekvlkglgferkdftrqt 161
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 162 seFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVT 234
Cdd:cd03221 71 --LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELE 141
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-500 |
9.12e-38 |
|
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: 145.82 E-value: 9.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF--GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAkPTTGNVTG---PKEAVIAYLPQHLLT 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISGevlLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 76 QDKVTVFEETMKAFEEVTQMqkelDELNEqlTIRTDYETDDYMKliervselsekfysieetnydAEVEKVLKGLGFERK 155
Cdd:COG1123 83 RRIGMVFQDPMTQLNPVTVG----DQIAE--ALENLGLSRAEAR---------------------ARVLELLEAVGLERR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 156 dFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD----IESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTI 231
Cdd:COG1123 136 -LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 232 EVTMGRIydykakyshylqlradrrihqlkayeeqqrfiadnqefidRFRGTyskTLQVQSRVKMLEklevieidEVDTS 311
Cdd:COG1123 215 VMDDGRI----------------------------------------VEDGP---PEEILAAPQALA--------AVPRL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 312 ALRLKFPPSPRSGQYPVM-VEELTKTY-----GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EID 378
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLeVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgSIL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 379 FEG----GLKVG----HNAKIGYFAQNQAALLDENLTVFETIDQiPLtdgsikikDLLGafMFSGDDTTKKV-----KV- 444
Cdd:COG1123 324 FDGkdltKLSRRslreLRRRVQMVFQDPYSSLNPRMTVGDIIAE-PL--------RLHG--LLSRAERRERVaelleRVg 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 445 ------------LSGGEKTRLAMIK-LLLEPvNVLILDEPTNHLDMKTKDIIKDALKD----FDGTLILVSHD 500
Cdd:COG1123 393 lppdladrypheLSGGQRQRVAIARaLALEP-KLLILDEPTSALDVSVQAQILNLLRDlqreLGLTYLFISHD 464
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-238 |
7.97e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.85 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV--------TGPKEAV---IAYLPQh 72
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsAMPPPEWrrqVAYVPQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 lltqdKVTVFEETMKAFeevtqmqkeldelneqltirtdyetddymklIERVSELSEKFYSIEEtnydaeVEKVLKGLGF 152
Cdd:COG4619 82 -----EPALWGGTVRDN-------------------------------LPFPFQLRERKFDRER------ALELLERLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 153 ERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINSAKAVMVISHDRAFVDNITN 228
Cdd:COG4619 120 PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVAD 199
|
250
....*....|
gi 1525942895 229 RTIEVTMGRI 238
Cdd:COG4619 200 RVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
2.57e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT------GPKEAVIAYLPQHlL 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQR-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDK---VTVfeetmkafEEVTQMqkeldelneqltirtdyetddymkliERVSELS-EKFYSIEEtnyDAEVEKVLK-- 148
Cdd:COG1121 85 EVDWdfpITV--------RDVVLM--------------------------GRYGRRGlFRRPSRAD---REAVDEALErv 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GLGfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSA-KAVMVISHDRAFVDN 225
Cdd:COG1121 128 GLE-DLAD--RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLreLRREgKTILVVTHDLGAVRE 204
|
250
....*....|....*
gi 1525942895 226 ITNRTIEVTMGRIYD 240
Cdd:COG1121 205 YFDRVLLLNRGLVAH 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
330-519 |
1.16e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGGLKVGHNA-----KIGYFAQn 397
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADldpptsgEIYLDGKPLSAMPPpewrrQVAYVPQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAALLDEnlTV---FETIDQI-PLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIK-LLLEPvNVLILDEPT 472
Cdd:COG4619 82 EPALWGG--TVrdnLPFPFQLrERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQP-DVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 473 NHLDMKTKDIIKDALKDF----DGTLILVSHDRDFLDGLVQKVFEFGNKRV 519
Cdd:COG4619 159 SALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
6.71e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.47 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--------GPKEA--VIAYLPQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HlltqdkvtvfeetmkafeevtqmqkelDELNEQLTIRtdyetdDYMKLIERvselsekFYSIEETNYDAEVEKVLKGLG 151
Cdd:COG1131 81 E---------------------------PALYPDLTVR------ENLRFFAR-------LYGLPRKEARERIDELLELFG 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 152 F-ERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSA---KAVMVISHD 219
Cdd:COG1131 121 LtDAAD--RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAaegKTVLLSTHY 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-238 |
2.28e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.11 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaylpqhllTQDKVT 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI----------------LIDGED 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMQKElDELNEQLTIRtdyetddymKLIERVSELsekfYSIEETNYDAEVEKVLKGLGFErkDFT-R 159
Cdd:COG4555 65 VRKEPREARRQIGVLPDE-RGLYDRLTVR---------ENIRYFAEL----YGLFDEELKKRIEELIELLGLE--EFLdR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI---NSAKAVMVISHDRAFVDNITNRTIEVTMG 236
Cdd:COG4555 129 RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRalkKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
..
gi 1525942895 237 RI 238
Cdd:COG4555 209 KV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
330-500 |
3.85e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.46 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDF-EGGLKV-GHN---------AKIGYFAQNQ 398
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVlGEDvardpaevrRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AalLDENLTVFETID------QIPLTDGSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:COG1131 83 A--LYPDLTVRENLRffarlyGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190
....*....|....*....|....*....|.
gi 1525942895 473 NHLDMKTKDIIKDALKDF---DGTLILVSHD 500
Cdd:COG1131 160 SGLDPEARRELWELLRELaaeGKTVLLSTHY 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
330-541 |
1.16e-27 |
|
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: 111.10 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-----------LKVGHNAKIGYFAQNQ 398
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsilidgedvrkEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AalLDENLTVFETID------QIPLTDGSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:COG4555 84 G--LYDRLTVRENIRyfaelyGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 473 NHLDMKTKDIIKD---ALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREHfEDIKGFLAYKKMDNLKEI 541
Cdd:COG4555 161 NGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ-GSLDELREEIGEENLEDA 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-238 |
2.69e-27 |
|
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: 107.87 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--------GPKEAV--IAYLPQ 71
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkEPEEVKrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HlltqdkvtvfeetmkafeevtqmqkelDELNEQLTIRtdyetdDYMKLiervselsekfysieetnydaevekvlkglg 151
Cdd:cd03230 81 E---------------------------PSLYENLTVR------ENLKL------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 ferkdftrqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSA---KAVMVISHDRAFVDNITN 228
Cdd:cd03230 97 -------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCD 163
|
250
....*....|
gi 1525942895 229 RTIEVTMGRI 238
Cdd:cd03230 164 RVAILNNGRI 173
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
231-315 |
4.32e-27 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 104.58 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 231 IEVTMGRIYDYKAKYSHYLQLRADRRIHQLKAYEEQQRFIADNQEFIDRFRGTYSKTLQVQSRVKMLEKLEVIEIDEVDT 310
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 1525942895 311 SALRL 315
Cdd:pfam12848 81 PKLRF 85
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-234 |
1.19e-26 |
|
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: 107.18 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV----------IAYLP 70
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaredyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 QHlltqdkvtvfeetmkafeevtqmqkelDELNEQLTIRtdyetdDYMKLIERVSELSEKfysieetnyDAEVEKVLKGL 150
Cdd:COG4133 82 HA---------------------------DGLKPELTVR------ENLRFWAALYGLRAD---------REAIDEALEAV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 151 GFE-RKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA----VMVISHDRAFVDN 225
Cdd:COG4133 120 GLAgLAD--LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAE-LIAAHLArggaVLLTTHQPLELAA 196
|
....*....
gi 1525942895 226 itNRTIEVT 234
Cdd:COG4133 197 --ARVLDLG 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-219 |
1.30e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 108.59 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKE--AVIAYL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHLLTQDKVTVFEetmkafeevtqmqkeldelneqlTI---RTdyetdDYMKLIERVSELSEkfysieetnydAEVEKV 146
Cdd:COG1120 81 PQEPPAPFGLTVRE-----------------------LValgRY-----PHLGLFGRPSAEDR-----------EAVEEA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 147 LKGLG---FERKDFTrqtsEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHD 219
Cdd:COG1120 122 LERTGlehLADRPVD----ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
330-500 |
4.80e-26 |
|
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: 104.40 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKV-GHNA---------KIGYFAQNq 398
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGeIKVlGKDIkkepeevkrRIGYLPEE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 aALLDENLTVFETIDqipltdgsikikdllgafmfsgddttkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMK 478
Cdd:cd03230 82 -PSLYENLTVRENLK-------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180
....*....|....*....|....*
gi 1525942895 479 TKDIIKDALKDF---DGTLILVSHD 500
Cdd:cd03230 130 SRREFWELLRELkkeGKTILLSSHI 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-226 |
5.70e-26 |
|
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: 111.57 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQ--HLLTQDKv 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrDALDPNK- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TVFEETMkafeevtqmqkeldelneqltirtdyETDDYMKLIERvselsekfysieETNYDAEVEKvlkgLGFERKDFTR 159
Cdd:TIGR03719 402 TVWEEIS--------------------------GGLDIIKLGKR------------EIPSRAYVGR----FNFKGSDQQK 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNI 226
Cdd:TIGR03719 440 KVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-239 |
6.75e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 105.31 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT------GPKEAVIAYLPQH--LLT 75
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRrsIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 76 QDKVTVFEETMKAFeevtqmqkeldelneqltirtdyetDDYMKLIERVSElSEKfysieetnydAEVEKVLKGLG-FER 154
Cdd:cd03235 82 DFPISVRDVVLMGL-------------------------YGHKGLFRRLSK-ADK----------AKVDEALERVGlSEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 KDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA----VMVISHDRAFVDNITNRT 230
Cdd:cd03235 126 AD--RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE-LLRELRRegmtILVVTHDLGLVLEYFDRV 202
|
....*....
gi 1525942895 231 IEVTMGRIY 239
Cdd:cd03235 203 LLLNRTVVA 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-192 |
1.33e-25 |
|
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: 102.34 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 17 FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV-----------IAYLPQHlltqdkvtvfeet 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkeIGYVFQD------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 86 mkafeevtqmqkelDELNEQLTIRTDyetddymkLIERVSelsekFYSIEETNYDAEVEKVLKGLGFE--RKDF-TRQTS 162
Cdd:pfam00005 68 --------------PQLFPRLTVREN--------LRLGLL-----LKGLSKREKDARAEEALEKLGLGdlADRPvGERPG 120
|
170 180 190
....*....|....*....|....*....|
gi 1525942895 163 EFSGGWRMRIELAKILLKKPDLILLDEPTN 192
Cdd:pfam00005 121 TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-237 |
4.55e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 101.17 E-value: 4.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLtqdkvtvfe 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 etmkafeevtqmqkeldelneqltirtdyetddymKLIERVSELSekfysieetnydaevekvlkglgferkdftrqtse 163
Cdd:cd00267 73 -----------------------------------RRIGYVPQLS----------------------------------- 82
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 164 fsGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK---AVMVISHDRAFVDNITNRTIEVTMGR 237
Cdd:cd00267 83 --GGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-238 |
8.03e-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: 102.58 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaYLPQHLLTQ 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII--------FDGKDLLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DkvtvfEETMKAFEEVTQM--QKELDELNEQLTIRtdyetddymKLIERVseLSEKFYSIEETNYDAEVEKVLKGLGFER 154
Cdd:cd03257 73 S-----RRLRKIRRKEIQMvfQDPMSSLNPRMTIG---------EQIAEP--LRIHGKLSKKEARKEAVLLLLVGVGLPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 KDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQW-LEDFLINSAK----AVMVISHDRAFVDNITNR 229
Cdd:cd03257 137 EVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQAqILDLLKKLQEelglTLLFITHDLGVVAKIADR 215
|
....*....
gi 1525942895 230 TIEVTMGRI 238
Cdd:cd03257 216 VAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-219 |
1.20e-24 |
|
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: 100.97 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKEA--VIAYLPQh 72
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaslSPKELarKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 lltqdkvtvfeetmkAFEEVtqmqkeldelneqltirtdyetddymklieRVSELSEKFYsieetnydaevekvlkglgf 152
Cdd:cd03214 81 ---------------ALELL------------------------------GLAHLADRPF-------------------- 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 153 erkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHD 219
Cdd:cd03214 96 ---------NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
330-518 |
1.20e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 100.01 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnaKIgyfaqnqaalldenltvf 409
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG-------EI------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 410 eTIDQIPLTDGSIKIKDLLGAFMFSgddttkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKD 489
Cdd:cd00267 57 -LIDGKDIAKLPLEELRRRIGYVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|..
gi 1525942895 490 F---DGTLILVSHDRDFLDGLVQKVFEFGNKR 518
Cdd:cd00267 126 LaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
3.86e-24 |
|
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: 101.42 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFG----GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltQ 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT----------------F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DKVTVFEETMKAFEEVTQM--QKELDELNEQLTIRtdyetddymklieRVseLSEKFYSIEETNYDAEVEKVLKGLGFER 154
Cdd:COG1124 65 DGRPVTRRRRKAFRRRVQMvfQDPYASLHPRHTVD-------------RI--LAEPLRIHGLPDREERIAELLEQVGLPP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 KDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQ--WLEdfLINSAKA-----VMVISHDRAFVDNIT 227
Cdd:COG1124 130 SFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDV-SVQaeILN--LLKDLREergltYLFVSHDLAVVAHLC 206
|
250
....*....|.
gi 1525942895 228 NRTIEVTMGRI 238
Cdd:COG1124 207 DRVAVMQNGRI 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-226 |
1.02e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 104.82 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHL--LTQDKv 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRdaLDPNK- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TVFEEtmkafeeVTqmqkeldelneqltirtdyETDDYMKLIERvselsekfysieETNYDAEVEKvlkgLGFERKDFTR 159
Cdd:PRK11819 404 TVWEE-------IS-------------------GGLDIIKVGNR------------EIPSRAYVGR----FNFKGGDQQK 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNI 226
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-231 |
1.40e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 98.69 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTT--LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---------TGPKEA--VIAYLP 70
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltkLSLKELrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 QH----LLTqdkVTVFEETMKAFEevtqmqkeldelNEQLtirtdyetddymkliervselsekfySIEETnyDAEVEKV 146
Cdd:cd03225 82 QNpddqFFG---PTVEEEVAFGLE------------NLGL--------------------------PEEEI--EERVEEA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 147 LKGLGFERKDfTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISHDRAFV 223
Cdd:cd03225 119 LELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELlkkLKAEGKTIIIVTHDLDLL 197
|
....*...
gi 1525942895 224 DNITNRTI 231
Cdd:cd03225 198 LELADRVI 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-301 |
1.59e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 104.48 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLtqdkvt 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQL------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 vfeETMKAFEEVTQMQKEL--DELNEQLTirtdyetdDYmkliervselsekfysieetnydaevekvLKGLGFERKDFT 158
Cdd:PRK10636 386 ---EFLRADESPLQHLARLapQELEQKLR--------DY-----------------------------LGGFGFQGDKVT 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 159 RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:PRK10636 426 EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 239 YDYKAKYSHYLQLRADRRIHQLKAYEEQQRFIADN-QEFIDRFRGTYSKTLQVQSRVKMLEKLE 301
Cdd:PRK10636 506 EPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSaQARKDQKRREAELRTQTQPLRKEIARLE 569
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
330-519 |
4.00e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 97.60 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------NEIDFEGGLKVGHNAKIGYFAQNQAALL 402
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkptsGSIRVFGKPLEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 403 DENLTVFETI----------DQIPLTDGSIKIKDLL---GAFMFSgddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILD 469
Cdd:cd03235 82 DFPISVRDVVlmglyghkglFRRLSKADKAKVDEALervGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 470 EPTNHLDMKTKDIIKDALKDF--DG-TLILVSHDRDFLDGLVQKVFEFgNKRV 519
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-513 |
8.73e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 102.19 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 30 IALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEaviaylpqhlltqdkvtvFEETMKAFEEvTQMQKELDELNEQlTIR 109
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS------------------WDEVLKRFRG-TELQNYFKKLYNG-EIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 110 TDYETDdYMKLIER-----VSELsekfysIEETNYDAEVEKVLKGLGFErKDFTRQTSEFSGGWRMRIELAKILLKKPDL 184
Cdd:PRK13409 162 VVHKPQ-YVDLIPKvfkgkVREL------LKKVDERGKLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 185 ILLDEPTNHMDI-------ESIQWL-EDflinsaKAVMVISHDRAFVDNITNrTIEVtmgrIYDYKAKYSHYLQLRADRR 256
Cdd:PRK13409 234 YFFDEPTSYLDIrqrlnvaRLIRELaEG------KYVLVVEHDLAVLDYLAD-NVHI----AYGEPGAYGVVSKPKGVRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 257 -IHQ-LKAY--EEQQRFiadnqefidrfrgtysktlqvqsRvkmleklevieiDEvdtsALRLKFPPSPRSGQYPVMVE- 331
Cdd:PRK13409 303 gINEyLKGYlpEENMRI-----------------------R------------PE----PIEFEERPPRDESERETLVEy 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 332 -ELTKTYGDHVVFQKASmVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAKIGYFAQNQAAllDENLTVFE 410
Cdd:PRK13409 344 pDLTKKLGDFSLEVEGG-EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-EVDPELKISYKPQYIKP--DYDGTVED 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 411 TIDQIPLTDGS----------IKIKDLLgafmfsgddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLD---- 476
Cdd:PRK13409 420 LLRSITDDLGSsyykseiikpLQLERLL----------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqr 489
|
490 500 510
....*....|....*....|....*....|....*....
gi 1525942895 477 MKTKDIIKDALKDFDGTLILVSHDRDFLDGLVQK--VFE 513
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRlmVFE 528
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
330-506 |
1.01e-22 |
|
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: 96.01 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGG----LKVGHNAKIGYFAQNQ 398
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllppsagEVLWNGEpirdAREDYRRRLAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AalLDENLTVFETID----QIPLTDGSIKIKDLLGAFMFSG--DdttKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:COG4133 85 G--LKPELTVRENLRfwaaLYGLRADREAIDEALEAVGLAGlaD---LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1525942895 473 NHLDMKTKDIIKDALKDF---DGTLILVSHDRDFLDG 506
Cdd:COG4133 160 TALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-238 |
2.95e-22 |
|
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: 94.95 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSInENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--------GPKE--AVIAYLPQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKlrRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HLLTQDKVTVFeetmkafeevtqmqkeldelnEQLtirtdyetdDYMKLIERVSelsekfysieETNYDAEVEKVLKGLG 151
Cdd:cd03264 80 EFGVYPNFTVR---------------------EFL---------DYIAWLKGIP----------SKEVKARVDEVLELVN 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 -FERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAVMVISHDRAFVDNITN 228
Cdd:cd03264 120 lGDRAK--KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLseLGEDRIVILSTHIVEDVESLCN 197
|
250
....*....|
gi 1525942895 229 RTIEVTMGRI 238
Cdd:cd03264 198 QVAVLNKGKL 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-231 |
3.58e-22 |
|
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: 94.63 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFG-GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV------TGPKE--AVIAYLPQHLL 74
Cdd:cd03226 2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpIKAKErrKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQdkvtVFEETmkAFEEVTQMQKELDELNEQltirtdyetddymkliervselsekfysieetnydaeVEKVLKGLG-FE 153
Cdd:cd03226 82 YQ----LFTDS--VREELLLGLKELDAGNEQ-------------------------------------AETVLKDLDlYA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 154 RKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISHDRAFVDNITNRT 230
Cdd:cd03226 119 LKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRV 196
|
.
gi 1525942895 231 I 231
Cdd:cd03226 197 L 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-231 |
3.91e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 10 SFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDK--VTVFEE-TM 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLvAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 87 KAFEEVTqmqkeldeLNEQLTIRTDYETDDYMkliERVselsekfysieetnydaevekvlkGL-GFERkdftRQTSEFS 165
Cdd:NF040873 81 GRWARRG--------LWRRLTRDDRAAVDDAL---ERV------------------------GLaDLAG----RQLGELS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 166 GGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA----VMVISHDRAFVDNITNRTI 231
Cdd:NF040873 122 GGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA-LLAEEHArgatVVVVTHDLELVRRADPCVL 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
3.94e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKEAV--IAYL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlSSRQLArrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHLLTQDKVTVfeetmkafeevtqmqKELDElneqltirtdYETDDYMKLIERVSELSEKF--YSIEETNYDAEVEKVL 147
Cdd:PRK11231 82 PQHHLTPEGITV---------------RELVA----------YGRSPWLSLWGRLSAEDNARvnQAMEQTRINHLADRRL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 148 kglgferkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISHD 219
Cdd:PRK11231 137 --------------TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLmreLNTQGKTVVTVLHD 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
338-522 |
4.01e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 100.24 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 338 GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKVGHNAKIGY----------------------F 394
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsYTFPGNWQLAWvnqetpalpqpaleyvidgdreY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 395 AQNQAALLDEN--------LTVFETIDQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVL 466
Cdd:PRK10636 92 RQLEAQLHDANerndghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 467 ILDEPTNHLDMKTKDIIKDALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREH 522
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-513 |
4.21e-22 |
|
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: 99.86 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 30 IALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEaviaylpqhlltqdkvtvFEETMKAFEEvTQMQKELDELNEQlTIR 109
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPS------------------WDEVLKRFRG-TELQDYFKKLANG-EIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 110 TDYETDdYMKLIER-----VSELSEKfysieeTNYDAEVEKVLKGLGFErKDFTRQTSEFSGGWRMRIELAKILLKKPDL 184
Cdd:COG1245 162 VAHKPQ-YVDLIPKvfkgtVRELLEK------VDERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 185 ILLDEPTNHMDI-------ESIQwlEdfLINSAKAVMVISHDRAFVDNITNrTIEVtmgrIYDYKAKYSHYLQLRADRR- 256
Cdd:COG1245 234 YFFDEPSSYLDIyqrlnvaRLIR--E--LAEEGKYVLVVEHDLAILDYLAD-YVHI----LYGEPGVYGVVSKPKSVRVg 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 257 IHQ-LKAY--EEQQRFIADNQEFidrfrgtysktlqvqsrvkmleklEVIEIDEVDTSALRLKFPpsprsgqypvmveEL 333
Cdd:COG1245 305 INQyLDGYlpEENVRIRDEPIEF------------------------EVHAPRREKEEETLVEYP-------------DL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 334 TKTYGDHVVFQKASMvIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAKIGYFAQNQAAllDENLTVFETID 413
Cdd:COG1245 348 TKSYGGFSLEVEGGE-IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-EVDEDLKISYKPQYISP--DYDGTVEEFLR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 414 QI--PLTDGSI---------KIKDLLgafmfsgddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLD----MK 478
Cdd:COG1245 424 SAntDDFGSSYykteiikplGLEKLL----------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLA 493
|
490 500 510
....*....|....*....|....*....|....*..
gi 1525942895 479 TKDIIKDALKDFDGTLILVSHDRDFLDGLVQK--VFE 513
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDIYLIDYISDRlmVFE 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
330-499 |
6.40e-22 |
|
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: 92.83 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD--HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnaKIgyfaqnqaalldenlt 407
Cdd:cd03228 3 FKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG-------EI---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 vfeTIDQIPLTDgsIKIKDLLG--------AFMFSGDdttkkVK--VLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDM 477
Cdd:cd03228 60 ---LIDGVDLRD--LDLESLRKniayvpqdPFLFSGT-----IRenILSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180
....*....|....*....|....
gi 1525942895 478 KTKDIIKDALKDFDG--TLILVSH 499
Cdd:cd03228 130 ETEALILEALRALAKgkTVIVIAH 153
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-240 |
1.35e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAyLPQHLLTQDKVT 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA-LSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEevtqmqkeldelneqLTIRTDYEtddymklIERVSELSeKFYSIEETNyDAEVEKVLKGLG---FERKDF 157
Cdd:PRK09536 82 VPQDTSLSFE---------------FDVRQVVE-------MGRTPHRS-RFDTWTETD-RAAVERAMERTGvaqFADRPV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 158 TrqtsEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI-ESIQWLEDF--LINSAKAVMVISHDRAFVDNITNRTIEVT 234
Cdd:PRK09536 138 T----SLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
....*.
gi 1525942895 235 MGRIYD 240
Cdd:PRK09536 214 DGRVRA 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
1.40e-21 |
|
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: 93.05 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqhlltqdKVTV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG---------------------EITF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEETM-KAFEEVTQMQKELD--ELNEQLTIRTDYETDDYMKLIErvselsekfysieetnyDAEVEKVLK--GLGFERKd 156
Cdd:cd03268 60 DGKSYqKNIEALRRIGALIEapGFYPNLTARENLRLLARLLGIR-----------------KKRIDEVLDvvGLKDSAK- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 157 ftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLIN---SAKAVMVISH 218
Cdd:cd03268 122 --KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSlrdQGITVLISSH 184
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
328-499 |
9.56e-21 |
|
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: 90.35 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGL------KVGHNAKIgyfAQNQAAL 401
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEitfdgkSYQKNIEA---LRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 402 LD-----------ENLTVFETIDQIPltdgSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDE 470
Cdd:cd03268 78 IEapgfypnltarENLRLLARLLGIR----KKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 471 PTNHLD----MKTKDIIKDaLKDFDGTLILVSH 499
Cdd:cd03268 153 PTNGLDpdgiKELRELILS-LRDQGITVLISSH 184
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-238 |
1.04e-20 |
|
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: 90.85 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--G--PKEAVIAYLPQH--LL 74
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdGkdITKKNLRELRRKvgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQD------KVTVFEETmkAF---------EEVtqmqkeldelneqltirtdyetddymkliervselsekfysieetny 139
Cdd:COG1122 81 FQNpddqlfAPTVEEDV--AFgpenlglprEEI----------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 140 DAEVEKVLKGLGFE-RKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMV 215
Cdd:COG1122 112 RERVEEALELVGLEhLAD--RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVII 189
|
250 260
....*....|....*....|...
gi 1525942895 216 ISHDRAFVDNITNRTIEVTMGRI 238
Cdd:COG1122 190 VTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
330-518 |
2.40e-20 |
|
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: 89.45 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDH--VVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGGLKVGHNA-----KIGYFA 395
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGllgptsgEVLVDGKDLTKLSLkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 396 QNQAA-LLdeNLTVFETI------DQIPLTDGSIKIKDLLGAFmfsGDDTTKKVKV--LSGGEKTRLAMIKLL-LEPvNV 465
Cdd:cd03225 82 QNPDDqFF--GPTVEEEVafglenLGLPEEEIEERVEEALELV---GLEGLRDRSPftLSGGQKQRVAIAGVLaMDP-DI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 466 LILDEPTNHLDMKTKDIIKDALKDF--DG-TLILVSHDRDFLDGLVQKVFEFGNKR 518
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-504 |
2.48e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.10 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKII--ADVAKPTTGNVTgpkeAVIAYLPQHLLTQDKV 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRII----YHVALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TVFEETMKAFEEVTQMQKELDELNEQLTIRTD-------------YETDdymKLIERVSE-LSEKFYSIEETNYDAEveK 145
Cdd:TIGR03269 77 KVGEPCPVCGGTLEPEEVDFWNLSDKLRRRIRkriaimlqrtfalYGDD---TVLDNVLEaLEEIGYEGKEAVGRAV--D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 146 VLKGLGFERKdFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKA---VMVI-SHDRA 221
Cdd:TIGR03269 152 LIEMVQLSHR-ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgiSMVLtSHWPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 222 FVDNITNRTIEVTMGRIYDykakyshylqlradrrihqlkayeeqqrfIADNQEFIDRFRGTysktlqvqsrVKMLEKLE 301
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKE-----------------------------EGTPDEVVAVFMEG----------VSEVEKEC 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 302 VIEIDEvdtsalrlkfppsprsgqyPVM-VEELTKTY-----GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN 375
Cdd:TIGR03269 272 EVEVGE-------------------PIIkVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 376 EIDFEGG---LKVGHN----AKIGYFAQNQA----ALLDENLTVFETIDQIP-LTDG-SIKIKDLLG------AFMFSGD 436
Cdd:TIGR03269 333 VLEPTSGevnVRVGDEwvdmTKPGPDGRGRAkryiGILHQEYDLYPHRTVLDnLTEAiGLELPDELArmkaviTLKMVGF 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 437 DTTKKVKVL-------SGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHDRDFL 504
Cdd:TIGR03269 413 DEEKAEEILdkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEMEQTFIIVSHDMDFV 491
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-244 |
2.67e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.73 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAVIAYLPQH 72
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqvlvngqDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 L--------LTQDKvTVFEetmkafeevtqmqkeldelNeqltirtdyetddyMKLIERVSELSEKfysieetNYDAEVE 144
Cdd:COG2884 81 IgvvfqdfrLLPDR-TVYE-------------------N--------------VALPLRVTGKSRK-------EIRRRVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 145 KVLKGLGFERKDFTRqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDflINSA-KAVMVISHD 219
Cdd:COG2884 120 EVLDLVGLSDKAKAL-PHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETsweiMELLEE--INRRgTTVLIATHD 196
|
250 260
....*....|....*....|....*
gi 1525942895 220 RAFVDNITNRTIEVTMGRIYDYKAK 244
Cdd:COG2884 197 LELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-238 |
5.65e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 89.86 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 15 TLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhLLTQDKVTVFEETMKAFEEVTQ 94
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS-------------FRGQDLYQLDRKQRRAFRRDVQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 95 M--QKELDELNEQLTIRtdyetddymkliERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMRI 172
Cdd:TIGR02769 92 LvfQDSPSAVNPRMTVR------------QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 173 ELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-238 |
6.14e-20 |
|
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: 88.42 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---------TGPKE--AVIAYLPQHlltqdkVTVFEETMK 87
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqLDPADlrRNIGYVPQD------VTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 88 afeevtqmqkeldelnEQLTIRTDYETDdymKLIERVSELSekfysieetnydaevekvlkGLG-FERKD---FTRQTSE 163
Cdd:cd03245 96 ----------------DNITLGAPLADD---ERILRAAELA--------------------GVTdFVNKHpngLDLQIGE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 164 ----FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES--------IQWLEDflinsaKAVMVISHDRAFVDnITNRTI 231
Cdd:cd03245 137 rgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSeerlkerlRQLLGD------KTLIIITHRPSLLD-LVDRII 209
|
....*..
gi 1525942895 232 EVTMGRI 238
Cdd:cd03245 210 VMDSGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-238 |
6.80e-20 |
|
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: 88.65 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAVIAYLP-----Q 71
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgeDITGLPPHEIARLGigrtfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HLLTQDKVTVFEETMKAFeevtqmqkeldELNEQLTIRTDYETDDYMKLIERVSELSEKFysieetnydaevekvlkGLG 151
Cdd:cd03219 83 IPRLFPELTVLENVMVAA-----------QARTGSGLLLARARREEREARERAEELLERV-----------------GLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 fERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAK-AVMVISHDRAFVDNITN 228
Cdd:cd03219 135 -DLAD--RPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIreLRERGiTVLLVEHDMDVVMSLAD 211
|
250
....*....|
gi 1525942895 229 RTIEVTMGRI 238
Cdd:cd03219 212 RVTVLDQGRV 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
330-500 |
1.03e-19 |
|
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: 87.95 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKA----SMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGGLKVGHNAK-------- 390
Cdd:cd03257 4 VKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgSIIFDGKDLLKLSRRlrkirrke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 391 IGYFAQNQAALLDENLTVFETID------QIPLTDGSIKIKDLLGAFMFSGDDT--TKKVKVLSGGEKTRLA-MIKLLLE 461
Cdd:cd03257 84 IQMVFQDPMSSLNPRMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAiARALALN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 462 PVnVLILDEPTNHLDMKTKDIIKDALKD----FDGTLILVSHD 500
Cdd:cd03257 164 PK-LLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHD 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-238 |
1.19e-19 |
|
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: 91.89 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhLLT 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL-------------FDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 76 QDKVTVFEETMKAFEEVTQM--QKELDELNEQLTIRTdyetddymkliervsELSE-----KFYSIEETnyDAEVEKVLK 148
Cdd:COG1123 327 KDLTKLSRRSLRELRRRVQMvfQDPYSSLNPRMTVGD---------------IIAEplrlhGLLSRAER--RERVAELLE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQW-----LEDFLINSAKAVMVISHDRAFV 223
Cdd:COG1123 390 RVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDLAVV 468
|
250
....*....|....*
gi 1525942895 224 DNITNRTIEVTMGRI 238
Cdd:COG1123 469 RYIADRVAVMYDGRI 483
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
330-500 |
1.80e-19 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 88.18 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEG----GLKVGHNAK-IGYFAQN 397
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllkpssgEVLLDGrdlaSLSRRELARrIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAAllDENLTVFETIdqipltdgsikikdLLGAF----MFSGDDTTKKVKV-------------------LSGGEKTR-- 452
Cdd:COG1120 84 PPA--PFGLTVRELV--------------ALGRYphlgLFGRPSAEDREAVeealertglehladrpvdeLSGGERQRvl 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 453 LAMIkLLLEPvNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:COG1120 148 IARA-LAQEP-PLLLLDEPTSHLDLAHQlevlELLRRLARERGRTVVMVLHD 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
330-511 |
2.03e-19 |
|
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: 85.70 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM--------------NEIDFEGGLKVGHNAKIGYFA 395
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAgleepdsgsilidgEDLTDLEDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 396 QnQAALLdENLTVFETIdqipltdgsikikdLLGafmfsgddttkkvkvLSGGEKTRLAMIK-LLLEPvNVLILDEPTNH 474
Cdd:cd03229 83 Q-DFALF-PHLTVLENI--------------ALG---------------LSGGQQQRVALARaLAMDP-DVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525942895 475 LDMKTKDIIKDALKDF---DG-TLILVSHDRDFLDGLVQKV 511
Cdd:cd03229 131 LDPITRREVRALLKSLqaqLGiTVVLVTHDLDEAARLADRV 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
328-511 |
2.24e-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: 87.04 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKV--GHNA---------KIGYFAQ 396
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAalLD------ENLTVFETIDQIPLTDGSIKIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDE 470
Cdd:cd03265 81 DLS--VDdeltgwENLYIHARLYGVPGAERRERIDELL-DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1525942895 471 PTNHLDMKTK----DIIKDALKDFDGTLILVSHDRDFLDGLVQKV 511
Cdd:cd03265 158 PTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-238 |
4.39e-19 |
|
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: 85.92 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNniSVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAVIAYLPQHL 73
Cdd:cd03292 3 FINVT--KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 LT--QD-----KVTVFEETMKAFEEVTQMQKELDElneqltirtdyetddymklieRVSELSEkfysieetnydaevekv 146
Cdd:cd03292 81 GVvfQDfrllpDRNVYENVAFALEVTGVPPREIRK---------------------RVPAALE----------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 147 LKGLGFERKDFTrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAVMVIS-HDRAFV 223
Cdd:cd03292 123 LVGLSHKHRALP---AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkINKAGTTVVVAtHAKELV 199
|
250
....*....|....*
gi 1525942895 224 DNITNRTIEVTMGRI 238
Cdd:cd03292 200 DTTRHRVIALERGKL 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-238 |
7.27e-19 |
|
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: 85.23 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGG----TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqhlltqd 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSG--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 78 KVTVFEETMKAFEEvtqmqKELDEL-NEQL-TIRTDYETDDYMKLIERVsELSEKFYSIEETNYDAEVEKVLKGLGFERK 155
Cdd:cd03255 60 EVRVDGTDISKLSE-----KELAAFrRRHIgFVFQSFNLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGLGDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 156 dFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINSAKAVMVISHDRAFVDnITNRTI 231
Cdd:cd03255 134 -LNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAE-YADRII 211
|
....*..
gi 1525942895 232 EVTMGRI 238
Cdd:cd03255 212 ELRDGKI 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-238 |
8.90e-19 |
|
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: 89.44 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF--GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--G------PKEAV---IAY 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlgGvdlrdlDEDDLrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHlltqdkVTVFEETMkafeevtqmqkeLDEL---NEQLTirtdyetddymkliervselsekfysieetnyDAEVEK 145
Cdd:COG4987 414 VPQR------PHLFDTTL------------RENLrlaRPDAT--------------------------------DEELWA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 146 VLK--GLGferkDFTRQTSE------------FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQ-WLEDFLINSA 210
Cdd:COG4987 444 ALErvGLG----DWLAALPDgldtwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEALA 519
|
250 260
....*....|....*....|....*....
gi 1525942895 211 -KAVMVISHDRAFVDNItNRTIEVTMGRI 238
Cdd:COG4987 520 gRTVLLITHRLAGLERM-DRILVLEDGRI 547
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
297-522 |
1.01e-18 |
|
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: 89.89 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 297 LEKLEVIEIDEVDTSALRLKFPPSPRSGQypVMVEELTKTYGDHV--VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM 374
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 375 N-EIDFEGGLKV-GHNAK----------IGYFAQNqAALLD----ENLTVFE---TIDQIpltdgsIKIKDLLGAFMF-- 433
Cdd:COG2274 523 GlYEPTSGRILIdGIDLRqidpaslrrqIGVVLQD-VFLFSgtirENITLGDpdaTDEEI------IEAARLAGLHDFie 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 434 ---SGDDTtkKV----KVLSGGEKTRLAMIK-LLLEPvNVLILDEPTNHLDMKTKDIIKDALKDFDG--TLILVSHDRDF 503
Cdd:COG2274 596 alpMGYDT--VVgeggSNLSGGQRQRLAIARaLLRNP-RILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLST 672
|
250
....*....|....*....
gi 1525942895 504 LDgLVQKVFEFGNKRVREH 522
Cdd:COG2274 673 IR-LADRIIVLDKGRIVED 690
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
330-500 |
1.05e-18 |
|
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: 84.02 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnakigyfaqnqaalldenlTVf 409
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG------------------------EI- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 410 eTIDQIPLTDGSIKIK-----------DLLGAFMFSGddttKKVKVLSGGEKTR--LAMIkLLLEPvNVLILDEPTNHLD 476
Cdd:cd03214 57 -LLDGKDLASLSPKELarkiayvpqalELLGLAHLAD----RPFNELSGGERQRvlLARA-LAQEP-PILLLDEPTSHLD 129
|
170 180
....*....|....*....|....*...
gi 1525942895 477 MKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:cd03214 130 IAHQiellELLRRLARERGKTVVMVLHD 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
347-473 |
1.42e-18 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 82.70 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIM-NEIDFEGGLKVGHNA-----------KIGYFAQNqaALLDENLTVFETIDQ 414
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAgLLSPTEGTILLDGQDltdderkslrkEIGYVFQD--PQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 415 IPLTDG------SIKIKDLLGAFMFSGDDTTK---KVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTN 473
Cdd:pfam00005 83 GLLLKGlskrekDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-219 |
2.55e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQ--HLLTQDK 78
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 VTVfeetmKAFeevtqmqkeldelneqLTIRTDYETDDYMKLIERVSelsekfysiEETNYDAEVEKVlkglgferkdft 158
Cdd:PRK09544 84 LTV-----NRF----------------LRLRPGTKKEDILPALKRVQ---------AGHLIDAPMQKL------------ 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 159 rqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAK-----AVMVISHD 219
Cdd:PRK09544 122 ------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD-LIDQLRreldcAVLMVSHD 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
305-521 |
2.65e-18 |
|
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: 88.28 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 305 IDEVDTSALRLKFP--PSPRSGQYPVMVEELTKTY--GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFE 380
Cdd:COG4987 309 LNELLDAPPAVTEPaePAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 381 GGlKV---GHN----------AKIGYFAQnQAALLD----ENLTVF-------------------ETIDQIPltDGsiki 424
Cdd:COG4987 389 SG-SItlgGVDlrdldeddlrRRIAVVPQ-RPHLFDttlrENLRLArpdatdeelwaalervglgDWLAALP--DG---- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 425 kdlLGAFMFSGDDTtkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSHDRD 502
Cdd:COG4987 461 ---LDTWLGEGGRR------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLA 531
|
250
....*....|....*....
gi 1525942895 503 FLDgLVQKVFEFGNKRVRE 521
Cdd:COG4987 532 GLE-RMDRILVLEDGRIVE 549
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-238 |
3.58e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 87.51 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-GPKE----------AVIAYL 69
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILiNGVDlsdldpaswrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHlltqdkVTVFEETMKAfeevtqmqkeldelNeqltIRtdyetddymkliervselsekFYSIEETnyDAEVEKVLKG 149
Cdd:COG4988 417 PQN------PYLFAGTIRE--------------N----LR---------------------LGRPDAS--DEELEAALEA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LGFErkDFTRQTSE------------FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK--AVMV 215
Cdd:COG4988 450 AGLD--EFVAALPDgldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVIL 527
|
250 260
....*....|....*....|...
gi 1525942895 216 ISHDRAFVDNItNRTIEVTMGRI 238
Cdd:COG4988 528 ITHRLALLAQA-DRILVLDDGRI 549
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
330-525 |
3.73e-18 |
|
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: 83.54 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTY-GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaIMN--------EIDFeGGLKVGHNA------KIGY- 393
Cdd:COG1122 3 LENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLR-LLNgllkptsgEVLV-DGKDITKKNlrelrrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 394 --FAQNQaaLLDEnlTVFETIdqipltdgsikikdllgAFM-----FSGDDTTKKVK-----------------VLSGGE 449
Cdd:COG1122 81 fqNPDDQ--LFAP--TVEEDV-----------------AFGpenlgLPREEIRERVEealelvglehladrpphELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 450 KTRLAMIKLL-LEPvNVLILDEPTNHLDMKTKDIIKDALKDFDG---TLILVSHDRDFLDGLVQKVFEFGNKRV------ 519
Cdd:COG1122 140 KQRVAIAGVLaMEP-EVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIvadgtp 218
|
....*.
gi 1525942895 520 REHFED 525
Cdd:COG1122 219 REVFSD 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-238 |
4.78e-18 |
|
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: 87.58 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT--LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKE--AVIAY 68
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHlltqdkVTVFEETMKafeevtqmqkeldelnEQLTIrTDYETDDymkliervselsekfysieetnydAEVEKVLK 148
Cdd:COG2274 554 VLQD------VFLFSGTIR----------------ENITL-GDPDATD------------------------EEIIEAAR 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GLGFErkDFTR------QT------SEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINsaKA 212
Cdd:COG2274 587 LAGLH--DFIEalpmgyDTvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLKG--RT 662
|
250 260
....*....|....*....|....*.
gi 1525942895 213 VMVISHDRAFVDNiTNRTIEVTMGRI 238
Cdd:COG2274 663 VIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
6.42e-18 |
|
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: 83.21 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIAdvakpttgnvtgpkeaviAYLPQhlLTQDKVT 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT------------------GDLPP--TYGNDVR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAfEEVTQMQKEL----DELneQLTIRTDyetddymkliERVSE--LSEKFYSIE-ETNYDAE----VEKVLKG 149
Cdd:COG1119 63 LFGERRGG-EDVWELRKRIglvsPAL--QLRFPRD----------ETVLDvvLSGFFDSIGlYREPTDEqrerARELLEL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 150 LGFE-RKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINSAKAVMVISH 218
Cdd:COG1119 130 LGLAhLAD--RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-221 |
7.37e-18 |
|
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: 86.57 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT-LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV-------TGPKEAV----IAYL 69
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvplADADADSwrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHlltqdkVTVFEETMKafeevtqmqkeldelnEQLTIRTDYETDDymkLIERVSELSekfysieetnYDAEVEKVLkG 149
Cdd:TIGR02857 402 PQH------PFLFAGTIA----------------ENIRLARPDASDA---EIREALERA----------GLDEFVAAL-P 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 150 LGFERKdFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAVMVISHDRA 221
Cdd:TIGR02857 446 QGLDTP-IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALraLAQGRTVLLVTHRLA 518
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-230 |
7.96e-18 |
|
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: 82.55 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV--------TGPKEA--VIAYLPQHlltqdkvtvfeetmka 88
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirTDRKAArqSLGYCPQF---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 89 feevtqmqkelDELNEQLTIRtdyetdDYMKLIERvselsekFYSIEETNYDAEVEKVLKGLGFERKDfTRQTSEFSGGW 168
Cdd:cd03263 84 -----------DALFDELTVR------EHLRFYAR-------LKGLPKSEIKEEVELLLRVLGLTDKA-NKRARTLSGGM 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 169 RMRIELAKILLKKPDLILLDEPTNHMDIES--IQWleDFL--INSAKAVMVISHDRAFVDNITNRT 230
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAIW--DLIleVRKGRSIILTTHSMDEAEALCDRI 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-502 |
1.18e-17 |
|
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: 81.80 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEG----GLKVgHNAKIGYFAQNq 398
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlerpdsgEILIDGrdvtGVPP-ERRNIGMVFQD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AALLDeNLTVFETIdQIPLTDGS-----IKIKDLLGAFMFS-GDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:cd03259 81 YALFP-HLTVAENI-AFGLKLRGvpkaeIRARVRELLELVGlEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 473 NHLDMKTK----DIIKDALKDFDGTLILVSHDRD 502
Cdd:cd03259 159 SALDAKLReelrEELKELQRELGITTIYVTHDQE 192
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-240 |
1.31e-17 |
|
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: 82.23 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFG-GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltqdkvt 80
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 vFEETmkafeEVTQMQ-KELDELNEQL-TIRTDYetddymKLIERVS--------ELSEK--FYSIEETNYDAEVEKVLK 148
Cdd:cd03256 60 -IDGT-----DINKLKgKALRQLRRQIgMIFQQF------NLIERLSvlenvlsgRLGRRstWRSLFGLFPKEEKQRALA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GL---GFERKDFTRqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD-IESIQWLEDFL-INSAKAVMVIS--HDRA 221
Cdd:cd03256 128 ALervGLLDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpASSRQVMDLLKrINREEGITVIVslHQVD 206
|
250 260
....*....|....*....|
gi 1525942895 222 FVDNITNRTIEVTMGRI-YD 240
Cdd:cd03256 207 LAREYADRIVGLKDGRIvFD 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-237 |
1.75e-17 |
|
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: 80.31 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhLLTQDkVTV 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-------------IDGED-LTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEETMKAFEEVTQMQKELDELNEQLTIRtdyetddymkliervselsekfysieetnydaevEKVLKGLgferkdftrqt 161
Cdd:cd03229 67 LEDELPPLRRRIGMVFQDFALFPHLTVL----------------------------------ENIALGL----------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 162 sefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI----NSAKAVMVISHDRAFVDNITNRTIEVTMGR 237
Cdd:cd03229 102 ---SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
319-500 |
2.14e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 85.19 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 319 PSPRSGQYPVMVEELTKTYGD-HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVGHN-------- 388
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpYSGSILINGVdlsdldpa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 389 ---AKIGYFAQN------------------------QAALLDENLTVFetIDQIP------LTDGSikikdllgafmfSG 435
Cdd:COG4988 408 swrRQIAWVPQNpylfagtirenlrlgrpdasdeelEAALEAAGLDEF--VAALPdgldtpLGEGG------------RG 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 436 ddttkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSHD 500
Cdd:COG4988 474 ---------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-221 |
2.57e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 79.73 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT--LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltqdkv 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tvfeetmkafeevtqmqkeLDELNeqltIRtDYETDDYMKLIERVSELSEKFY-SIEEtNydaevekVLkglgferkdft 158
Cdd:cd03228 61 -------------------IDGVD----LR-DLDLESLRKNIAYVPQDPFLFSgTIRE-N-------IL----------- 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 159 rqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINsaKAVMVISHDRA 221
Cdd:cd03228 98 ------SGGQRQRIAIARALLRDPPILILDEATSALDPETealiLEALRALAKG--KTVIVIAHRLS 156
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-238 |
2.65e-17 |
|
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: 80.87 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkEAVIAYLPQHLLTQ 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT---VDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DKVTVFEETMKafeevtqmqkeldeLNEQLTIRtdyetddymkliERVsELSEKFYSIEETNYDAEVEKVLKGLGFErkD 156
Cdd:cd03266 78 RRLGFVSDSTG--------------LYDRLTAR------------ENL-EYFAGLYGLKGDELTARLEELADRLGME--E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 157 F-TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISHDRAFVDNITNRTIE 232
Cdd:cd03266 129 LlDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFirqLRALGKCILFSTHIMQEVERLCDRVVV 208
|
....*.
gi 1525942895 233 VTMGRI 238
Cdd:cd03266 209 LHRGRV 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-219 |
4.13e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.21 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGG----TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV-------TGPKEAvIAYLP 70
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvTGPGPD-RGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 QhlltQDKV----TVFEETMKAFeEVTQMQKEldelneqltirtdyetddymKLIERVSELSEKFysieetnydaevekv 146
Cdd:cd03293 80 Q----QDALlpwlTVLDNVALGL-ELQGVPKA--------------------EARERAEELLELV--------------- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 147 lkGL-GFERKdftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI---ESIQ-WLEDFLINSAKAVMVISHD 219
Cdd:cd03293 120 --GLsGFENA----YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLQeELLDIWRETGKTVLLVTHD 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-498 |
4.52e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.69 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGG-LKVGHNAKIGYfaqnqaaL 401
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilapdsgEVLWDGEpLDPEDRRRIGY-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 402 LDE-----NLTVfetIDQI---------PLTDGSIKIKDLLGAFMFsGDDTTKKVKVLSGGEKTRLAMIKLLL-EPvNVL 466
Cdd:COG4152 77 PEErglypKMKV---GEQLvylarlkglSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLhDP-ELL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 467 ILDEPTNHLDMKTKDIIKDALKDF--DGTLILVS 498
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFS 185
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
330-519 |
7.03e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 79.85 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKV---GHN-------------AKIGY 393
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSG-EVlidGEDisglseaelyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 394 FAQnQAALLDeNLTVFETIdQIPL------TDGSI--KIKDLLGAFMFSGDDtTKKVKVLSGGEKTRLAMIK-LLLEPVn 464
Cdd:cd03261 82 LFQ-SGALFD-SLTVFENV-AFPLrehtrlSEEEIreIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARaLALDPE- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 465 VLILDEPTNHLDMKTKDIIKD---ALKD-FDGTLILVSHDRDFLDGLVQKVFEFGNKRV 519
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDlirSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
330-499 |
9.20e-17 |
|
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: 79.25 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEG-GLKVGHNAKIGYFAQNQAAL 401
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiilpdsgEVLFDGkPLDIAARNRIGYLPEERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 402 LD----ENLTVFETIDQIPLTDGSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDM 477
Cdd:cd03269 83 PKmkviDQLVYLAQLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180
....*....|....*....|....*
gi 1525942895 478 KTKDIIKDA---LKDFDGTLILVSH 499
Cdd:cd03269 162 VNVELLKDVireLARAGKTVILSTH 186
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
328-520 |
9.25e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 79.47 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGD--HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKVGHN----------AKIGYF 394
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtAYINGYsirtdrkaarQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 395 AQNQAalLDENLTVFET------IDQIPLTDGSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLIL 468
Cdd:cd03263 81 PQFDA--LFDELTVREHlrfyarLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 469 DEPTNHLDMKTKDIIKDALKDFDG--TLILVSHDRDFLDGLVQKVFEFGNKRVR 520
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-231 |
1.94e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFsINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpKEAVIAYLPQHLLTQDKVT 80
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKPDYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAfeevtqmqkeldelneqltirtdyeTDDYmkliervselSEKFYSIEetnydaevekVLKGLGFERKdFTRQ 160
Cdd:PRK13409 417 VEDLLRSI-------------------------TDDL----------GSSYYKSE----------IIKPLQLERL-LDKN 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE-------SIQWLEDfliNSAKAVMVISHDRAFVDNITNRTI 231
Cdd:PRK13409 451 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRIAE---EREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-240 |
2.42e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.53 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaVIAYLP-----QHLltqDKVTVFeetmkaFEEVT 93
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPwkrrkKFL---RRIGVV------FGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 94 QMQKELDELNEQLTIRTDYETDD--YMKLIERVSELsekfysieetnydAEVEKVLKglgferkdftRQTSEFSGGWRMR 171
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPParFKKRLDELSEL-------------LDLEELLD----------TPVRQLSLGQRMR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 172 IELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK----AVMVISHDRAFVDNITNRTIEVTMGRI-YD 240
Cdd:cd03267 162 AEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVLVIDKGRLlYD 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-198 |
3.18e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.80 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkEAVIAylpQHLLTQDKVTV 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------RATVA---GHDVVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEETMKAFEEVTqmqkeldeLNEQLTIRtdyetddymkliERVsELSEKFYSIEETNYDAEVEKVLKGLGF-ERKDftRQ 160
Cdd:cd03265 72 RRRIGIVFQDLS--------VDDELTGW------------ENL-YIHARLYGVPGAERRERIDELLDFVGLlEAAD--RL 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES 198
Cdd:cd03265 129 VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
3.85e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.16 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAVIAYLP--- 70
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGrilfdgrDITGLPPHRIARLGiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 --QHlltqdkVTVFEEtMKAFEEV-TQMQKELDELNEQLTIRTDYETDDYMKLIERVSELSEKFysieetnydaevekvl 147
Cdd:COG0411 84 tfQN------PRLFPE-LTVLENVlVAAHARLGRGLLAALLRLPRARREEREARERAEELLERV---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 148 kGLGfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAK--AVMVISHDRAFV 223
Cdd:COG0411 141 -GLA-DRAD--EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIrrLRDERgiTILLIEHDMDLV 216
|
....*.
gi 1525942895 224 DNITNR 229
Cdd:COG0411 217 MGLADR 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-219 |
4.41e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.21 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV------IAYLP 70
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVtgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 QH------LltqdkvTVFEETMKAFEEVTQMQKELDElneqltiRTDyetddymKLIERVselsekfysieetnydaeve 144
Cdd:COG1116 87 QEpallpwL------TVLDNVALGLELRGVPKAERRE-------RAR-------ELLELV-------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 145 kvlkGL-GFERKdFTRQtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI---ESIQ-WLEDFLINSAKAVMVISHD 219
Cdd:COG1116 127 ----GLaGFEDA-YPHQ---LSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERLQdELLRLWQETGKTVLFVTHD 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-231 |
4.60e-16 |
|
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: 77.83 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 23 SINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAViAYLPQHLLTQDKVTVfeetmkafeevtqmQKELDEL 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTV--------------RDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 103 NEQLTIRTDYETDdymkliervselsekfysieetnydaevekVLKGLGFERKdFTRQTSEFSGGWRMRIELAKILLKKP 182
Cdd:cd03237 86 TKDFYTHPYFKTE------------------------------IAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 183 DLILLDEPTNHMDIE----SIQWLEDFLINSAKAVMVISHDRAFVDNITNRTI 231
Cdd:cd03237 135 DIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-511 |
7.15e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.86 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 339 DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHNAK----------IGYFAQNQ---AALLD 403
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvLLDGTDIRqldpadlrrnIGYVPQDVtlfYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 ENLTvfetidqipLTDGSIKIKDLLGAFMFSG-DDTTKKVKV------------LSGGEKTRLAMIKLLLEPVNVLILDE 470
Cdd:cd03245 96 DNIT---------LGAPLADDERILRAAELAGvTDFVNKHPNgldlqigergrgLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 471 PTNHLDMKTKDIIKDALKDF--DGTLILVSHDRDFLDgLVQKV 511
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLD-LVDRI 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-501 |
7.40e-16 |
|
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: 80.41 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 319 PSPRSGQYPVMVEELTKTYGDH-VVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVGHNAKIGYFA- 395
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADADAd 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 396 --QNQAALLDENLTVFE-TI-DQIPLTDGSIKIKDLLGAFMFSGDDTTKKV-------KV------LSGGEKTRLAMIKL 458
Cdd:TIGR02857 393 swRDQIAWVPQHPFLFAgTIaENIRLARPDASDAEIREALERAGLDEFVAAlpqgldtPIgeggagLSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1525942895 459 LLEPVNVLILDEPTNHLDMKTKDIIKDALKDFDG--TLILVSHDR 501
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-231 |
1.21e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 79.83 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFGGTTLFSDVTfSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgPKEAVIAYLPQHlltqdkvtvfeet 85
Cdd:COG1245 346 DLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQY------------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 86 mkafeevtqmqkeldelneqltIRTDYEtddymkliERVSE-LSEKFYSIEETNYdAEVEkVLKGLGFERKdFTRQTSEF 164
Cdd:COG1245 410 ----------------------ISPDYD--------GTVEEfLRSANTDDFGSSY-YKTE-IIKPLGLEKL-LDKNVKDL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 165 SGGWRMRIELAKILLKKPDLILLDEPTNHMDIES-------IQwleDFLINSAKAVMVISHDRAFVDNITNRTI 231
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQrlavakaIR---RFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
330-503 |
1.93e-15 |
|
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: 75.60 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD----HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaIMNEID--FEGGLKV-GH--------------N 388
Cdd:cd03255 3 LKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDrpTSGEVRVdGTdisklsekelaafrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 389 AKIGY-FaqnQAALLDENLTVFE------TIDQIPLTDGSIKIKDLLGAFMFsGDDTTKKVKVLSGGEKTRLAMIKLLLE 461
Cdd:cd03255 82 RHIGFvF---QSFNLLPDLTALEnvelplLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525942895 462 PVNVLILDEPTNHLDMKTKDIIKDAL----KDFDGTLILVSHDRDF 503
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPEL 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
330-522 |
1.98e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 78.79 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTY--GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN----------EIDFEGGLKVGHN-----AKIG 392
Cdd:COG1123 7 VRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphggrisgEVLLDGRDLLELSealrgRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 393 YFAQNQAALLDEnLTVFETI------DQIPLTDGSIKIKDLLGAFmfsGDDTTKKVKV--LSGGEKTR--LAMIkLLLEP 462
Cdd:COG1123 87 MVFQDPMTQLNP-VTVGDQIaealenLGLSRAEARARVLELLEAV---GLERRLDRYPhqLSGGQRQRvaIAMA-LALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 463 VnVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREH 522
Cdd:COG1123 162 D-LLIADEPTTALDVTTQaeilDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
330-527 |
2.17e-15 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 75.79 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKV---GHN-------------AKIGY 393
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG-EIlvdGQDitglsekelyelrRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 394 FAQnQAALLDeNLTVFETIdQIPL---TDGSIKIKD-----------LLGA-FMFSGDdttkkvkvLSGGektrlaMIK- 457
Cdd:COG1127 87 LFQ-GGALFD-SLTVFENV-AFPLrehTDLSEAEIRelvleklelvgLPGAaDKMPSE--------LSGG------MRKr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 458 ------LLLEPvNVLILDEPTNHLDMKTKDIIkDAL-----KDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREH--FE 524
Cdd:COG1127 150 valaraLALDP-EILLYDEPTAGLDPITSAVI-DELirelrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEgtPE 227
|
...
gi 1525942895 525 DIK 527
Cdd:COG1127 228 ELL 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-190 |
2.26e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.49 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV----------TGPKEAVIAYLPQ 71
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftnLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 ------HLltqdkvTVFEETmkAFeevtqmqkeldelneQLTIRTDYETDdymklI-ERVSELsekfysieetnydaeVE 144
Cdd:COG1118 83 hyalfpHM------TVAENI--AF---------------GLRVRPPSKAE-----IrARVEEL---------------LE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 145 KV-LKGLGferkdfTRQTSEFSGGWRMRIELAKILLKKPDLILLDEP 190
Cdd:COG1118 120 LVqLEGLA------DRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-238 |
2.28e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 15 TLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviAYLPQHLLTQDKvtvfeETMKAFEEVTQ 94
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV--------SWRGEPLAKLNR-----AQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 95 M--QKELDELNEQLTIRtdyetddymkliERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMRI 172
Cdd:PRK10419 93 MvfQDSISAVNPRKTVR------------EIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 173 ELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-238 |
2.49e-15 |
|
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: 74.86 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTG--PKEAVIAYLPQ--- 71
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeilidgrDVTGvpPERRNIGMVFQdya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 ---HLltqdkvTVFEETmkAFeevtqmqkeldelneQLTIRTdyetddymkliervselsekfysIEETNYDAEVEKVLK 148
Cdd:cd03259 83 lfpHL------TVAENI--AF---------------GLKLRG-----------------------VPKAEIRARVRELLE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GLGFERkDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL---INSAKAVMV-ISHDRAFVD 224
Cdd:cd03259 117 LVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELkelQRELGITTIyVTHDQEEAL 195
|
250
....*....|....
gi 1525942895 225 NITNRTIEVTMGRI 238
Cdd:cd03259 196 ALADRIAVMNEGRI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-195 |
3.11e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 75.45 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKEAVIAYLPQH 72
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQDKVTVFEETmkAFeevtqmqkeldelneQLTIRTDYETDDYMKLIERVSELsekfysieetnydaeVEKV-LKGLG 151
Cdd:cd03296 83 YALFRHMTVFDNV--AF---------------GLRVKPRSERPPEAEIRAKVHEL---------------LKLVqLDWLA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1525942895 152 ferkdfTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:cd03296 131 ------DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
330-499 |
3.28e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 73.23 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAKIGYFAQNQAALldeNLTVf 409
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG-EILVDGKEVSFASPRDAR---RAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 410 ETIDQipltdgsikikdllgafmfsgddttkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD----IIKD 485
Cdd:cd03216 78 AMVYQ------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVErlfkVIRR 127
|
170
....*....|....
gi 1525942895 486 aLKDFDGTLILVSH 499
Cdd:cd03216 128 -LRAQGVAVIFISH 140
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-219 |
3.55e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--G-------PKE--AVIAYL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlnGrpladwsPAElaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHlltqdkVTVfeetmkAF----EEVTQM--------QKELDELneqltirtdyeTDDYMKLIErVSELSEKFYsieet 137
Cdd:PRK13548 82 PQH------SSL------SFpftvEEVVAMgraphglsRAEDDAL-----------VAAALAQVD-LAHLAGRDY----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 138 nydaevekvlkglgferkdftrqtSEFSGGWRMRIELAKILL------KKPDLILLDEPTNHMDI----ESIQWLEDFLI 207
Cdd:PRK13548 133 ------------------------PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAH 188
|
250
....*....|..
gi 1525942895 208 NSAKAVMVISHD 219
Cdd:PRK13548 189 ERGLAVIVVLHD 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-240 |
4.52e-15 |
|
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: 77.92 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 7 ISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaylpqhlltqdKVTVFEE-- 84
Cdd:TIGR03269 290 ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-------------------NVRVGDEwv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 85 --TMKAFEEVTQMQKELDELNEQLTIRTDYETDDymKLIERVS-ELSEKFYSIEETNydaevekVLKGLGFERKD----F 157
Cdd:TIGR03269 351 dmTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLD--NLTEAIGlELPDELARMKAVI-------TLKMVGFDEEKaeeiL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 158 TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAV----MVISHDRAFVDNITNRTIEV 233
Cdd:TIGR03269 422 DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqtfIIVSHDMDFVLDVCDRAALM 501
|
....*..
gi 1525942895 234 TMGRIYD 240
Cdd:TIGR03269 502 RDGKIVK 508
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-238 |
4.81e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAViaylpqhLLTQDKvtv 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI-------NLVRDK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 fEETMKAFEevtqmQKELDELNEQLT-IRTDYETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQ 160
Cdd:PRK10619 76 -DGQLKVAD-----KNQLRLLRTRLTmVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE---SIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGR 237
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
.
gi 1525942895 238 I 238
Cdd:PRK10619 230 I 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-238 |
7.31e-15 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 73.72 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAViaylpqHLL 74
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKNI------NEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKVTVFE-----ETMKAFEEVTQMQKELDELNEQLTIRTDyetddyMKLIERVSeLSEKfysieETNYDAEVekvlkg 149
Cdd:cd03262 75 RQKVGMVFQqfnlfPHLTVLENITLAPIKVKGMSKAEAEERA------LELLEKVG-LADK-----ADAYPAQL------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 lgferkdftrqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK---AVMVISHDRAFVDNI 226
Cdd:cd03262 137 ---------------SGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREV 201
|
250
....*....|..
gi 1525942895 227 TNRTIEVTMGRI 238
Cdd:cd03262 202 ADRVIFMDDGRI 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-195 |
7.53e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAylpQHLLTQDKVTV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA---RARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 feetmkafeeVTQmqkeLDELNEQLTIRTDyetddymkLIervseLSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRqT 161
Cdd:PRK13536 119 ----------VPQ----FDNLDLEFTVREN--------LL-----VFGRYFGMSTREIEAVIPSLLEFARLESKADAR-V 170
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 162 SEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK13536 171 SDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-500 |
9.02e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF--GGT--TLFSDVTFSINENDKIALMGKNGAGKS-TILKIIADVAKPTTGNVTGPkeavIAYLPQHLLT 75
Cdd:PRK15134 5 LLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPSGD----IRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 76 QDKVT-----------VFEETMKAFEEVTQMQKELDE-LNEQLTIRTDYETDDYMKLIERVSelsekfysieetnydaeV 143
Cdd:PRK15134 81 ASEQTlrgvrgnkiamIFQEPMVSLNPLHTLEKQLYEvLSLHRGMRREAARGEILNCLDRVG-----------------I 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 144 EKVLKGLgferKDFTRQtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQWLEDFLINSAK-----AVMVISH 218
Cdd:PRK15134 144 RQAAKRL----TDYPHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAQILQLLRELQqelnmGLLFITH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 219 DRAFVDNITNRTIEVTMGRIYDykakyshylQLRADRRIHQLKAYEEQQRFIADNQefidrfrgtySKTLQVQSRVKMLe 298
Cdd:PRK15134 216 NLSIVRKLADRVAVMQNGRCVE---------QNRAATLFSAPTHPYTQKLLNSEPS----------GDPVPLPEPASPL- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 299 kLEVieidevdtSALRLKFPpsPRSGQypvmveeLTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM---- 374
Cdd:PRK15134 276 -LDV--------EQLQVAFP--IRKGI-------LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLrlin 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 375 --NEIDFEGG----------LKVGHNAKIGYfaQNQAALLDENLTVFETIDQ-----IPLTDGSIKIKDLLGAFMFSGDD 437
Cdd:PRK15134 338 sqGEIWFDGQplhnlnrrqlLPVRHRIQVVF--QDPNSSLNPRLNVLQIIEEglrvhQPTLSAAQREQQVIAVMEEVGLD 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 438 TTKKVKV---LSGGEKTRLAMIK-LLLEPvNVLILDEPTNHLDMKTKDIIKDALKDFDGT----LILVSHD 500
Cdd:PRK15134 416 PETRHRYpaeFSGGQRQRIAIARaLILKP-SLIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHD 485
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
7-196 |
9.80e-15 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 74.08 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 7 ISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlLTQDKVTVFEETM 86
Cdd:TIGR03873 7 VSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD--------------LAGVDLHGLSRRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 87 KAFEEVTQMQKELDELNeqLTIRTdyetddyMKLIERVSELSekFYSIEETNYDAEVEKVLKGLGFErkDF-TRQTSEFS 165
Cdd:TIGR03873 73 RARRVALVEQDSDTAVP--LTVRD-------VVALGRIPHRS--LWAGDSPHDAAVVDRALARTELS--HLaDRDMSTLS 139
|
170 180 190
....*....|....*....|....*....|.
gi 1525942895 166 GGWRMRIELAKILLKKPDLILLDEPTNHMDI 196
Cdd:TIGR03873 140 GGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-219 |
1.34e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 76.25 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 12 GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-----------GPKEAVIAYLPQ--HLLTqdk 78
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQdaHLFD--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 VTVFEETMKAFEEVTqmqkeldelneqltirtdyetddymkliervselsekfysieetnyDAEVEKVLKGLGFErkDFT 158
Cdd:TIGR02868 423 TTVRENLRLARPDAT----------------------------------------------DEELWAALERVGLA--DWL 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 159 RQTSE------------FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE-SIQWLEDFL-INSAKAVMVISHD 219
Cdd:TIGR02868 455 RALPDgldtvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLaALSGRTVVLITHH 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
305-500 |
1.56e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 76.25 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 305 IDEVDTSALRLKFPPSPRSGQYPV-----MVEELTKTY-GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID 378
Cdd:TIGR02868 307 IVEVLDAAGPVAEGSAPAAGAVGLgkptlELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 379 FEGG---------LKVGHN---AKIGYFAQNQ---AALLDENLTVF-ETIDQIPLTDG--SIKIKDLLGAfMFSGDDT-- 438
Cdd:TIGR02868 387 PLQGevtldgvpvSSLDQDevrRRVSVCAQDAhlfDTTVRENLRLArPDATDEELWAAleRVGLADWLRA-LPDGLDTvl 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 439 TKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKT-KDIIKDALKDFDG-TLILVSHD 500
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
331-519 |
1.73e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 72.44 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 331 EELTKTYGDHVV-FQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGL-KVG-------HNAKIGYFAQN---- 397
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTiRVNgqdvsdlRGRAIPYLRRKigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 -QAALLDENLTVFET------IDQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKvLSGGEKTRLAMIKLLLEPVNVLILDE 470
Cdd:cd03292 84 fQDFRLLPDRNVYENvafaleVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 471 PTNHLDMKTKDIIKDALKDFD--GTLILVS-HDRDFLDGLVQKVFEFGNKRV 519
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
330-500 |
1.98e-14 |
|
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: 72.50 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD----HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI-------MNEIDFEGGLKVGHNAKIGYFAQnQ 398
Cdd:cd03293 3 VRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIaglerptSGEVLVDGEPVTGPGPDRGYVFQ-Q 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AALLdENLTVFETIdQIPLTDGSIKIKDLLGAfmfsGDDTTKKV----------KVLSGGEKTRLAMIK-LLLEPvNVLI 467
Cdd:cd03293 82 DALL-PWLTVLDNV-ALGLELQGVPKAEARER----AEELLELVglsgfenaypHQLSGGMRQRVALARaLAVDP-DVLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1525942895 468 LDEPTNHLDMKTKDIIKDALKD----FDGTLILVSHD 500
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-223 |
3.27e-14 |
|
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: 72.19 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV------------IAYLPQ 71
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhkrarlgIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HLLTQDKVTVfEETMKAFEEVTqmqkeldelneqltirtdyeTDDYMKLIERVSELSEKFysieetnydaEVEKVLKGLG 151
Cdd:cd03218 83 EASIFRKLTV-EENILAVLEIR--------------------GLSKKEREEKLEELLEEF----------HITHLRKSKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 ferkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD---IESIQWLEDFLINSAKAVMVISH---------D 219
Cdd:cd03218 132 ----------SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDHnvretlsitD 201
|
....
gi 1525942895 220 RAFV 223
Cdd:cd03218 202 RAYI 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-227 |
3.44e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 70.54 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltqdkvtvFE 83
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL----------------------VD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 ETMKAFEEVTQMQKeldelneqltirtdyetddymKLIERVSELsekfysieetnydaevekvlkglgferkdftrqtse 163
Cdd:cd03216 61 GKEVSFASPRDARR---------------------AGIAMVYQL------------------------------------ 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 164 fSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISH----DRAFVDNIT 227
Cdd:cd03216 84 -SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISHrldeVFEIADRVT 153
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
1-234 |
4.57e-14 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 71.65 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-----GGTTL--FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviayLPQHl 73
Cdd:TIGR02324 1 LLEVEDLSKTFtlhqqGGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRI----------LVRH- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 ltQDKVTvfeetmkafEEVTQMQKELDELNEQlTIrtDYETDdYMKLIERVSELS-------EKFYSIEETNydAEVEKV 146
Cdd:TIGR02324 70 --EGAWV---------DLAQASPREVLEVRRK-TI--GYVSQ-FLRVIPRVSALEvvaepllERGVPREAAR--ARAREL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 147 LKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAK----AVMVISHDRAF 222
Cdd:TIGR02324 133 LARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVE-LIAEAKargaALIGIFHDEEV 211
|
250
....*....|..
gi 1525942895 223 VDNITNRTIEVT 234
Cdd:TIGR02324 212 RELVADRVMDVT 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-237 |
7.00e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.93 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-----GGTTL--FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-------------G 60
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 61 PKE------AVIAYLPQHLLTQDKVTvfeetmkAFEEVTQmqkeldelneqltirtdyetddymKLIERVSELSEKfysi 134
Cdd:COG4778 84 PREilalrrRTIGYVSQFLRVIPRVS-------ALDVVAE------------------------PLLERGVDREEA---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 135 eetnyDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA-- 212
Cdd:COG4778 129 -----RARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE-LIEEAKArg 202
|
250 260
....*....|....*....|....*..
gi 1525942895 213 -VMV-ISHDRAFVDNITNRTIEVTMGR 237
Cdd:COG4778 203 tAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
330-499 |
7.62e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 69.65 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYG--DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnaKIgYFAQNQAALLDENLT 407
Cdd:cd03247 3 INNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG-------EI-TLDGVPVSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 -VFETIDQIP-LTDGSIKikDLLGafmfsgddttkkvKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----D 481
Cdd:cd03247 75 sLISVLNQRPyLFDTTLR--NNLG-------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITErqllS 139
|
170
....*....|....*...
gi 1525942895 482 IIKDALKdfDGTLILVSH 499
Cdd:cd03247 140 LIFEVLK--DKTLIWITH 155
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
330-500 |
8.44e-14 |
|
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: 70.67 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MN----------EIDFEG----GLKVGHNA---K 390
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNdlipgapdegEVLLDGkdiyDLDVDVLElrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 391 IGYFAQnQAALLDenLTVFETIDqIPLTDGSIKIKDLLGAFM---FSGDDTTKKVK------VLSGGEKTRLAMIK-LLL 460
Cdd:cd03260 83 VGMVFQ-KPNPFP--GSIYDNVA-YGLRLHGIKLKEELDERVeeaLRKAALWDEVKdrlhalGLSGGQQQRLCLARaLAN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 461 EPvNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSHD 500
Cdd:cd03260 159 EP-EVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-238 |
8.84e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 70.39 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV-------TGPKEAVIAYLPQHLL 74
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKVTVFEEtMKAFEEVTQMQKeldelnEQLTIRTDYetddymkLIERVsELSEKfysieetnydaeVEKVLKglgfer 154
Cdd:cd03269 81 LYPKMKVIDQ-LVYLAQLKGLKK------EEARRRIDE-------WLERL-ELSEY------------ANKRVE------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 kdftrqtsEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISHDRAFVDNITNRTI 231
Cdd:cd03269 128 --------ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVL 199
|
....*..
gi 1525942895 232 EVTMGRI 238
Cdd:cd03269 200 LLNKGRA 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-238 |
1.04e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGN-------VTGPKEAViaylpqHL 73
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdglkVNDPKVDE------RL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 LTQDKVTVFEE-----TMKAFEEV----TQMQKELDELNEQLTirtdyetddyMKLIERVselsekfysieetnydaeve 144
Cdd:PRK09493 75 IRQEAGMVFQQfylfpHLTALENVmfgpLRVRGASKEEAEKQA----------RELLAKV-------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 145 kvlkGLGfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDfLINSAKAVMVISHDR 220
Cdd:PRK09493 125 ----GLA-ERAH--HYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQD-LAEEGMTMVIVTHEI 196
|
250
....*....|....*...
gi 1525942895 221 AFVDNITNRTIEVTMGRI 238
Cdd:PRK09493 197 GFAEKVASRLIFIDKGRI 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-238 |
1.06e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 70.61 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKE-----AVIA 67
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 68 YLPQH--LLtqDKVTVFEETMKAFEEVTQMQKEldELNEQLTirtdyetddyMKLiERVselsekfysieetnydaevek 145
Cdd:cd03261 81 MLFQSgaLF--DSLTVFENVAFPLREHTRLSEE--EIREIVL----------EKL-EAV--------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 146 vlkGL-GFERKdftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD-------IESIQWLEDFLINSakaVMVIS 217
Cdd:cd03261 125 ---GLrGAEDL----YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGLT---SIMVT 194
|
250 260
....*....|....*....|.
gi 1525942895 218 HDRAFVDNITNRTIEVTMGRI 238
Cdd:cd03261 195 HDLDTAFAIADRIAVLYDGKI 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-218 |
1.24e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 5 NNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaVIAYLPQHlltqdkvtvFEE 84
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI------LIDGQEMR---------FAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 85 TMKAFEE-VTQMQKELdELNEQLTirtdyetddymklierVSE------LSEKFYSIEETNYDAEVEKVLKGLGfERKDF 157
Cdd:PRK11288 73 TTAALAAgVAIIYQEL-HLVPEMT----------------VAEnlylgqLPHKGGIVNRRLLNYEAREQLEHLG-VDIDP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 158 TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPT---NHMDIESIQWLEDFLINSAKAVMVISH 218
Cdd:PRK11288 135 DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTsslSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-240 |
1.36e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.07 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFG----GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltq 76
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 dkvtvFEETmkafeEVTQM-QKELDEL-NE------QltirtDYETDDYMKLIERVsELSEKFYSIEETNYDAEVEKVLK 148
Cdd:COG1136 67 -----IDGQ-----DISSLsERELARLrRRhigfvfQ-----FFNLLPELTALENV-ALPLLLAGVSRKERRERARELLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 --GLGfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINSAKAVMVISHDRAf 222
Cdd:COG1136 131 rvGLG-DRLD--HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPE- 206
|
250
....*....|....*...
gi 1525942895 223 VDNITNRTIEVTMGRIYD 240
Cdd:COG1136 207 LAARADRVIRLRDGRIVS 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
1.54e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.53 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHL------L 74
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarrravL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKVTVFeetmkAF--EEVTQM--------QKELDELNEQLTIRTDyetddymklierVSELSEKFYsieetnydaeve 144
Cdd:COG4559 81 PQHSSLAF-----PFtvEEVVALgraphgssAAQDRQIVREALALVG------------LAHLAGRSY------------ 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 145 kvlkglgferkdftrqtSEFSGGWRMRIELAKILL-------KKPDLILLDEPTNHMDI 196
Cdd:COG4559 132 -----------------QTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
1.70e-13 |
|
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: 68.78 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT--LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKE--AVIAY 68
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQhlltqdKVTVFEETmkafeevtqmqkeldelneqltirtdyetddymkLIERVselsekfysieetnydaevekvlk 148
Cdd:cd03246 81 LPQ------DDELFSGS----------------------------------IAENI------------------------ 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 149 glgferkdftrqtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA----VMVISH 218
Cdd:cd03246 97 ---------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ-AIAALKAagatRIVIAH 154
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
340-507 |
1.93e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 340 HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEidfeggLKVGHNAKIGYFAQNQaalLDENLTVFETIDQIPLTD 419
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------LKGTPVAGCVDVPDNQ---FGREASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 420 GSIKIKDLLG---AFMFsgddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIK----DALKDFDG 492
Cdd:COG2401 114 DAVELLNAVGlsdAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVArnlqKLARRAGI 188
|
170
....*....|....*
gi 1525942895 493 TLILVSHDRDFLDGL 507
Cdd:COG2401 189 TLVVATHHYDVIDDL 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-504 |
1.97e-13 |
|
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: 69.21 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAK----------IGYFAQNqaalLDENL---TVFE--TIDQ 414
Cdd:cd03226 23 LYAGEIIALTGKNGAGKTTLAKILAGLIKESSG-SILLNGKpikakerrksIGYVMQD----VDYQLftdSVREelLLGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 415 IPLTDGSIKIKDLLGAFMFSGDDTtKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF---D 491
Cdd:cd03226 98 KELDAGNEQAETVLKDLDLYALKE-RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELaaqG 176
|
170
....*....|...
gi 1525942895 492 GTLILVSHDRDFL 504
Cdd:cd03226 177 KAVIVITHDYEFL 189
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
337-499 |
4.27e-13 |
|
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: 69.34 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 337 YGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM--------NEIDFEGGLKVGHN-----AKIGYFAQNQAALLD 403
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygNDVRLFGERRGGEDvwelrKRIGLVSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 ENLTVFETIdqipLT--DGSI------------KIKDLLGAF-MfsGDDTTKKVKVLSGGEKTRL----AMIKlllEPVn 464
Cdd:COG1119 93 RDETVLDVV----LSgfFDSIglyreptdeqreRARELLELLgL--AHLADRPFGTLSQGEQRRVliarALVK---DPE- 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1525942895 465 VLILDEPTNHLDMKTKDIIKDAL----KDFDGTLILVSH 499
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLdklaAEGAPTLVLVTH 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-238 |
4.65e-13 |
|
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: 67.94 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVA--KPTTGNVTgpkeaviaylpqhlltqdkvtv 81
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEIL---------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEEtmkafEEVTQMQKEldelneqltirtdyetddymkliervselsekfysieetnydaevEKVLKG--LGFER----- 154
Cdd:cd03217 61 FKG-----EDITDLPPE---------------------------------------------ERARLGifLAFQYppeip 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 ----KDFTRQTSE-FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISHDRAFVDNI 226
Cdd:cd03217 91 gvknADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
250
....*....|...
gi 1525942895 227 TNRTIEVTM-GRI 238
Cdd:cd03217 171 KPDRVHVLYdGRI 183
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
330-503 |
5.14e-13 |
|
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: 68.75 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD-HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIDfEGGLKV--------------GHNAKIG 392
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPT-SGSVLIdgtdinklkgkalrQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 393 YFAQNQAalLDENLTVFETI-----DQIPLtdgsikIKDLLGafMFSGDDT----------------TKKVKVLSGGEKT 451
Cdd:cd03256 82 MIFQQFN--LIERLSVLENVlsgrlGRRST------WRSLFG--LFPKEEKqralaalervglldkaYQRADQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 452 RLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF---DGTLILVS-HDRDF 503
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDL 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-59 |
5.57e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-----GGTTL-----------------FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhePSRSLkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
.
gi 1525942895 59 T 59
Cdd:COG1134 84 E 84
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
337-502 |
6.57e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 67.26 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 337 YGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVGHNAKIGYFAQNQAalLDENL--TVFETID 413
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAGGARVAYVPQRSE--VPDSLplTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 414 ---------QIPLT--DGSIKIKDL--LGAFMFSGddttKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK 480
Cdd:NF040873 80 mgrwarrglWRRLTrdDRAAVDDALerVGLADLAG----RQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180
....*....|....*....|....*
gi 1525942895 481 DIIKDALKDF--DG-TLILVSHDRD 502
Cdd:NF040873 156 ERIIALLAEEhaRGaTVVVVTHDLE 180
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-247 |
7.98e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF---GGTTLF----------SDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviA 67
Cdd:PRK15079 8 LLEVADLKVHFdikDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV--------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 68 YLPQHLLTQDkvtvfEETMKAFEEVTQM--QKELDELNEQLTIRtdyetddymkliERVSELSEKFY---SIEETNydAE 142
Cdd:PRK15079 80 WLGKDLLGMK-----DDEWRAVRSDIQMifQDPLASLNPRMTIG------------EIIAEPLRTYHpklSRQEVK--DR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 143 VEKVLKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQ-----WLEDFLINSAKAVMVIS 217
Cdd:PRK15079 141 VKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQaqvvnLLQQLQREMGLSLIFIA 219
|
250 260 270
....*....|....*....|....*....|...
gi 1525942895 218 HDRAFVDNITNRTIEVTMGR---IYDYKAKYSH 247
Cdd:PRK15079 220 HDLAVVKHISDRVLVMYLGHaveLGTYDEVYHN 252
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
8.52e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 66.95 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGG--TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltqdkv 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tvFEETmkafeEVTQMQKELDELneqltirtdyetddymklierVSELSEKFYSIEETnydaevekVLKGLGferkdftr 159
Cdd:cd03247 61 --LDGV-----PVSDLEKALSSL---------------------ISVLNQRPYLFDTT--------LRNNLG-------- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 160 qtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSA--KAVMVISH 218
Cdd:cd03247 97 --RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLkdKTLIWITH 155
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-229 |
8.92e-13 |
|
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: 68.08 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqhlltqdKVT 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG---------------------EIL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEetmkafEEVTQM-QKELDELNEQ-------------LTIRtdyetddymkliERVSelsekFYSIEETNYDAE---- 142
Cdd:COG1127 64 VDG------QDITGLsEKELYELRRRigmlfqggalfdsLTVF------------ENVA-----FPLREHTDLSEAeire 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 143 -VEKVLK--GL-GFERKdftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA-----V 213
Cdd:COG1127 121 lVLEKLElvGLpGAADK----MPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDE-LIRELRDelgltS 195
|
250
....*....|....*.
gi 1525942895 214 MVISHDRAFVDNITNR 229
Cdd:COG1127 196 VVVTHDLDSAFAIADR 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-191 |
9.60e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKEAV---IAYLPQ 71
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrSPRDAQaagIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HLLTQDKVTVFE------ETMKAFeevtqmqkeldelneqlTIrtdyetdDYMKLIERVSELsekfysieetnydaevek 145
Cdd:COG1129 87 ELNLVPNLSVAEniflgrEPRRGG-----------------LI-------DWRAMRRRAREL------------------ 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525942895 146 vLKGLGFERkDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPT 191
Cdd:COG1129 125 -LARLGLDI-DPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
337-511 |
1.16e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 67.74 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 337 YGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaIMNEIDF--EGGLKVG----------HNAKIGY-FAQNQAALLD 403
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLK-ILSGLLQptSGEVRVAglvpwkrrkkFLRRIGVvFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 ----ENLTVFETIDQIPltDGSIKIK-DLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMK 478
Cdd:cd03267 110 lpviDSFYLLAAIYDLP--PARFKKRlDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1525942895 479 TK----DIIKDALKDFDGTLILVSHDRDFLDGLVQKV 511
Cdd:cd03267 188 AQenirNFLKEYNRERGTTVLLTSHYMKDIEALARRV 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
330-518 |
1.17e-12 |
|
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: 67.75 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVfQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAK-----------IGYFAQNQ 398
Cdd:cd03299 3 VENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG-KILLNGKditnlppekrdISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AalLDENLTVFETID---------------QIPLTDGSIKIKDLLgafmfsgddtTKKVKVLSGGEKTRLAMIK-LLLEP 462
Cdd:cd03299 81 A--LFPHMTVYKNIAyglkkrkvdkkeierKVLEIAEMLGIDHLL----------NRKPETLSGGEQQRVAIARaLVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 463 vNVLILDEPTNHLDMKTKD----IIKDALKDFDGTLILVSHDRD-----------FLDGlvqKVFEFGNKR 518
Cdd:cd03299 149 -KILLLDEPFSALDVRTKEklreELKKIRKEFGVTVLHVTHDFEeawaladkvaiMLNG---KLIQVGKPE 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-234 |
1.47e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.22 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 13 GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQH----LLTqdkvtvfeetmka 88
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylpLGT------------- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 89 feevtqmqkeldeLNEQLTirtdyetddYMKLIERVSelsekfysieetnyDAEVEKVLK--GLG--FERKDFTRQ-TSE 163
Cdd:COG4178 442 -------------LREALL---------YPATAEAFS--------------DAELREALEavGLGhlAERLDEEADwDQV 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 164 FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVIS--HdRAFVDNITNRTIEVT 234
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISvgH-RSTLAAFHDRVLELT 557
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-254 |
1.55e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF---------GGT--TLFS----------DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGAlkGLFRreyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 60 gpkeaVIAYLPQhlltqdkvtvfeetmkafeevtqmqKELDELNEQLTI----RT----D---YETDDYMKLIervsels 128
Cdd:COG4586 81 -----VLGYVPF-------------------------KRRKEFARRIGVvfgqRSqlwwDlpaIDSFRLLKAI------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 129 ekfYSIEETNYDAEVEKVLKGLGFErkDF-TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL- 206
Cdd:COG4586 124 ---YRIPDAEYKKRLDELVELLDLG--ELlDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLk 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 207 -INSAKAVMVI--SHDRAFVDNITNRTIEVTMGR-IYD-----YKAKYSHYLQLRAD 254
Cdd:COG4586 199 eYNRERGTTILltSHDMDDIEALCDRVIVIDHGRiIYDgsleeLKERFGPYKTIVLE 255
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
330-500 |
1.59e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYG--DHV--VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHN-------AKIGYFAQ 396
Cdd:PRK10584 9 VHHLKKSVGqgEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGevSLVGQPlhqmdeeARAKLRAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 N-----QAALLDENLTVFETIdQIPL----------TDGSIKIKDLLGAfmfsGDDTTKKVKVLSGGEKTRLAMIKLLLE 461
Cdd:PRK10584 89 HvgfvfQSFMLIPTLNALENV-ELPAllrgessrqsRNGAKALLEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 462 PVNVLILDEPTNHLDMKTKDIIKDAL----KDFDGTLILVSHD 500
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-238 |
1.88e-12 |
|
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: 66.82 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIA-----DVAKPTTG-------NVTGPKEAVIAYl 69
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlIPGAPDEGevlldgkDIYDLDVDVLEL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 pqhlltQDKVT-VFEETMkAFEevtqmqkeldelneqLTIRtdyetdDYMKLIERVSELSEKfysieeTNYDAEVEKVLK 148
Cdd:cd03260 80 ------RRRVGmVFQKPN-PFP---------------GSIY------DNVAYGLRLHGIKLK------EELDERVEEALR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 --GLGFERKDFTRQTSeFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAK---AVMVISHDRAFV 223
Cdd:cd03260 126 kaALWDEVKDRLHALG-LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEE-LIAELKkeyTIVIVTHNMQQA 203
|
250
....*....|....*
gi 1525942895 224 DNITNRTIEVTMGRI 238
Cdd:cd03260 204 ARVADRTAFLLNGRL 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-240 |
1.93e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 14 TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaYLPQHLLTQDKVTVFEETMKAFEEVT 93
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI--------FNGQPMSKLSSAAKAELRNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 94 QMQKELDELNEQLTIRtdyetddyMKLI---ERVSELSEKfysieetnydaeVEKVLKGLGFERKDFTRQtSEFSGGWRM 170
Cdd:PRK11629 94 QFHHLLPDFTALENVA--------MPLLigkKKPAEINSR------------ALEMLAAVGLEHRANHRP-SELSGGERQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 171 RIELAKILLKKPDLILLDEPTNHMDI---ESI-QWLEDFLINSAKAVMVISHDRAFVDNItNRTIEVTMGRIYD 240
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDArnaDSIfQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
2.24e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKEAV---IAY 68
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynklDHKLAAqlgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHLLTQDKVTVFEETMKAfeevtqmqkeldelneQLTIRTDYETD--DYMKLIERVSELsekfysieetnydaevekv 146
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG----------------RHLTKKVCGVNiiDWREMRVRAAMM------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 147 LKGLGFERkDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLedFLI-----NSAKAVMVISHDRA 221
Cdd:PRK09700 130 LLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLImnqlrKEGTAIVYISHKLA 206
|
....*...
gi 1525942895 222 FVDNITNR 229
Cdd:PRK09700 207 EIRRICDR 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-238 |
2.40e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV------------IAYL 69
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhararrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHLLTQDKVTVFEETMKAFEevtqmqkeldelneqltIRTDYETDDYMkliERVSELSEKFYsieetnydaeVEKVLKG 149
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQ-----------------IRDDLSAEQRE---DRANELMEEFH----------IEHLRDS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LGferkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD---IESIQWLEDFLINSAKAVMVISHDRAFVDNI 226
Cdd:PRK10895 134 MG----------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAV 203
|
250
....*....|..
gi 1525942895 227 TNRTIEVTMGRI 238
Cdd:PRK10895 204 CERAYIVSQGHL 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-216 |
2.51e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEA--------VIAYLpQH 72
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiddpdvaeACHYL-GH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 lltqdkvtvfeetmkafeevtqmqkeLDELNEQLTIRtdyetddymkliERVsELSEKFYSIEETNYDAEVEKV-LKGLg 151
Cdd:PRK13539 81 --------------------------RNAMKPALTVA------------ENL-EFWAAFLGGEELDIAAALEAVgLAPL- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 152 ferkdFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLED-FLINSAKAVMVI 216
Cdd:PRK13539 121 -----AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAElIRAHLAQGGIVI 181
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-238 |
2.69e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 66.90 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIA--DVAKPTTGNVTGPKEAVIAYLPQH-------LL 74
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDEraraglfLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKVTVFEETMKAFeevtqmqkeldeLNEQLTIRTDYETDDYMKLIERVSELSEKfysieetnydaevekvLKGLGFER 154
Cdd:TIGR01978 83 FQYPEEIPGVSNLEF------------LRSALNARRSARGEEPLDLLDFEKLLKEK----------------LALLDMDE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 KDFTRQTSE-FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAK----AVMVISHDRAFVDNITNR 229
Cdd:TIGR01978 135 EFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAE-GINRLRepdrSFLIITHYQRLLNYIKPD 213
|
250
....*....|
gi 1525942895 230 TIEVTM-GRI 238
Cdd:TIGR01978 214 YVHVLLdGRI 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-241 |
2.72e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.83 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKS-TILKIIADVAKptTGNVTGP-----KEavIAYLP 70
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAA--NGRIGGSatfngRE--ILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 QHLLTQdkvtvfeetMKAfEEVTQM-QKELDELNEqltirtdyetddYMKLIERVselsekfysieetnydAEVEKVLKG 149
Cdd:PRK09473 88 EKELNK---------LRA-EQISMIfQDPMTSLNP------------YMRVGEQL----------------MEVLMLHKG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LG----FE--------------RKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQWLEDFLINSAK 211
Cdd:PRK09473 130 MSkaeaFEesvrmldavkmpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLNELK 208
|
250 260 270
....*....|....*....|....*....|....*
gi 1525942895 212 -----AVMVISHDRAFVDNITNRTIEVTMGRIYDY 241
Cdd:PRK09473 209 refntAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-237 |
3.87e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAvIAYLPQHLL------ 74
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH-IEGLPGHQIarmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 -TQDKVTVFEEtMKAFEE--VTQMQKeldeLNEQLtIRTDYETDDYMKliervselSEKfysiEETNYDAE-VEKVlkGL 150
Cdd:PRK11300 84 rTFQHVRLFRE-MTVIENllVAQHQQ----LKTGL-FSGLLKTPAFRR--------AES----EALDRAATwLERV--GL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 151 gferKDFT-RQTSEFSGGWRMRIELAKILLKKPDLILLDEPT---NHMDIESIQWLEDFLINSAK-AVMVISHDRAFVDN 225
Cdd:PRK11300 144 ----LEHAnRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvTVLLIEHDMKLVMG 219
|
250
....*....|..
gi 1525942895 226 ITNRTIEVTMGR 237
Cdd:PRK11300 220 ISDRIYVVNQGT 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
330-472 |
4.20e-12 |
|
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: 65.92 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEG----GLKVGHNAK--IGYFAQ 396
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllpprsgSIRFDGrditGLPPHERARagIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAalLDENLTVFETIdqipltdgsikikdLLGAFMFSGDDTTK------------------KVKVLSGGEKTRLAMIKL 458
Cdd:cd03224 83 GRR--IFPELTVEENL--------------LLGAYARRRAKRKArlervyelfprlkerrkqLAGTLSGGEQQMLAIARA 146
|
170
....*....|....
gi 1525942895 459 LLEPVNVLILDEPT 472
Cdd:cd03224 147 LMSRPKLLLLDEPS 160
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-195 |
4.67e-12 |
|
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: 65.35 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---------TGPKEAVIAYLPQH 72
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQDKVTVFEETMKAFEEVTQMQKELDelneqltirtdyetddymkliERVSELSEKFysieetnydaEVEKVLKglgf 152
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEID---------------------ERVREVAELL----------QIEHLLD---- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 153 erkdftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:cd03301 126 ------RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
330-499 |
5.12e-12 |
|
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: 64.54 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD--HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMneidfeGGLKVGHNakigyfaqnqaalldenlT 407
Cdd:cd03246 3 VENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL------GLLRPTSG------------------R 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 VfeTIDQIPLTD-GSIKIKDLLGAFM-----FSGddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD 481
Cdd:cd03246 59 V--RLDGADISQwDPNELGDHVGYLPqddelFSG---SIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180
....*....|....*....|.
gi 1525942895 482 IIKDALKDFD---GTLILVSH 499
Cdd:cd03246 134 ALNQAIAALKaagATRIVIAH 154
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
327-512 |
5.35e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.61 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 327 PVMVEELTKTYGDHVVFQK-----ASMVIERGEKVAFVGKNGEGKSTMI------------KAIMNEIDF-EGGLKVGH- 387
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEKkaldnVNIEIEDGEFVGLIGHTGSGKSTLIqhlngllkptsgKIIIDGVDItDKKVKLSDi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 388 NAKIGY-FAQNQAALLDEnlTVFETIDQIP----LTDGSIK--IKDLLGAFMFSGDDTTKKVKV-LSGGEKTRLAMIKLL 459
Cdd:PRK13637 82 RKKVGLvFQYPEYQLFEE--TIEKDIAFGPinlgLSEEEIEnrVKRAMNIVGLDYEDYKDKSPFeLSGGQKRRVAIAGVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 460 -LEPvNVLILDEPTNHLDMKTKD----IIKDALKDFDGTLILVSHDRDFLDGLVQKVF 512
Cdd:PRK13637 160 aMEP-KILILDEPTAGLDPKGRDeilnKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
325-514 |
5.36e-12 |
|
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: 65.89 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 325 QYPVMVeeltKTYGD-HVVFQKASmvIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKVGHNAKIGYFAQNQAAllD 403
Cdd:cd03237 2 TYPTMK----KTLGEfTLEVEGGS--ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA--D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 ENLTVFE---TIDQIPLTDG--------SIKIKDLLgafmfsgddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:cd03237 74 YEGTVRDllsSITKDFYTHPyfkteiakPLQIEQIL----------DREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525942895 473 NHLDMKTKDIIKDALKDF----DGTLILVSHDRDFLDGLVQKVFEF 514
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
353-500 |
7.01e-12 |
|
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: 65.01 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 353 GEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGGLKVG---------HNAKIGYFAQNQAalLDENLTVFETI---- 412
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGlekpdggTIVLNGTVLFDsrkkinlppQQRKIGLVFQQYA--LFPHLNVRENLafgl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 413 ---DQIPLTDGSIKIKDLLGAfmfsgdDTTKKVKV--LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDII---- 483
Cdd:cd03297 101 krkRNREDRISVDELLDLLGL------DHLLNRYPaqLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLlpel 174
|
170
....*....|....*..
gi 1525942895 484 KDALKDFDGTLILVSHD 500
Cdd:cd03297 175 KQIKKNLNIPVIFVTHD 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
320-499 |
8.39e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 320 SPRSGQYPVMVEEL---TKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIDfEGGLKV--------- 385
Cdd:PRK13536 31 ASIPGSMSTVAIDLagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgMTSPD-AGKITVlgvpvpara 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 386 -GHNAKIGYFAQ----NQAALLDENLTVFETIDQIPLTDGSIKIKDLLG-AFMFSGDDTtkKVKVLSGGEKTRLAMIKLL 459
Cdd:PRK13536 110 rLARARIGVVPQfdnlDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEfARLESKADA--RVSDLSGGMKRRLTLARAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIKDALKDF---DGTLILVSH 499
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLlarGKTILLTTH 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-241 |
8.62e-12 |
|
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: 64.86 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 17 FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhllTQDKVT-VFEETMKafeevtqm 95
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT---------------VRGRVSsLLGLGGG-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 96 qkeldeLNEQLTIRtdyetdDYMKLIERV-----SELSEKFYSIEEtnydaevekvLKGLGferKDFTRQTSEFSGGWRM 170
Cdd:cd03220 95 ------FNPELTGR------ENIYLNGRLlglsrKEIDEKIDEIIE----------FSELG---DFIDLPVKTYSSGMKA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 171 RIELAKILLKKPDLILLDEPTNHMDIE----SIQWLEDFLINSAKAVMViSHDRAFVDNITNRTIEVTMGRIYDY 241
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQGKTVILV-SHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-191 |
9.55e-12 |
|
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: 64.76 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-GPKEavIAYLPQHLLTQDKVTVF 82
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRD--ITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 83 EETMKAFEEVTQMQkeldelNEQLTIRTDYEtDDYMKLIERVSELsekFysieetnydaeveKVLKglgfERKDftRQTS 162
Cdd:cd03224 81 PEGRRIFPELTVEE------NLLLGAYARRR-AKRKARLERVYEL---F-------------PRLK----ERRK--QLAG 131
|
170 180
....*....|....*....|....*....
gi 1525942895 163 EFSGGWRMRIELAKILLKKPDLILLDEPT 191
Cdd:cd03224 132 TLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-238 |
9.75e-12 |
|
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: 64.62 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNnISVSFGGTTLfsDVTFSINENdKIALMGKNGAGKSTILKIIADVAKPTTGNV---------------TGPKEAV 65
Cdd:cd03297 1 MLCVD-IEKRLPDFTL--KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 66 IAYLPQHLLTQDKVTVFEETMKAFEEVTQMQKELdelneqltirtdyetddymklieRVSELSEKFysieetnydaEVEK 145
Cdd:cd03297 77 IGLVFQQYALFPHLNVRENLAFGLKRKRNREDRI-----------------------SVDELLDLL----------GLDH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 146 VLKglgferkdftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK----AVMVISHDRA 221
Cdd:cd03297 124 LLN----------RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKnlniPVIFVTHDLS 193
|
250
....*....|....*..
gi 1525942895 222 FVDNITNRTIEVTMGRI 238
Cdd:cd03297 194 EAEYLADRIVVMEDGRL 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-239 |
1.13e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.78 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTL-FSdvtFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---------TGPKEAVIAYLP 70
Cdd:COG3840 1 MLRLDDLTYRYGDFPLrFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltaLPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 Q------HLltqdkvTVFEetmkafeevtqmqkeldelNEQLTIRTDyetddyMKLiervselsekfySIEETnydAEVE 144
Cdd:COG3840 78 QennlfpHL------TVAQ-------------------NIGLGLRPG------LKL------------TAEQR---AQVE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 145 KVLKGLGFERKDfTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHDR 220
Cdd:COG3840 112 QALERVGLAGLL-DRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDP 190
|
250
....*....|....*....
gi 1525942895 221 AFVDNITNRTIEVTMGRIY 239
Cdd:COG3840 191 EDAARIADRVLLVADGRIA 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-197 |
1.30e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV----------TGPKEAVIAylpq 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsKTPSDKAIR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 hLLTQDKVTVFEETmkafeevtqmqkeldELNEQLTIRTDyetddymkLIE---RVSELSEkfysiEETNydAEVEKVLK 148
Cdd:PRK11124 79 -ELRRNVGMVFQQY---------------NLWPHLTVQQN--------LIEapcRVLGLSK-----DQAL--ARAEKLLE 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GLGFErkDFT-RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE 197
Cdd:PRK11124 128 RLRLK--PYAdRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
330-503 |
1.31e-11 |
|
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: 64.09 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIDfEG-----GLKVGHN--------AKIGYF 394
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD-SGtiiidGLKLTDDkkninelrQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 395 AQNQAalLDENLTVFETIdqiplTDGSIKIK------------DLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIK-LLLE 461
Cdd:cd03262 82 FQQFN--LFPHLTVLENI-----TLAPIKVKgmskaeaeeralELLEKVGLA-DKADAYPAQLSGGQQQRVAIARaLAMN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 462 PvNVLILDEPTNHLDMKTK----DIIKDALKdfDG-TLILVSHDRDF 503
Cdd:cd03262 154 P-KVMLFDEPTSALDPELVgevlDVMKDLAE--EGmTMVVVTHEMGF 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
328-500 |
1.43e-11 |
|
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: 64.20 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIDfEGGLKVGHN------AK---IGYFAQ 396
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIagLEEPT-SGRIYIGGRdvtdlpPKdrdIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAalLDENLTVFETIdQIPLT-----DGSIKIKDLLGAFMFSGDDT-TKKVKVLSGGEKTRLAMIKLLLEPVNVLILDE 470
Cdd:cd03301 80 NYA--LYPHMTVYDNI-AFGLKlrkvpKDEIDERVREVAELLQIEHLlDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 471 PTNHLDMK----TKDIIKDALKDFDGTLILVSHD 500
Cdd:cd03301 157 PLSNLDAKlrvqMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-195 |
1.51e-11 |
|
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: 64.18 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-GPKEavIAYLPQHlltQDKV- 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILlDGKD--ITNLPPH---KRPVn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TVFEE-----TMKAFEEVT---QMQKeldeLNEQlTIRtdyetddymkliERVselsekfysieetnydAEVEKVLKGLG 151
Cdd:cd03300 76 TVFQNyalfpHLTVFENIAfglRLKK----LPKA-EIK------------ERV----------------AEALDLVQLEG 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1525942895 152 FERKDftrqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:cd03300 123 YANRK----PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
347-504 |
1.58e-11 |
|
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: 63.64 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAKIGYFAQN---QAALLDENLTVFETIDQiPLTDGSIK 423
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-SVSVPGSIAYVSQEpwiQNGTIRENILFGKPFDE-ERYEKVIK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 424 ----IKDLlgAFMFSGDDTT---KKVKvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKT-KDIIKDALKDF---DG 492
Cdd:cd03250 103 acalEPDL--EILPDGDLTEigeKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLllnNK 179
|
170
....*....|..
gi 1525942895 493 TLILVSHDRDFL 504
Cdd:cd03250 180 TRILVTHQLQLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-500 |
1.88e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPK-------EAVIAYL 69
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQ------HLLTQDKVTVFEETMKAFEEVTQMQkelDELNEQLTIRTDYETDDYMKLIERVSELSEKfysieetnydAEV 143
Cdd:PRK10261 92 EQsaaqmrHVRGADMAMIFQEPMTSLNPVFTVG---EQIAESIRLHQGASREEAMVEAKRMLDQVRI----------PEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 144 EKVLkglgferkdfTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHD 219
Cdd:PRK10261 159 QTIL----------SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 220 RAFVDNITNRTIEVTMGRIYD-------YKAKYSHYLQ--LRADRRIHQLKAYEEQQRFIADNQEfidrfrgtysktlQV 290
Cdd:PRK10261 229 MGVVAEIADRVLVMYQGEAVEtgsveqiFHAPQHPYTRalLAAVPQLGAMKGLDYPRRFPLISLE-------------HP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 291 QSRVKMLEKLEVIEIDEV-DTSALRLKFPpsPRSGQYPVMVEELtktygdHVVfQKASMVIERGEKVAFVGKNGEGKSTM 369
Cdd:PRK10261 296 AKQEPPIEQDTVVDGEPIlQVRNLVTRFP--LRSGLLNRVTREV------HAV-EKVSFDLWPGETLSLVGESGSGKSTT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 370 IKAIMNEIDFEGGlKVGHNAK----------------IGYFAQNQAALLDENLTVFETIDQiPLtdgsiKIKDLLgafmf 433
Cdd:PRK10261 367 GRALLRLVESQGG-EIIFNGQridtlspgklqalrrdIQFIFQDPYASLDPRQTVGDSIME-PL-----RVHGLL----- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 434 SGDDTTKKVKVL------------------SGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----DIIKDALKDFD 491
Cdd:PRK10261 435 PGKAAAARVAWLlervgllpehawryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLLLDLQRDFG 514
|
....*....
gi 1525942895 492 GTLILVSHD 500
Cdd:PRK10261 515 IAYLFISHD 523
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
338-499 |
1.92e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.78 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 338 GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG---------LKVGHNA---KIGYFAQNQAALLDen 405
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidiRDISRKSlrsMIGVVLQDTFLFSG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 406 lTVFETI---DQIPLTDGSIKIKDLLGAFMF-----SGDDTT--KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHL 475
Cdd:cd03254 92 -TIMENIrlgRPNATDEEVIEAAKEAGAHDFimklpNGYDTVlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180
....*....|....*....|....*.
gi 1525942895 476 DMKTKDIIKDAL-KDFDG-TLILVSH 499
Cdd:cd03254 171 DTETEKLIQEALeKLMKGrTSIIIAH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
328-500 |
2.34e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVGHNAKIGYFAQNQAalLDENL 406
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGKLRIGYVPQKLY--LDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 407 TVfeTIDQIPLTDGSIKIKDLLGAFmfsgddttKKVKV----------LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLD 476
Cdd:PRK09544 83 PL--TVNRFLRLRPGTKKEDILPAL--------KRVQAghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*...
gi 1525942895 477 MKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:PRK09544 153 VNGQvalyDLIDQLRRELDCAVLMVSHD 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
328-500 |
2.41e-11 |
|
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: 63.80 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------NEIDFEGGLKVG---HNAKIGYFAQN 397
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfetptsGEILLDGKDITNlppHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAalLDENLTVFE------TIDQIPLTDGSIKIKDLLGaFMFSGDDTTKKVKVLSGGEKTRLAMIK-LLLEPvNVLILDE 470
Cdd:cd03300 81 YA--LFPHLTVFEniafglRLKKLPKAEIKERVAEALD-LVQLEGYANRKPSQLSGGQQQRVAIARaLVNEP-KVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 471 PTNHLDMK-TKDI---IKDALKDFDGTLILVSHD 500
Cdd:cd03300 157 PLGALDLKlRKDMqleLKRLQKELGITFVFVTHD 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-220 |
2.50e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAvIAYLPQHlltQDKVT 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPY---QRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMQkeldelNEQLTIRTDYETDDYMKliERVSELSEKFYSIEetnydaevekvlkglgFERkdftRQ 160
Cdd:PRK11607 95 MMFQSYALFPHMTVEQ------NIAFGLKQDKLPKAEIA--SRVNEMLGLVHMQE----------------FAK----RK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPT--------NHMDIESIQWLEDFlinSAKAVMViSHDR 220
Cdd:PRK11607 147 PHQLSGGQRQRVALARSLAKRPKLLLLDEPMgaldkklrDRMQLEVVDILERV---GVTCVMV-THDQ 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-499 |
2.58e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 310 TSALRL----------KFPPS--PRSGQYPVMVEELTKTYGD--HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN 375
Cdd:PRK11160 309 ASARRIneiteqkpevTFPTTstAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 376 EIDFEGG--LKVGHNAKigyfAQNQAALlDENLTVfetIDQ-IPLTDGSIKiKDLLGAFMFSGDDTTKKV--KV------ 444
Cdd:PRK11160 389 AWDPQQGeiLLNGQPIA----DYSEAAL-RQAISV---VSQrVHLFSATLR-DNLLLAAPNASDEALIEVlqQVglekll 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 445 ----------------LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:PRK11160 460 eddkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITH 532
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
339-499 |
2.70e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.17 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 339 DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAImneidfeGGLKVGHNAKIGYFAQNQAALLDenltvfetidQIP-L 417
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLWPWGSGRIGMPEGEDLLFLP----------QRPyL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 418 TDGSikikdLLGAFMFSGDDttkkvkVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDFDGTLILV 497
Cdd:cd03223 76 PLGT-----LREQLIYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
..
gi 1525942895 498 SH 499
Cdd:cd03223 145 GH 146
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
347-498 |
3.16e-11 |
|
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: 62.57 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFE---GGLKV-GHN-------AKIGYFAQNQAALldENLTVFETidqi 415
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvsGEVLInGRPldkrsfrKIIGYVPQDDILH--PTLTVRET---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 416 pltdgsikikdllgaFMFSGddttkKVKVLSGGEKTRLAM-IKLLLEPvNVLILDEPTNHLDMKTKDIIKDALKDF--DG 492
Cdd:cd03213 103 ---------------LMFAA-----KLRGLSGGERKRVSIaLELVSNP-SLLFLDEPTSGLDSSSALQVMSLLRRLadTG 161
|
....*.
gi 1525942895 493 TLILVS 498
Cdd:cd03213 162 RTIICS 167
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
3.17e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.73 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGG----TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGN-------VTGPkeaviayl 69
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEitldgvpVTGP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 pqhllTQDKVTVFeetmkafeevtqmQKE--LDELNeqltirtdyetddymkLIERVsELSEKFYSIEETNYDAEVEKVL 147
Cdd:COG4525 75 -----GADRGVVF-------------QKDalLPWLN----------------VLDNV-AFGLRLRGVPKAERRARAEELL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 148 K--GL-GFERkdftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI---ESIQ-WLEDFLINSAKAVMVISHD 219
Cdd:COG4525 120 AlvGLaDFAR----RRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQMQeLLLDVWQRTGKGVFLITHS 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-191 |
3.20e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG---------NVTGPKEAV---IAY 68
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGeilidgkpvRIRSPRDAIalgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHLLTQDKVTVFEETMKAFEEVTQmqkeldelneqltIRTDYEtddymKLIERVSELSEKFysieetnydaevekvlk 148
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKG-------------GRLDRK-----AARARIRELSERY----------------- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 149 GLGFerkDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPT 191
Cdd:COG3845 130 GLDV---DPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-190 |
3.65e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.73 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTG--PKEAVIAYLPQ 71
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrilldgrDVTGlpPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 ------HLltqdkvTVFEETmkAFEevtqmqkeldelneqLTIRtdyetddymklieRVSElSEKfysieetnyDAEVEK 145
Cdd:COG3842 85 dyalfpHL------TVAENV--AFG---------------LRMR-------------GVPK-AEI---------RARVAE 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1525942895 146 VLK--GL-GFERkdftRQTSEFSGGWRMRIELAKILLKKPDLILLDEP 190
Cdd:COG3842 119 LLElvGLeGLAD----RYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-241 |
3.71e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.12 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLfSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTG--PKEAVIAYLPQH 72
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkillngkDITNlpPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQDKVTVFEETMKAFEEVTQMQKELDElneqltirtdyetddymklieRVSELSEKFysieetnydaEVEKVLkglgf 152
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIER---------------------KVLEIAEML----------GIDHLL----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 153 ERKDFTrqtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI---ESIQWLEDFLINSAK-AVMVISHDRAFVDNITN 228
Cdd:cd03299 124 NRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKEFGvTVLHVTHDFEEAWALAD 198
|
250
....*....|...
gi 1525942895 229 RTIEVTMGRIYDY 241
Cdd:cd03299 199 KVAIMLNGKLIQV 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
330-517 |
4.80e-11 |
|
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: 62.84 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEG----GLKVGHNAKIGYFAQNQ 398
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflrptsgSVLFDGeditGLPPHEIARLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AALLDENLTVFETID---QIPLTDGSI-------------KIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIKLL-LE 461
Cdd:cd03219 83 IPRLFPELTVLENVMvaaQARTGSGLLlararreereareRAEELL-ERVGLADLADRPAGELSYGQQRRLEIARALaTD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 462 PvNVLILDEPT---NHLDM-KTKDIIKDaLKDFDGTLILVSHDRDFLDGLVQK--VFEFGNK 517
Cdd:cd03219 162 P-KLLLLDEPAaglNPEETeELAELIRE-LRERGITVLLVEHDMDVVMSLADRvtVLDQGRV 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-218 |
4.97e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 62.87 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 14 TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYlpQHLLTQDKVTVfeetmkafeeVT 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKYLHSKVSL----------VG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 94 QmqkeldelNEQLTIRTDYETDDY---MKLIERVSELSEK-----FYSIEETNYDAEVEKvlKGlgferkdftrqtSEFS 165
Cdd:cd03248 95 Q--------EPVLFARSLQDNIAYglqSCSFECVKEAAQKahahsFISELASGYDTEVGE--KG------------SQLS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 166 GGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI--NSAKAVMVISH 218
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAH 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-238 |
5.45e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.33 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTG--PKEAVIAYLPQH 72
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgtDVSRlhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQDKVTVFEETmkAFEEVTQMQKEldelneqltiRTDYETDDY--MKLIERV--SELSEKFysieetnydaevekvlk 148
Cdd:PRK10851 83 YALFRHMTVFDNI--AFGLTVLPRRE----------RPNAAAIKAkvTQLLEMVqlAHLADRY----------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 glgferkdftrqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWL----EDFLINSakaVMViSHDR 220
Cdd:PRK10851 134 ------------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLrqlhEELKFTS---VFV-THDQ 197
|
250
....*....|....*...
gi 1525942895 221 AFVDNITNRTIEVTMGRI 238
Cdd:PRK10851 198 EEAMEVADRVVVMSQGNI 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
325-503 |
5.47e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.11 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 325 QYPVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-----------------NEIDFEGGLKVG- 386
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitgdksagshiellgRTVQREGRLARDi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 387 --HNAKIGYFAQnQAALLDEnLTVFETI-----DQIPL------------TDGSIKIKDLLGAFMFSgddtTKKVKVLSG 447
Cdd:PRK09984 82 rkSRANTGYIFQ-QFNLVNR-LSVLENVligalGSTPFwrtcfswftreqKQRALQALTRVGMVHFA----HQRVSTLSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 448 GEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF---DGTLILVS-HDRDF 503
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDY 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-238 |
5.61e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.15 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFG-GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-GPK----------EAVIAYL 69
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlNGFslkdidrhtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHLLTQDKVTVFEETMKAFEEVTQmqkeldelneqltirtdyetddymKLIERVSELSEkfysieetnYDAEVEKVLKG 149
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQ------------------------DEIWAACEIAE---------IKDDIENMPLG 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LGferKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLIN-SAKAVMVISHdRAFVDNITN 228
Cdd:TIGR01193 601 YQ---TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNlQDKTIIFVAH-RLSVAKQSD 676
|
250
....*....|
gi 1525942895 229 RTIEVTMGRI 238
Cdd:TIGR01193 677 KIIVLDHGKI 686
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
330-499 |
5.88e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------NEIDFEGG--LKVGHNAKIGYFAQNQAa 400
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAgllppaaGTIKLDGGdiDDPDVAEACHYLGHRNA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 401 lLDENLTVFETID--QIPLTDGSIKIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMK 478
Cdd:PRK13539 84 -MKPALTVAENLEfwAAFLGGEELDIAAAL-EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*
gi 1525942895 479 TK----DIIKDALKDfDGTLILVSH 499
Cdd:PRK13539 162 AValfaELIRAHLAQ-GGIVIAATH 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-487 |
7.02e-11 |
|
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: 65.32 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAKIGYFAQN------------------------ 397
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG-KIKHSGRISFSPQTswimpgtikdniifglsydeyryt 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 ---QAALLDENLTVFETIDQIPLTDGSIkikdllgafmfsgddttkkvkVLSGGEKTRLAMIKLLLEPVNVLILDEPTNH 474
Cdd:TIGR01271 520 sviKACQLEEDIALFPEKDKTVLGEGGI---------------------TLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170
....*....|....
gi 1525942895 475 LDMKT-KDIIKDAL 487
Cdd:TIGR01271 579 LDVVTeKEIFESCL 592
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-195 |
9.15e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQhllTQDKVTV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH---ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 feetmkafeeVTQmqkeLDELNEQLTIRTDyetddyMKLIERvselsekFYSIEETNYDAEVEKVLKGLGFERKDfTRQT 161
Cdd:PRK13537 85 ----------VPQ----FDNLDPDFTVREN------LLVFGR-------YFGLSAAAARALVPPLLEFAKLENKA-DAKV 136
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 162 SEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK13537 137 GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-190 |
9.27e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV------------IAY 68
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHlltqdkVTVF-----EETMKAFEEVTQMQKEldelneqltirtdyetddymKLIERVSELSEKFysieetnydaEV 143
Cdd:COG1137 83 LPQE------ASIFrkltvEDNILAVLELRKLSKK--------------------EREERLEELLEEF----------GI 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 144 EKVLKGLGferkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEP 190
Cdd:COG1137 127 THLRKSKA----------YSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-219 |
9.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLF-----SDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeavIAYLPQHLLTQ 76
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT------VDDITITHKTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DKVtvFEETMKAFEEVTQMQkeldelneqltirtdyETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKD 156
Cdd:PRK13646 77 DKY--IRPVRKRIGMVFQFP----------------ESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 157 FTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINSAKAVMVISHD 219
Cdd:PRK13646 139 MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD 205
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-191 |
1.01e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.82 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYlPQHLLTQDKVT 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTqmqkeldeLNEQLTIRTDY-ETDDYMKLIERVSELSEKFYsieetnydaevekvlkglgfERKdfTR 159
Cdd:PRK11614 84 IVPEGRRVFSRMT--------VEENLAMGGFFaERDQFQERIKWVYELFPRLH--------------------ERR--IQ 133
|
170 180 190
....*....|....*....|....*....|..
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPT 191
Cdd:PRK11614 134 RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
330-500 |
1.11e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAK-IGYFAQNQ----AALLDe 404
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSG-TVFLGDKpISMLSSRQlarrLALLP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 405 nltvfetidQIPLTDGSIKIKDLLgAF----------MFSGDD----------------TTKKVKVLSGGEKTR--LAMI 456
Cdd:PRK11231 83 ---------QHHLTPEGITVRELV-AYgrspwlslwgRLSAEDnarvnqameqtrinhlADRRLTDLSGGQRQRafLAMV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 457 klLLEPVNVLILDEPTNHLD-------MKTKDIIKDALKdfdgTLILVSHD 500
Cdd:PRK11231 153 --LAQDTPVVLLDEPTTYLDinhqvelMRLMRELNTQGK----TVVTVLHD 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-218 |
1.50e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.97 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 17 FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQdkvtvfeetmkafeeVTQMQ 96
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ---------------VALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 97 KELDELNEQLTIRTDYETDDY-MKLIERVSELS--EKFYSIEETNYDAEVEKvlKGlgferkdftrqtSEFSGGWRMRIE 173
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYGLTDTpDEEIMAAAKAAnaHDFIMEFPNGYDTEVGE--KG------------SQLSGGQKQRIA 627
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1525942895 174 LAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVISH 218
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-218 |
1.73e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.65 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 9 VSF---GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--G------PKEAV---IAYLPQhll 74
Cdd:COG1132 345 VSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidGvdirdlTLESLrrqIGVVPQ--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 tqdKVTVFEETMK---AF--EEVTQmqkelDELNE-----QLTirtdyetddymkliERVSELSEKfysieetnYDAEVE 144
Cdd:COG1132 422 ---DTFLFSGTIReniRYgrPDATD-----EEVEEaakaaQAH--------------EFIEALPDG--------YDTVVG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 145 KvlKGlgferkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES---IQW-LEDFLINsaKAVMVISH 218
Cdd:COG1132 472 E--RG------------VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealIQEaLERLMKG--RTTIVIAH 533
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
321-497 |
1.83e-10 |
|
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: 60.50 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 321 PRSGQypVMVEELTKTYGDHV--VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnaKIGYFAQNQ 398
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG-------KIEIDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AAL----LDENLTVfetIDQIP-LTDGSIKIKdlLGAF-MFSGDDTTKKVKV------LSGGEKTRLAMIKLLLEPVNVL 466
Cdd:cd03369 73 STIpledLRSSLTI---IPQDPtLFSGTIRSN--LDPFdEYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190
....*....|....*....|....*....|..
gi 1525942895 467 ILDEPTNHLDMKTKDIIKDAL-KDFDGTLILV 497
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIrEEFTNSTILT 179
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-235 |
1.94e-10 |
|
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: 60.26 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 8 SVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIAdvAKPTTGNVTG-------PKE-----AVIAYLPQHllt 75
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA--GRRTGLGVSGevlingrPLDkrsfrKIIGYVPQD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 76 qdkvtvfeetmkafeevtqmqkelDELNEQLTIRtdyetddymkliervselsEKFYsieetnYDAEvekvLKGLgferk 155
Cdd:cd03213 91 ------------------------DILHPTLTVR-------------------ETLM------FAAK----LRGL----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 156 dftrqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDiesiqwledflinSAKAVMVISHDRAFVDniTNRTIEVTM 235
Cdd:cd03213 113 ---------SGGERKRVSIALELVSNPSLLFLDEPTSGLD-------------SSSALQVMSLLRRLAD--TGRTIICSI 168
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-499 |
1.99e-10 |
|
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: 60.96 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 341 VVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHN---AKIGYFAQNQAALLDENLTVFETI-DQ 414
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvLVDGHDlalADPAWLRRQVGVVLQENVLFNRSIrDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 415 IPLTDGS------IKIKDLLGAFMF-----SGDDTT--KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD 481
Cdd:cd03252 96 IALADPGmsmervIEAAKLAGAHDFiselpEGYDTIvgEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180
....*....|....*....|
gi 1525942895 482 IIKDALKDF-DG-TLILVSH 499
Cdd:cd03252 176 AIMRNMHDIcAGrTVIIIAH 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-59 |
2.25e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 61.25 E-value: 2.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT 59
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-221 |
2.27e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKP---TTGNV--------TGPKEA-VIAY 68
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVllngrrltALPAEQrRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHLLTQDKVTVFEETmkAFEEVTQMQKEldelneqltirtdyetddymkliERvselsekfysieetnyDAEVEKVLK 148
Cdd:COG4136 81 LFQDDLLFPHLSVGENL--AFALPPTIGRA-----------------------QR----------------RARVEQALE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 --GL-GFERKDftrqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK-----AVMViSHDR 220
Cdd:COG4136 120 eaGLaGFADRD----PATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRqrgipALLV-THDE 194
|
.
gi 1525942895 221 A 221
Cdd:COG4136 195 E 195
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
328-500 |
2.35e-10 |
|
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: 60.82 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGGLKVGHNAK---IGYFAQN 397
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlerpdsgTILFGGEDATDVPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAalLDENLTVFETI----------DQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKvLSGGEKTRLAMIK-LLLEPvNVL 466
Cdd:cd03296 83 YA--LFRHMTVFDNVafglrvkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQ-LSGGQRQRVALARaLAVEP-KVL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1525942895 467 ILDEPTNHLDMKTKDIIKDALK----DFDGTLILVSHD 500
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRrlhdELHVTTVFVTHD 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.57e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.66 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT------GPKE-AVIAYLPqhl 73
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgeplDPEDrRRIGYLP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 ltqdkvtvfEE-----TMKAFeevtqmqkeldelnEQLTirtdyetddYM---------KLIERVSELSEKFysieetny 139
Cdd:COG4152 78 ---------EErglypKMKVG--------------EQLV---------YLarlkglskaEAKRRADEWLERL-------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 140 daevekvlkGLGfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKA-VMVI-- 216
Cdd:COG4152 118 ---------GLG-DRAN--KKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIfs 185
|
...
gi 1525942895 217 SHD 219
Cdd:COG4152 186 SHQ 188
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
337-499 |
2.58e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 63.22 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 337 YGDHVVfQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHNAK----------IGYFAQN----QAA 400
Cdd:TIGR01193 485 YGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeiLLNGFSLKdidrhtlrqfINYLPQEpyifSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 401 LLD-------ENLTVFETIDQIPLTDGSIKIKDLLGAFmfsGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTN 473
Cdd:TIGR01193 564 ILEnlllgakENVSQDEIWAACEIAEIKDDIENMPLGY---QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180
....*....|....*....|....*..
gi 1525942895 474 HLDMKT-KDIIKDALKDFDGTLILVSH 499
Cdd:TIGR01193 641 NLDTITeKKIVNNLLNLQDKTIIFVAH 667
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-238 |
3.00e-10 |
|
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: 60.67 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGT----TLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---------GPKEAV-- 65
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 66 ---IAYLPQH--LLTQDkvTVFEETMKAFeEVTQMQKEldelneqltirtdyetddymKLIERVSELSEkfysieetnyd 140
Cdd:cd03258 81 rrrIGMIFQHfnLLSSR--TVFENVALPL-EIAGVPKA--------------------EIEERVLELLE----------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 141 aevekvLKGLGfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAK--AVMVI 216
Cdd:cd03258 127 ------LVGLE-DKAD--AYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLrdINRELglTIVLI 197
|
250 260
....*....|....*....|..
gi 1525942895 217 SHDRAFVDNITNRTIEVTMGRI 238
Cdd:cd03258 198 THEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-239 |
3.04e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.27 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAVIAYLPQH 72
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 --LLTQDKVTVFEETMkafeevtqmqkeLDELNEQLTIRTDYETDdymkLIERVSelsekfysieetnydAEVEKVlkGL 150
Cdd:PRK10908 81 igMIFQDHHLLMDRTV------------YDNVAIPLIIAGASGDD----IRRRVS---------------AALDKV--GL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 151 GFERKDFTRQtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMD---IESIQWLEDFLINSAKAVMVISHDRAFVDNIT 227
Cdd:PRK10908 128 LDKAKNFPIQ---LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRS 204
|
250
....*....|..
gi 1525942895 228 NRTIEVTMGRIY 239
Cdd:PRK10908 205 YRMLTLSDGHLH 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
328-499 |
3.20e-10 |
|
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: 60.32 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHV-VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHN----------AKIGYF 394
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGsiLIDGQDirevtldslrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 395 AQNQAALldeNLTVFETID--QIPLTDGSI-------KIKDLLGAFMFsGDDTtkkvKV------LSGGEKTRLAMIKLL 459
Cdd:cd03253 81 PQDTVLF---NDTIGYNIRygRPDATDEEVieaakaaQIHDKIMRFPD-GYDT----IVgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIKDALKD-FDG-TLILVSH 499
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAH 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-504 |
3.27e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.24 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 335 KTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVghNAKIgyfaqnqAALL------DENLT 407
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpDSGTVTV--RGRV-------SSLLglgggfNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 VFETIdqipLTDGSIK------IKDLLGAF-MFS--GDDTTKKVKVLSGGEKTRLAM-IKLLLEPvNVLILDEPTNHLDM 477
Cdd:cd03220 101 GRENI----YLNGRLLglsrkeIDEKIDEIiEFSelGDFIDLPVKTYSSGMKARLAFaIATALEP-DILLIDEVLAVGDA 175
|
170 180 190
....*....|....*....|....*....|
gi 1525942895 478 KTKDIIKDALKDF---DGTLILVSHDRDFL 504
Cdd:cd03220 176 AFQEKCQRRLRELlkqGKTVILVSHDPSSI 205
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
318-487 |
4.63e-10 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 62.04 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 318 PPSPRSGQYP-------VMVEELTKTYG--DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVG 386
Cdd:TIGR02203 314 PPEKDTGTRAierargdVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqiLLDG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 387 HN----------------------------AKIGYFAQNQA-------ALLDENLTVFetIDQIPLtdgsikikdllgaf 431
Cdd:TIGR02203 394 HDladytlaslrrqvalvsqdvvlfndtiaNNIAYGRTEQAdraeierALAAAYAQDF--VDKLPL-------------- 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 432 mfsGDDTTKKVK--VLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDAL 487
Cdd:TIGR02203 458 ---GLDTPIGENgvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL 512
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
350-500 |
4.75e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKVGHN----------AKI-GYFAQNQAALLdeNLTVFETI-----D 413
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQpleawsaaelARHrAYLSQQQTPPF--AMPVFQYLtlhqpD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 414 QIPLTDGSIKIKDLLGAFMFsGDDTTKKVKVLSGGE--KTRLAMIKLLLEPVN-----VLILDEPTNHLDMKTKDIIKDA 486
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEwqRVRLAAVVLQVWPDInpagqLLLLDEPMNSLDVAQQAALDRL 175
|
170
....*....|....*..
gi 1525942895 487 LKDF---DGTLILVSHD 500
Cdd:PRK03695 176 LSELcqqGIAVVMSSHD 192
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-224 |
4.94e-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: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 32 LMGKNGAGKSTILKIIADVAKPTTGNVTGPKE--AVIAYLPQHLLtQDKVT-VFEETMKAF---EEVTQMQKELDELNEQ 105
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEILDEFRGSEL-QNYFTkLLEGDVKVIvkpQYVDLIPKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 106 LTIRTDyETDDYMKLIERVselsekfysieetnydaEVEKVLKglgferkdftRQTSEFSGGWRMRIELAKILLKKPDLI 185
Cdd:cd03236 110 LLKKKD-ERGKLDELVDQL-----------------ELRHVLD----------RNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 186 LLDEPTNHMDIE---SIQWLEDFLINSAKAVMVISHDRAFVD 224
Cdd:cd03236 162 FFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-230 |
5.36e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKII---ADVAKPTTgnVTGpkeaVIAYLPQHLLTQD 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVT--ITG----SIVYNGHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 78 KVTVfeetmkafeevtQMQKELDELNEQ-----LTIrtdYETDDYMKLIERVSElsekfysieETNYDAEVEKVLKGLGF 152
Cdd:PRK14239 79 TDTV------------DLRKEIGMVFQQpnpfpMSI---YENVVYGLRLKGIKD---------KQVLDEAVEKSLKGASI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 153 --ERKDFTRQTS-EFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK--AVMVISHDRAFVDNIT 227
Cdd:PRK14239 135 wdEVKDRLHDSAlGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRIS 214
|
...
gi 1525942895 228 NRT 230
Cdd:PRK14239 215 DRT 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-191 |
5.56e-10 |
|
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: 59.61 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTG--PKEAV---IAY 68
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgeDITGlpPHRIArlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQ------HLltqdkvTVfEEtmkafeevtqmqkeldelNEQLTIRTDYETDDYMKLIERVSELsekFysieetnydae 142
Cdd:COG0410 83 VPEgrrifpSL------TV-EE------------------NLLLGAYARRDRAEVRADLERVYEL---F----------- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1525942895 143 veKVLKglgfERKDftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPT 191
Cdd:COG0410 124 --PRLK----ERRR--QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
327-499 |
5.91e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 327 PVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGL---------KVGHNAKIGYFAQN 397
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSislcgepvpSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAALLD------ENLTVFETIDQIPLTDGSIKIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEP 471
Cdd:PRK13537 87 QFDNLDpdftvrENLLVFGRYFGLSAAAARALVPPLL-EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190
....*....|....*....|....*....|.
gi 1525942895 472 TNHLDMKTKDIIKDALKDF---DGTLILVSH 499
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLlarGKTILLTTH 196
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
338-499 |
5.95e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.72 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 338 GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnaKIgyfaqnqaalldenltvfeTIDQIPL 417
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG-------RI-------------------LIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 418 TDgsIKIKDLLG--------AFMFSG----------DDTT--------KKVKV---------------------LSGGEK 450
Cdd:COG1132 405 RD--LTLESLRRqigvvpqdTFLFSGtirenirygrPDATdeeveeaaKAAQAhefiealpdgydtvvgergvnLSGGQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 451 TRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-203 |
6.18e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.04 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPqhlltqdkvtvfe 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 etmkafeevtQMQKELDELNEQLTIRTdyetddymklieRVSELsEKFYSIEETNYDAEVEKVLK--GL-GFERKDFtrq 160
Cdd:cd03231 70 ----------SIARGLLYLGHAPGIKT------------TLSVL-ENLRFWHADHSDEQVEEALArvGLnGFEDRPV--- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 161 tSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLE 203
Cdd:cd03231 124 -AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
7.09e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPttgnVTGPKEAVIAYLP-QHLLTQDKVt 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIEL----YPEARVSGEVYLDgQDIFKMDVI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 vfeETMKAFEEVTQMQKELDEL----NEQLTIRTDYETDDYMKLIERVSELSEKFYSIEETnydaevekvlkglgfeRKD 156
Cdd:PRK14247 79 ---ELRRRVQMVFQIPNPIPNLsifeNVALGLKLNRLVKSKKELQERVRWALEKAQLWDEV----------------KDR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 157 FTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK--AVMVISH 218
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
328-499 |
7.40e-10 |
|
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: 59.41 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTY---GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGH--NAKIGYFAQNQAA 400
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqvLLDGKpiSQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 401 LLDENLTVF--ETIDQIP--LTDGSI-KIKDLLGAF--------MFSGDDTT--KKVKVLSGGEKTRLAMIKLLLEPVNV 465
Cdd:cd03248 92 LVGQEPVLFarSLQDNIAygLQSCSFeCVKEAAQKAhahsfiseLASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1525942895 466 LILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
330-476 |
7.58e-10 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 58.74 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGeKVAFVGKNGEGKSTMIKAI------------MNEIDFeGGLKVGHNAKIGYFAQN 397
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILatltppssgtirIDGQDV-LKQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 qaALLDENLTVFETID------QIPLTDGSIKIKDLLGAFMFsGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEP 471
Cdd:cd03264 81 --FGVYPNFTVREFLDyiawlkGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
....*
gi 1525942895 472 TNHLD 476
Cdd:cd03264 158 TAGLD 162
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-218 |
8.94e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 59.17 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT--LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHL------ 73
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 LTQDKV----TVFEETMKAFEEVTQMQkeldelneqltirtdyetddymklIERVSELSEKFYSIEET--NYDAEVEkvl 147
Cdd:cd03251 81 VSQDVFlfndTVAENIAYGRPGATREE------------------------VEEAARAANAHEFIMELpeGYDTVIG--- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 148 kglgfERKdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES---IQ-WLEDFLINsaKAVMVISH 218
Cdd:cd03251 134 -----ERG------VKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlVQaALERLMKN--RTTFVIAH 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-476 |
9.07e-10 |
|
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: 58.82 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDfEGGLKVGH---NAK----------IGYFAQNQAALldENLTV 408
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSGQilfNGQprkpdqfqkcVAYVRQDDILL--PGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 409 FETI---DQIPLTD-GSIKIKDLLGAFMFSGD--DTT---KKVKVLSGGEKTRLAM-IKLLLEPVnVLILDEPTNHLD 476
Cdd:cd03234 99 RETLtytAILRLPRkSSDAIRKKRVEDVLLRDlaLTRiggNLVKGISGGERRRVSIaVQLLWDPK-VLILDEPTSGLD 175
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
328-499 |
9.87e-10 |
|
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: 58.53 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKA----SMVIERGEKVAFVGKNGEGKSTMIKAIMN---------EIDfegGLKVGHN-----A 389
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAvdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllepdagfaTVD---GFDVVKEpaearR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 390 KIGYFAQNQAalLDENLTVFETIDQIPLTDG------SIKIKDLLGAFMFsGDDTTKKVKVLSGGEKTRLAMIKLLLEPV 463
Cdd:cd03266 79 RLGFVSDSTG--LYDRLTARENLEYFAGLYGlkgdelTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1525942895 464 NVLILDEPTNHLDMKTKDIIKD---ALKDFDGTLILVSH 499
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREfirQLRALGKCILFSTH 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-238 |
1.02e-09 |
|
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: 60.13 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFGGTTLfsDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaYLPQHLLTQDKVTVFEET 85
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI---------VLNGRTLFDSRKGIFLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 86 MK-----AFEEVTqmqkeldeLNEQLTIRTDYEtddYMKLIERVSELSEKFysieetnydaevEKVLKGLGFERKdFTRQ 160
Cdd:TIGR02142 73 EKrrigyVFQEAR--------LFPHLSVRGNLR---YGMKRARPSERRISF------------ERVIELLGIGHL-LGRL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMG 236
Cdd:TIGR02142 129 PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
..
gi 1525942895 237 RI 238
Cdd:TIGR02142 209 RV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
330-499 |
1.10e-09 |
|
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: 58.75 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKA----SMVIERGEKVAFVGKNGEGKSTMIKAI-MNEIDFEGGLKV-GHN-------------AK 390
Cdd:cd03258 4 LKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERPTSGSVLVdGTDltllsgkelrkarRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 391 IGYFAQNQAALldENLTVFET------IDQIPLTDGSIKIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIK-LLLEPv 463
Cdd:cd03258 84 IGMIFQHFNLL--SSRTVFENvalpleIAGVPKAEIEERVLELL-ELVGLEDKADAYPAQLSGGQKQRVGIARaLANNP- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1525942895 464 NVLILDEPTNHLDMKTKDIIKDALKD----FDGTLILVSH 499
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITH 199
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-218 |
1.12e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.93 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIAdvakpttGNvtgpkeaviaylPQHLLTQDKVTvFE 83
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM-------GH------------PKYEVTSGSIL-LD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 EtmkafEEVTQMqkELDE-------LNEQ-------LTIRtdyetdDYMKLIerVSELSEKFYSIEEtnYDAEVEKVLKG 149
Cdd:COG0396 63 G-----EDILEL--SPDEraragifLAFQypveipgVSVS------NFLRTA--LNARRGEELSARE--FLKLLKEKMKE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 150 LGFERKDFTRQTSE-FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDF---LINSAKAVMVISH 218
Cdd:COG0396 126 LGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGvnkLRSPDRGILIITH 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
318-502 |
1.15e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.23 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 318 PPSPRSGQYPVM-VEELTKTY-GDHVVfQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-EIDFEG-----GLKVGH-- 387
Cdd:PRK11607 9 QAKTRKALTPLLeIRNLTKSFdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGqimldGVDLSHvp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 388 --NAKIGYFAQNQAalLDENLTVFETI------DQIPLTDGSIKIKDLLGaFMFSGDDTTKKVKVLSGGEKTRLAMIKLL 459
Cdd:PRK11607 88 pyQRPINMMFQSYA--LFPHMTVEQNIafglkqDKLPKAEIASRVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIK----DALKDFDGTLILVSHDRD 502
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQE 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-238 |
1.29e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.99 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqhlltqdKVT 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG---------------------TIR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMQKELDELNEQLT-IRTDYETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDfTR 159
Cdd:PRK11264 62 VGDITIDTARSLSQQKGLIRQLRQHVGfVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE-TS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE-------SIQWLEDflinsAKAVMVI-SHDRAFVDNITNRTI 231
Cdd:PRK11264 141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgevlnTIRQLAQ-----EKRTMVIvTHEMSFARDVADRAI 215
|
....*..
gi 1525942895 232 EVTMGRI 238
Cdd:PRK11264 216 FMDQGRI 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-218 |
1.33e-09 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 58.39 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgPKEAVIAYLPQHLLTQDKVT 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL-IDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMkAFEevtqmqkelDELNEQLTIRTDYETDdymkliERVSELSekfysiEETNYDAEVEKVLKGLGFERKDftrQ 160
Cdd:cd03254 82 VLQDTF-LFS---------GTIMENIRLGRPNATD------EEVIEAA------KEAGAHDFIMKLPNGYDTVLGE---N 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAVMVISH 218
Cdd:cd03254 137 GGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-233 |
1.37e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--------GPKEAVIAYLPQH 72
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 lltqdkvtvfEETMKAF----EEVTQMQKEldelneqltirtdyetdDYMKLIERVSELSEKFysieetnYDAEVEKVlk 148
Cdd:PRK15056 87 ----------EEVDWSFpvlvEDVVMMGRY-----------------GHMGWLRRAKKRDRQI-------VTAALARV-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 glgfERKDFT-RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDfLINSAKAVMVISHDRAFV 223
Cdd:PRK15056 131 ----DMVEFRhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTeariISLLRE-LRDEGKTMLVSTHNLGSV 205
|
250
....*....|
gi 1525942895 224 DNITNRTIEV 233
Cdd:PRK15056 206 TEFCDYTVMV 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
330-500 |
1.41e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.94 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI-------MNEIDFEGgLKVgHNAKIGYFAQNQAALL 402
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrllppdSGEVLVDG-LDV-ATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 403 DEN-----LTV-----F-------------------ETIDQIPLTDgsikikdLLGAFMfsgdDTtkkvkvLSGGEKTR- 452
Cdd:COG4604 82 QENhinsrLTVrelvaFgrfpyskgrltaedreiidEAIAYLDLED-------LADRYL----DE------LSGGQRQRa 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 453 -LAMIklLLEPVNVLILDEPTNHLDMK----TKDIIKDALKDFDGTLILVSHD 500
Cdd:COG4604 145 fIAMV--LAQDTDYVLLDEPLNNLDMKhsvqMMKLLRRLADELGKTVVIVLHD 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
333-499 |
1.43e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 333 LTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM---------NEIDFEGG-LKVGH---NAKIGYFAQNQA 399
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSpLKASNirdTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 400 ALLDENLTVFETI---DQIPLTDG-------SIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILD 469
Cdd:TIGR02633 87 LTLVPELSVAENIflgNEITLPGGrmaynamYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 470 EPTNHLDMKTKDIIKDALKDFDG---TLILVSH 499
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAhgvACVYISH 199
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
445-505 |
1.57e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.00 E-value: 1.57e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 445 LSGGEKT------RLAMIKLLLEPVNVLILDEPTNHLD-----MKTKDIIKDALKDFDGTLILVSHDRDFLD 505
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIVITHDEELVD 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-218 |
1.64e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.22 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF--GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHL------ 73
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALrqaisv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 LTQdKVTVFEETmkafeevtqmqkeldeLNEQLTIRTDYETDDymKLIE---RVselsekfysieetnydaEVEKVLKG- 149
Cdd:PRK11160 419 VSQ-RVHLFSAT----------------LRDNLLLAAPNASDE--ALIEvlqQV-----------------GLEKLLEDd 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 150 ------LGferkDFTRQtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLINsaKAVMVISH 218
Cdd:PRK11160 463 kglnawLG----EGGRQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITH 532
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-218 |
2.03e-09 |
|
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: 56.78 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISV-SFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQH-LLTQdkV 79
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRpYLPL--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TvfeetmkafeevtqmqkeldeLNEQLTirtdYETDDymkliervselsekfysieetnydaevekvlkglgferkdftr 159
Cdd:cd03223 79 T---------------------LREQLI----YPWDD------------------------------------------- 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 160 qtsEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES----IQWLEDFLInsakAVMVISH 218
Cdd:cd03223 91 ---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESedrlYQLLKELGI----TVISVGH 146
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-500 |
2.10e-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: 60.08 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGG----TTLFSDVTFSINENDKIALMGKNGAGKS----TILKIIADVAKPTTGNvtgpkeavIAYLPQH 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGS--------ILFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQDKVT-----------VFEETMKAfeevtqmqkeldeLNEQLTI-RTDYETddyMKLIERVSELSEKfysieetnyd 140
Cdd:COG4172 78 LLGLSERElrrirgnriamIFQEPMTS-------------LNPLHTIgKQIAEV---LRLHRGLSGAAAR---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 141 AEVEKVLKGLGF---ERKdFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQW--LEdfLINSAK---- 211
Cdd:COG4172 132 ARALELLERVGIpdpERR-LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqiLD--LLKDLQrelg 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 212 -AVMVISHDRAFVDNITNRTIEVTMGRIydykakyshylqlradrrihqlkayEEQqrfiADNQEFIDRFRGTYSKTLqv 290
Cdd:COG4172 208 mALLLITHDLGVVRRFADRVAVMRQGEI-------------------------VEQ----GPTAELFAAPQHPYTRKL-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 291 qsrvkmLEKLEVIEIDEVDTSA--------LRLKFPpSPRSGqypvmveeLTKTYGDHVVFQKASMVIERGEKVAFVGKN 362
Cdd:COG4172 257 ------LAAEPRGDPRPVPPDApplleardLKVWFP-IKRGL--------FRRTVGHVKAVDGVSLTLRRGETLGLVGES 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 363 GEGKSTMIKAIMNEIDFEGGLKV-GHNakIGyfAQNQAAL-----------------LDENLTVFETID------QIPLT 418
Cdd:COG4172 322 GSGKSTLGLALLRLIPSEGEIRFdGQD--LD--GLSRRALrplrrrmqvvfqdpfgsLSPRMTVGQIIAeglrvhGPGLS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 419 DGSI--KIKDLLGAFMFSGDDTTKKVKVLSGGEKTRL----AMIkllLEPvNVLILDEPTNHLDMKT-KDIIkDALKD-- 489
Cdd:COG4172 398 AAERraRVAEALEEVGLDPAARHRYPHEFSGGQRQRIaiarALI---LEP-KLLVLDEPTSALDVSVqAQIL-DLLRDlq 472
|
570
....*....|...
gi 1525942895 490 --FDGTLILVSHD 500
Cdd:COG4172 473 reHGLAYLFISHD 485
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-238 |
2.46e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaYLPQHLLTQDKVTvfe 83
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRDGQLRDLYA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 etmkafeevtqmqkeLDELNEQLTIRTDY---ETDDYMKLIERVS---ELSEKFYSIEETNYDAEVEKVLKGLGFERKDF 157
Cdd:PRK11701 78 ---------------LSEAERRRLLRTEWgfvHQHPRDGLRMQVSaggNIGERLMAVGARHYGDIRATAGDWLERVEIDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 158 TR---QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQW-LEDFLINSAK----AVMVISHDRAFVDNITNR 229
Cdd:PRK11701 143 ARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQArLLDLLRGLVRelglAVVIVTHDLAVARLLAHR 221
|
....*....
gi 1525942895 230 TIEVTMGRI 238
Cdd:PRK11701 222 LLVMKQGRV 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-219 |
2.47e-09 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 58.08 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV-----------IAYL 69
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpvelrrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQ------HLLTQDKVTVfeetmkafeeVTQMQKELDElneqltirtdyetddymKLIERVSELsekfysieetnydaev 143
Cdd:cd03295 81 IQqiglfpHMTVEENIAL----------VPKLLKWPKE-----------------KIRERADEL---------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 144 ekvLKGLGFERKDFT-RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD-IESIQWLEDFL-INSA--KAVMVISH 218
Cdd:cd03295 118 ---LALVGLDPAEFAdRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpITRDQLQEEFKrLQQElgKTIVFVTH 194
|
.
gi 1525942895 219 D 219
Cdd:cd03295 195 D 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-253 |
2.55e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 59.73 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTL--FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHL------ 73
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLrrqval 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 LTQDkVTVFEETMkaFEEVTqmqkeldelneqltirtdY-ETDDY-MKLIERVselsekfysIEETNYDAEVEKVLKGLG 151
Cdd:TIGR02203 411 VSQD-VVLFNDTI--ANNIA------------------YgRTEQAdRAEIERA---------LAAAYAQDFVDKLPLGLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 FERKDftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAVMVISHDRAFVDNiTNR 229
Cdd:TIGR02203 461 TPIGE---NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALerLMQGRTTLVIAHRLSTIEK-ADR 536
|
250 260 270
....*....|....*....|....*....|
gi 1525942895 230 TIEVTMGRIY------DYKAKYSHYLQLRA 253
Cdd:TIGR02203 537 IVVMDDGRIVergthnELLARNGLYAQLHN 566
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-500 |
3.46e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIdfEGGLKVghNAKIGYFAQN-------- 397
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNEL--ESEVRV--EGRVEFFNQNiyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 -----QAALL--DENLTVFETIDQIP----------------LTDGSIKIKDLLgafmfsgDDTTKKVKV----LSGGEK 450
Cdd:PRK14258 84 nrlrrQVSMVhpKPNLFPMSVYDNVAygvkivgwrpkleiddIVESALKDADLW-------DEIKHKIHKsaldLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 451 TRLAMIKLLLEPVNVLILDEPTNHLD----MKTKDIIKDALKDFDGTLILVSHD 500
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
344-505 |
3.64e-09 |
|
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: 56.18 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 344 QKASMVIERGEKVAFVGKNGEGKSTMIkaimneidFEGGLKVGHNAKIGYFAQNqaallDENLTVFetIDQIpltdgSIK 423
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV--------NEGLYASGKARLISFLPKF-----SRNKLIF--IDQL-----QFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 424 IKDLLGaFMFSGddttKKVKVLSGGEKTRLAMIK-LLLEPVNVL-ILDEPTNHLDMKTKDIIKDALK---DFDGTLILVS 498
Cdd:cd03238 72 IDVGLG-YLTLG----QKLSTLSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIE 146
|
....*..
gi 1525942895 499 HDRDFLD 505
Cdd:cd03238 147 HNLDVLS 153
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
333-520 |
4.13e-09 |
|
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: 58.58 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 333 LTKTYGDHVVfqKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------------NEIDFEGGLKV---GHNAKIGYFAQ 396
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAgltrpdegeivlnGRTLFDSRKGIflpPEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 nQAAL-----LDENLTVFETIDQIPLTDGSI-KIKDLLGAfmfsGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDE 470
Cdd:TIGR02142 83 -EARLfphlsVRGNLRYGMKRARPSERRISFeRVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 471 PTNHLDMKTKDIIKDALK----DFDGTLILVSHDRDFLDGLVQKVFEFGNKRVR 520
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLErlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-238 |
4.18e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIAdvAKP----TTGNVTGPKEAVIAYLPQHlltQ 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEE---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DKVTVFeetmKAFeevtQMQKELDELNEQLTIRTDYETDDYMKLIERVSELSekFYSIeetnydaeVEKVLKGLGFERKD 156
Cdd:CHL00131 82 AHLGIF----LAF----QYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLE--FLEI--------INEKLKLVGMDPSF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 157 FTRQTSE-FSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLE---DFLINSAKAVMVISHDRAFVDNITNRTIE 232
Cdd:CHL00131 144 LSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYIKPDYVH 223
|
....*..
gi 1525942895 233 VTM-GRI 238
Cdd:CHL00131 224 VMQnGKI 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
276-513 |
5.00e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.67 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 276 FIDRFR--GTYSKTLQvqsRVKMLEklEVIE-IDEVDTSALRLKFPPSPRsgqypVMVEELT-KTYGDHVVFQKASMVIE 351
Cdd:COG4178 318 FVDNYQslAEWRATVD---RLAGFE--EALEaADALPEAASRIETSEDGA-----LALEDLTlRTPDGRPLLEDLSLSLK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 352 RGEKVAFVGKNGEGKSTMIKAImneidfeGGL------KVGH--NAKIGYFAQnQAALLDENLtvfetIDQI--PLTDGS 421
Cdd:COG4178 388 PGERLLITGPSGSGKSTLLRAI-------AGLwpygsgRIARpaGARVLFLPQ-RPYLPLGTL-----REALlyPATAEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 422 IKIKDL--------LGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKD--FD 491
Cdd:COG4178 455 FSDAELrealeavgLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPG 534
|
250 260
....*....|....*....|..
gi 1525942895 492 GTLILVSHdRDFLDGLVQKVFE 513
Cdd:COG4178 535 TTVISVGH-RSTLAAFHDRVLE 555
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-219 |
5.03e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.02 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAylPqhllTQDKVT 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--P----GAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEEtmkafEEVTQMQKELDELNEQLTIRtdyetddymkliervselsekfySIEETNYDAEVEKVLKGLGFERKDfTRQ 160
Cdd:PRK11248 75 VFQN-----EGLLPWRNVQDNVAFGLQLA-----------------------GVEKMQRLEIAHQMLKKVGLEGAE-KRY 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI----NSAKAVMVISHD 219
Cdd:PRK11248 126 IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-227 |
5.99e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADV--------------AKPTTGNVTGPKEAVI 66
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgeiywsgSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 67 AYLPQHLLTQDKVTVFEETMkafeevtqmqkeldeLNEQLTIRTDYETDDYMKLiervselsekfysieetnydaEVEKV 146
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIF---------------LGNEITLPGGRMAYNAMYL---------------------RAKNL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 147 LKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAK----AVMVISHD--- 219
Cdd:TIGR02633 125 LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLD-IIRDLKahgvACVYISHKlne 203
|
....*....
gi 1525942895 220 -RAFVDNIT 227
Cdd:TIGR02633 204 vKAVCDTIC 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
331-500 |
6.00e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 331 EELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKA---IMNEID---FEGGLKVGHNA------KIGYFAQNq 398
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTlsrLMTPAHghvWLDGEHIQHYAskevarRIGLLAQN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 aALLDENLTVFETI------DQIPLTDGSIKIKDLLGAFMFSGDDT---TKKVKVLSGGEKTRLAMIKLLLEPVNVLILD 469
Cdd:PRK10253 90 -ATTPGDITVQELVargrypHQPLFTRWRKEDEEAVTKAMQATGIThlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1525942895 470 EPTNHLDMKTKDIIKDALKDFDG----TLILVSHD 500
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
330-510 |
6.06e-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: 58.66 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIDFEGGLKVGHNA---KIGY-----FAQNQA 399
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVAlceKCGYverpsKVGEPC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 400 ALLDENLTVFEtIDQIPLTDGSIKIKDLLGAFMFS------GDDTT--------------------------KKVKV--- 444
Cdd:TIGR03269 83 PVCGGTLEPEE-VDFWNLSDKLRRRIRKRIAIMLQrtfalyGDDTVldnvlealeeigyegkeavgravdliEMVQLshr 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 445 -------LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDAL----KDFDGTLILVSHDRDFLDGLVQK 510
Cdd:TIGR03269 162 ithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDLSDK 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-238 |
6.16e-09 |
|
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: 56.35 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINEndKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPqhllTQDKVT- 80
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGE--ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP----ADRPVSm 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEEtmkafeevtqmqkelDELNEQLTIRTDYETDDYMKLieRVSELSEKfysieetnydaEVEKVLKGLGFERKDfTRQ 160
Cdd:cd03298 75 LFQE---------------NNLFAHLTVEQNVGLGLSPGL--KLTAEDRQ-----------AIEVALARVGLAGLE-KRL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK----AVMVISHDRAFVDNITNRTIEVTMG 236
Cdd:cd03298 126 PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
..
gi 1525942895 237 RI 238
Cdd:cd03298 206 RI 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
350-505 |
6.28e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.70 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKVghN-------------AKIGYFAQNQ---AALLDENLTvfetID 413
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKI--NgielreldpeswrKHLSWVGQNPqlpHGTLRDNVL----LG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 414 QIPLTDGSI-------KIKDLLGAfMFSGDDTTKKVKV--LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIK 484
Cdd:PRK11174 447 NPDASDEQLqqalenaWVSEFLPL-LPQGLDTPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180
....*....|....*....|...
gi 1525942895 485 DALKD--FDGTLILVSHDRDFLD 505
Cdd:PRK11174 526 QALNAasRRQTTLMVTHQLEDLA 548
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-218 |
6.30e-09 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 9 VSFG---GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT----GPKEAVIAYLPQHL--LTQDKV 79
Cdd:cd03253 6 VTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqDIREVTLDSLRRAIgvVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tVFEETMKAfeevtqmqkeldelneqlTIR--TDYETDDYMKLIERVSELSEKFYSIEEtNYDAEV-EKVLKglgferkd 156
Cdd:cd03253 86 -LFNDTIGY------------------NIRygRPDATDEEVIEAAKAAQIHDKIMRFPD-GYDTIVgERGLK-------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 157 ftrqtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSA--KAVMVISH 218
Cdd:cd03253 138 -------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSkgRTTIVIAH 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-218 |
7.72e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 16 LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT-----GPKEAVIAYLPQHL--LTQDKVtVFEETMK- 87
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshNLKDINLKWWRSKIgvVSQDPL-LFSNSIKn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 88 -------AFEEVTQMQKELDELNEQLTIRTDYETDDYMKLIERVSELSEKFYSIE--------ETNYDAEVEKVLKGLGF 152
Cdd:PTZ00265 479 nikyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNEliemrknyQTIKDSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 153 ErkDFT------------RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESiQWLEDFLINSAKA-----VMV 215
Cdd:PTZ00265 559 H--DFVsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQKTINNLKGnenriTII 635
|
...
gi 1525942895 216 ISH 218
Cdd:PTZ00265 636 IAH 638
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
7.76e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT-----LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNvtgpkeavIAYLPQHLLTQ 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT--------IEWIFKDEKNK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DKVTVFEETMKAFEEVTQMQKELDELNE-QLTIRTDYETDDYmKLIERVSELSEKF----YSIEETNYDAEVEKVLKGLG 151
Cdd:PRK13651 75 KKTKEKEKVLEKLVIQKTRFKKIKKIKEiRRRVGVVFQFAEY-QLFEQTIEKDIIFgpvsMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 FERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE-SIQWLEDF--LINSAKAVMVISHDrafVDNI-- 226
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFdnLNKQGKTIILVTHD---LDNVle 230
|
250
....*....|...
gi 1525942895 227 -TNRTIEVTMGRI 238
Cdd:PRK13651 231 wTKRTIFFKDGKI 243
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-238 |
9.34e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.05 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--GpkeaviaylpqhlltQDKVTVFEETMKAFEEVTQM- 95
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdG---------------QDITGLSGRELRPLRRRMQMv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 96 -QKELDELNEQLTIRTdyetddymkLIE---RVSELSEKfysieeTNYDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMR 171
Cdd:COG4608 101 fQDPYASLNPRMTVGD---------IIAeplRIHGLASK------AERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 172 IELAKILLKKPDLILLDEPTNHMDIeSIQ-----WLEDF-----LinsakAVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDV-SIQaqvlnLLEDLqdelgL-----TYLFISHDLSVVRHISDRVAVMYLGKI 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
321-499 |
9.81e-09 |
|
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: 58.38 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 321 PRSGQypVMVEELTKTY--GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLK---VGHNA------ 389
Cdd:TIGR01271 1213 PSGGQ--MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQidgVSWNSvtlqtw 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 390 ---------KI----GYFAQN---QAALLDENLtvFETIDQIPLTDGSIKIKDLLGAFMFSGDdttkkvKVLSGGEKTRL 453
Cdd:TIGR01271 1291 rkafgvipqKVfifsGTFRKNldpYEQWSDEEI--WKVAEEVGLKSVIEQFPDKLDFVLVDGG------YVLSNGHKQLM 1362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1525942895 454 AMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEH 1410
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-59 |
1.15e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.25 E-value: 1.15e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 1 MINVNNISVSFG-GT----TLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT 59
Cdd:COG1101 1 MLELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
328-499 |
1.33e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTY--GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHNAKIGYFA--QNQAAL 401
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGeiLLDGHDLRDYTLAslRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 402 LDENLTVF-ETI--------------DQIpltdgsIKIKDLLGAFMF-----SGDDTT--KKVKVLSGGEKTRLAMIKLL 459
Cdd:PRK11176 422 VSQNVHLFnDTIanniayarteqysrEQI------EEAARMAYAMDFinkmdNGLDTVigENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAH 537
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-58 |
1.34e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.15 E-value: 1.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLF--SDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV 58
Cdd:PRK13632 7 MIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI 66
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
325-498 |
1.38e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 325 QYPVMVEELTKTYGD-HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMneidfeGGLKVGHnAKIGYFAQNQAALLD 403
Cdd:PRK15056 4 QAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM------GFVRLAS-GKISILGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 ENLTVFetIDQIPLTDGS--IKIKD--LLGAFMFSG-------------DDTTKKVKV----------LSGGEKTRLAMI 456
Cdd:PRK15056 77 KNLVAY--VPQSEEVDWSfpVLVEDvvMMGRYGHMGwlrrakkrdrqivTAALARVDMvefrhrqigeLSGGQKKRVFLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1525942895 457 KLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVS 498
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdEGKTMLVS 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
349-507 |
1.58e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 349 VIERGEKVAFVGKNGEGKSTMIKAIMNEI-----DFEGglKVGHNAKIGYFAQNQ-----AALLDENLTVF---ETIDQI 415
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELipnlgDYEE--EPSWDEVLKRFRGTElqnyfKKLYNGEIKVVhkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 416 P-LTDGsiKIKDLL------GAFmfsgDDTTKK----------VKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLD-- 476
Cdd:PRK13409 173 PkVFKG--KVRELLkkvderGKL----DEVVERlglenildrdISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDir 246
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 477 --MKTKDIIKDALKdfDGTLILVSHDRDFLDGL 507
Cdd:PRK13409 247 qrLNVARLIRELAE--GKYVLVVEHDLAVLDYL 277
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
1.58e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 14 TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKpttgnvtGPKEAVIAYLPQHLLTQDKVTVfeetmkafeevt 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------GTPVAGCVDVPDNQFGREASLI------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 94 qmqkeldelnEQLTIRTDyeTDDYMKLIERVSeLSEKFYsieetnydaevekvlkglgferkdFTRQTSEFSGGWRMRIE 173
Cdd:COG2401 104 ----------DAIGRKGD--FKDAVELLNAVG-LSDAVL------------------------WLRRFKELSTGQKFRFR 146
|
170 180
....*....|....*....|..
gi 1525942895 174 LAKILLKKPDLILLDEPTNHMD 195
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLD 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-500 |
1.61e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYgdhVVFQKA------------------------SMVIERGEKVAFVGKNGEGKSTMIKaIMNEIDF--EGGL 383
Cdd:COG4586 4 VENLSKTY---RVYEKEpglkgalkglfrreyreveavddiSFTIEPGEIVGFIGPNGAGKSTTIK-MLTGILVptSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 384 KV-GHN---------AKIGY-FAQNQAALLD----ENLTVFETIDQIPLTDGSIKIKDL-----LGAFMfsgddtTKKVK 443
Cdd:COG4586 80 RVlGYVpfkrrkefaRRIGVvFGQRSQLWWDlpaiDSFRLLKAIYRIPDAEYKKRLDELvelldLGELL------DTPVR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 444 VLSGGEKTR--LAMIkLLLEPVnVLILDEPTNHLDMKTKDIIKDALKD----FDGTLILVSHD 500
Cdd:COG4586 154 QLSLGQRMRceLAAA-LLHRPK-ILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-239 |
1.80e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSinENDKIALMGKNGAGKSTILKIIADVAKPTTGNV-TGPKEaviaylpqhlltqdkvtvFEETMKAFEEVTQMQK 97
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlVGGKD------------------IETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 98 ELDELNEQLTIRtdyetdDYMKLIERVselseKFYSIEETNYdaEVEKVLKGLGFERKDfTRQTSEFSGGWRMRIELAKI 177
Cdd:TIGR01257 1010 QHNILFHHLTVA------EHILFYAQL-----KGRSWEEAQL--EMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIA 1075
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 178 LLKKPDLILLDEPTNHMDIESIQWLEDFLIN--SAKAVMVISHDRAFVDNITNRTIEVTMGRIY 239
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKyrSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-238 |
1.88e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.18 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--GPKEAVIAylPQHLLTQDKVTVFEETMkafeevtqmq 96
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdGHDLALAD--PAWLRRQVGVVLQENVL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 97 keldeLNEqlTIRTDYETDDYMKLIERVSELSE-----KFYSIEETNYDAEVEKvlKGLGFerkdftrqtsefSGGWRMR 171
Cdd:cd03252 88 -----FNR--SIRDNIALADPGMSMERVIEAAKlagahDFISELPEGYDTIVGE--QGAGL------------SGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 172 IELAKILLKKPDLILLDEPTNHMDIES----IQWLEDflINSAKAVMVISHDRAFVDNiTNRTIEVTMGRI 238
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESehaiMRNMHD--ICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-218 |
1.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.90 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 11 FGGTTLFsDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAylpqhlltqdkvtvfeetmkafe 90
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS----------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 91 evTQMQKELDELNEQLTIRTDY-ETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQTSEFSGGWR 169
Cdd:PRK13643 73 --TSKQKEIKPVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 170 MRIELAKILLKKPDLILLDEPTNHMD----IESIQWLEDfLINSAKAVMVISH 218
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVTH 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-236 |
2.03e-08 |
|
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: 55.16 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPqhlltqDKVTVFEETmkafeevtqmqke 98
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP------DRMVVFQNY------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 99 ldELNEQLTIRtdyetDDYMKLIERVselsekFYSIEETNYDAEVEKVLKGLGFERKDFTRQTsEFSGGWRMRIELAKIL 178
Cdd:TIGR01184 64 --SLLPWLTVR-----ENIALAVDRV------LPDLSKSERRAIVEEHIALVGLTEAADKRPG-QLSGGMKQRVAIARAL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 179 LKKPDLILLDEPTNHMDIESIQWLEDFLINSAK----AVMVISHDrafVDN---ITNRTIEVTMG 236
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRGNLQEELMQIWEehrvTVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-195 |
2.06e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgPKEAVIAYLPQHLLTQDKV 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-IKGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 T--VFEETmkafeevtqmqkeldelNEQLTIRTDYETDDYMKLIERVSElsekfysiEETnyDAEVEKVLKGL---GFER 154
Cdd:PRK13639 80 VgiVFQNP-----------------DDQLFAPTVEEDVAFGPLNLGLSK--------EEV--EKRVKEALKAVgmeGFEN 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525942895 155 KdftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK13639 133 K----PPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
330-505 |
2.07e-08 |
|
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: 54.46 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN---------EIDFEG----GLKVGHNAKIGYFAQ 396
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyevtegEILFKGeditDLPPEERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAALldenltvfetidQIPltdgSIKIKDLLgAFMFSGddttkkvkvLSGGEKTRLAMIKLL-LEPvNVLILDEPTNHL 475
Cdd:cd03217 83 FQYPP------------EIP----GVKNADFL-RYVNEG---------FSGGEKKRNEILQLLlLEP-DLAILDEPDSGL 135
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 476 DMKTKDIIKDA---LKDFDGTLILVSHDRDFLD 505
Cdd:cd03217 136 DIDALRLVAEVinkLREEGKSVLIITHYQRLLD 168
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
4-196 |
2.07e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSfggtTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAkPTTGNVTGPKEAVIAYLPQHL------LTQD 77
Cdd:COG4138 3 LNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELarhrayLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 78 KVTVFeeTMKAFEEVTQMQKelDELNEQLTIRTdyetddymklierVSELSEKfysieetnydaevekvlkgLGFERKdF 157
Cdd:COG4138 78 QSPPF--AMPVFQYLALHQP--AGASSEAVEQL-------------LAQLAEA-------------------LGLEDK-L 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 158 TRQTSEFSGG-WRmRIELAKILLK-----KPD--LILLDEPTNHMDI 196
Cdd:COG4138 121 SRPLTQLSGGeWQ-RVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDV 166
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
330-499 |
2.14e-08 |
|
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: 54.81 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDH--VVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKV--GHN-AKIGYFAqnqaalLDE 404
Cdd:cd03244 5 FKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidGVDiSKIGLHD------LRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 405 NLTVfetIDQIP-LTDGSI----------------------KIKDLLGAfMFSGDDTTKKV--KVLSGGEKTRLAMIKLL 459
Cdd:cd03244 79 RISI---IPQDPvLFSGTIrsnldpfgeysdeelwqalervGLKEFVES-LPGGLDTVVEEggENLSVGQRQLLCLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
328-499 |
2.24e-08 |
|
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: 54.93 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHV--VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDF-EGGLKV-GHN----------AKIGY 393
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIdGHDvrdytlaslrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 394 FAQNqAALLDEnlTVFETI---------DQIpltdgsIKIKDLLGAFMF-----SGDDTT---KKVKvLSGGEKTRLAMI 456
Cdd:cd03251 81 VSQD-VFLFND--TVAENIaygrpgatrEEV------EEAARAANAHEFimelpEGYDTVigeRGVK-LSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1525942895 457 KLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-221 |
2.30e-08 |
|
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: 56.68 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTT--LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV--------TGPKEA---VIAY 68
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQWDREElgrHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQHlltqdkVTVFEETMKA----FEEVTqmqkelDElneqltirtdyetddymKLIE-----RVSELSEKFysieETNY 139
Cdd:COG4618 411 LPQD------VELFDGTIAEniarFGDAD------PE-----------------KVVAaaklaGVHEMILRL----PDGY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 140 DAEVEKVLKGLgferkdftrqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA----VMV 215
Cdd:COG4618 458 DTRIGEGGARL--------------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA-AIRALKArgatVVV 522
|
....*.
gi 1525942895 216 ISHDRA 221
Cdd:COG4618 523 ITHRPS 528
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
330-499 |
2.37e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------NEIDFEG------GLKVGHNAKIG---- 392
Cdd:COG3845 8 LRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYglyqpdsGEILIDGkpvrirSPRDAIALGIGmvhq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 393 YFaqnqaaLLDENLTVFETI---------DQIPLTDGSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPV 463
Cdd:COG3845 88 HF------MLVPNLTVAENIvlgleptkgGRLDRKAARARIRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 464 NVLILDEPTNHLdmkT-------KDIIKdALKDFDGTLILVSH 499
Cdd:COG3845 161 RILILDEPTAVL---TpqeadelFEILR-RLAAEGKSIIFITH 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-219 |
2.40e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpKEAVIAYLPQHLLTQDKVT 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKAFEEVTQMqkeldelnEQLTIrtdYETDDYMKLIERVSELSEKFYSIEETnydaevekvLKGLGFERKDFTR- 159
Cdd:PRK14246 88 LRKEVGMVFQQPNPF--------PHLSI---YDNIAYPLKSHGIKEKREIKKIVEEC---------LRKVGLWKEVYDRl 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 160 --QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK--AVMVISHD 219
Cdd:PRK14246 148 nsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
326-503 |
2.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 326 YPVMVEELTKTYGDHV-VFQKASMVIERGEKVAFVGKNGEGKSTMIKAiMNEIDF--EGGLKVGH---NAKIGYFAQNQA 399
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLH-LNGIYLpqRGRVKVMGrevNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 400 ALL----DENL---TVFETIDQIPLTDG------SIKIKDLLGAF-MFSGDDttKKVKVLSGGEKTRLAMIKLLLEPVNV 465
Cdd:PRK13647 82 GLVfqdpDDQVfssTVWDDVAFGPVNMGldkdevERRVEEALKAVrMWDFRD--KPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525942895 466 LILDEPTNHLDMKTKDIIKDALKDFDG---TLILVSHDRDF 503
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDL 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
330-499 |
2.80e-08 |
|
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: 53.90 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGG-------------LKVGHNA 389
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgEVRWNGTplaeqrdepheniLYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 390 KIG---YFAQN----QAALLDENLTVFETIDQIPLTDgsikIKDLLGAFmfsgddttkkvkvLSGGEKTRLAMIKLLLEP 462
Cdd:TIGR01189 83 GLKpelSALENlhfwAAIHGGAQRTIEDALAAVGLTG----FEDLPAAQ-------------LSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1525942895 463 VNVLILDEPTNHLDMKTKDIIKDALKDF---DGTLILVSH 499
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
327-502 |
2.84e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 327 PVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKVG----HNAKIGYFAQNQAAL 401
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtVLVAgddvEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 402 LDENLTVFE-TIDQI-------------PLTDGSIKI----KDLLGAFMFSGDDTTKkvkvLSGGEKTRLAMIKLLLEPV 463
Cdd:PRK09536 83 PQDTSLSFEfDVRQVvemgrtphrsrfdTWTETDRAAveraMERTGVAQFADRPVTS----LSGGERQRVLLARALAQAT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1525942895 464 NVLILDEPTNHLDM----KTKDIIKDaLKDFDGTLILVSHDRD 502
Cdd:PRK09536 159 PVLLLDEPTASLDInhqvRTLELVRR-LVDDGKTAVAAIHDLD 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-237 |
2.96e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG-------NVTGPKEAViaylpQHLLTQDKVTVFEEtmkAFEE 91
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGelyyqgqDLLKADPEA-----QKLLRQKIQIVFQN---PYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 92 VTQMQKELDELNEQLTIRTDyetddyMKLIERVselsekfysieetnydAEVEKVLKGLGFERKDFTRQTSEFSGGWRMR 171
Cdd:PRK11308 105 LNPRKKVGQILEEPLLINTS------LSAAERR----------------EKALAMMAKVGLRPEHYDRYPHMFSGGQRQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 172 IELAKILLKKPDLILLDEPTNHMDIeSIQ-----WLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGR 237
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDV-SVQaqvlnLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-195 |
3.01e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHlltQDKVTVFEEt 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ---RDICMVFQS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 86 mkafeevtqmqkeldelneqltirtdYETDDYMKLIERVsELSEKFYSIEETNYDAEVEKVLKGL---GFErkdfTRQTS 162
Cdd:PRK11432 87 --------------------------YALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVdlaGFE----DRYVD 135
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 163 EFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK11432 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
301-504 |
3.72e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 301 EVIEIDEVdtsALRLKFPPSPRSGQYPVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaIMNEIDF- 379
Cdd:COG1134 3 SMIEVENV---SKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLK-LIAGILEp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 380 -EGGLKVghNAKIgyfaqnqAALLD------------EN---------LTVFETIDQIPltdgsiKIKDL--LGAFMfsg 435
Cdd:COG1134 79 tSGRVEV--NGRV-------SALLElgagfhpeltgrENiylngrllgLSRKEIDEKFD------EIVEFaeLGDFI--- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 436 dDTtkKVKVLSGGEKTRLAM-IKLLLEPvNVLILDEPTNHLDM----KTKDIIKDALKDfDGTLILVSHDRDFL 504
Cdd:COG1134 141 -DQ--PVKTYSSGMRARLAFaVATAVDP-DILLVDEVLAVGDAafqkKCLARIRELRES-GRTVIFVSHSMGAV 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
328-503 |
3.80e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI-MNEIDFEGGLKVGH---------NAKIGYFAQN 397
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInFLEKPSEGSIVVNGqtinlvrdkDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAALLDENL-------------TVFETIDQIPL-------TDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIK 457
Cdd:PRK10619 86 QLRLLRTRLtmvfqhfnlwshmTVLENVMEAPIqvlglskQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525942895 458 -LLLEPvNVLILDEPTNHLDMKTKD---IIKDALKDFDGTLILVSHDRDF 503
Cdd:PRK10619 166 aLAMEP-EVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMGF 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-244 |
4.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.74 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 13 GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLltQDKV-TVFEE------T 85
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV--RSKVgLVFQDpddqvfS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 86 MKAFEEVTqmqkeLDELNEQLtirtdyetddymklieRVSELSEKfysieetnydaeVEKVLKGLGFerKDFT-RQTSEF 164
Cdd:PRK13647 95 STVWDDVA-----FGPVNMGL----------------DKDEVERR------------VEEALKAVRM--WDFRdKPPYHL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 165 SGGWRMRIELAKILLKKPDLILLDEPTNHMD---IESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIYDY 241
Cdd:PRK13647 140 SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
...
gi 1525942895 242 KAK 244
Cdd:PRK13647 220 GDK 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
347-519 |
4.05e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 53.65 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMN-EIDFEGGLKVGhnaKIGYFAQNQAA-----LLDEN-----LTVFETID-- 413
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLIN---GVDVTAAPPADrpvsmLFQENnlfahLTVEQNVGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 414 ---QIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF 490
Cdd:cd03298 95 lspGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 491 ----DGTLILVSHDRDFLDGLVQKVFEFGNKRV 519
Cdd:cd03298 175 haetKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
327-500 |
4.09e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 327 PVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-EIDFEGGLKVGhNAKIGYfAQNQAALL--D 403
Cdd:PRK11247 12 PLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAGELLAG-TAPLAE-AREDTRLMfqD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 ENLTVFET-IDQIPL-TDGSIKiKDLLGAFMFSG--DDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKT 479
Cdd:PRK11247 90 ARLLPWKKvIDNVGLgLKGQWR-DAALQALAAVGlaDRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180
....*....|....*....|....*
gi 1525942895 480 K----DIIKDALKDFDGTLILVSHD 500
Cdd:PRK11247 169 RiemqDLIESLWQQHGFTVLLVTHD 193
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
4.67e-08 |
|
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: 55.06 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTtGNVTGpkeaVIAYLPQHLLTQ 76
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP-GITSG----EILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DkvtvfEETMKAF--EEVtQM--QKELDELNEQLTIRtdyetddymkliERVSELSEKFYSIEETNYDAEVEKVLK--GL 150
Cdd:COG0444 76 S-----EKELRKIrgREI-QMifQDPMTSLNPVMTVG------------DQIAEPLRIHGGLSKAEARERAIELLErvGL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 151 GFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIeSIQW--LEdfLINSAK-----AVMVISHDRAFV 223
Cdd:COG0444 138 PDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLN--LLKDLQrelglAILFITHDLGVV 214
|
250
....*....|....*..
gi 1525942895 224 DNITNRTieVTM--GRI 238
Cdd:COG0444 215 AEIADRV--AVMyaGRI 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
342-486 |
4.88e-08 |
|
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: 54.48 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAKIGYFAQN------------------------ 397
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-KIKHSGRISFSSQFswimpgtikeniifgvsydeyryk 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 ---QAALLDENLTVFETIDQIPLTDGSIkikdllgafmfsgddttkkvkVLSGGEKTRLAMIKLLLEPVNVLILDEPTNH 474
Cdd:cd03291 131 svvKACQLEEDITKFPEKDNTVLGEGGI---------------------TLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170
....*....|..
gi 1525942895 475 LDMKTKDIIKDA 486
Cdd:cd03291 190 LDVFTEKEIFES 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
328-500 |
4.99e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.04 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNEIDfEGGLKVGHN-------AK--IGYFAQ 396
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagLEDIT-SGDLFIGEKrmndvppAErgVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAalLDENLTVFETIdqipltdgSIKIKdLLGAfmfSGDDTTKKV-----------------KVLSGGEKTRLAMIKLL 459
Cdd:PRK11000 83 SYA--LYPHLSVAENM--------SFGLK-LAGA---KKEEINQRVnqvaevlqlahlldrkpKALSGGQRQRVAIGRTL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 460 LEPVNVLILDEPTNHLD------MKTKdiIKDALKDFDGTLILVSHD 500
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDaalrvqMRIE--ISRLHKRLGRTMIYVTHD 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
342-500 |
5.25e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.67 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTMIKAI-------MNEIDFEG--------GLKVG-HNAKIGYFAQNQAALLD-- 403
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLggldtptSGDVIFNGqpmsklssAAKAElRNQKLGFIYQFHHLLPDft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 --ENLTVFETIDQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD 481
Cdd:PRK11629 104 alENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|...
gi 1525942895 482 IIKDALKDFD---GTLIL-VSHD 500
Cdd:PRK11629 183 SIFQLLGELNrlqGTAFLvVTHD 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-200 |
5.35e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.62 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISV-SFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAkPTTGNVT--GP--KEAVIAYLPQHL--L 74
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKinGIelRELDPESWRKHLswV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKvTVFEETMKafEEVTQMQKELDElnEQLtirtdyetddyMKLIERvSELSEkFysieetnydaeVEKVLKGLGFER 154
Cdd:PRK11174 429 GQNP-QLPHGTLR--DNVLLGNPDASD--EQL-----------QQALEN-AWVSE-F-----------LPLLPQGLDTPI 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525942895 155 KDftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQ 200
Cdd:PRK11174 480 GD---QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-198 |
5.38e-08 |
|
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: 53.65 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF--GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaV----IAYLPQHLL- 74
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL-----IdgvdISKIGLHDLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 ------TQDkVTVFEETMKafeevtqmqKELDELNEQltirTDYETDDYMK---LIERVSELSEKFYSIEETNydaevek 145
Cdd:cd03244 78 srisiiPQD-PVLFSGTIR---------SNLDPFGEY----SDEELWQALErvgLKEFVESLPGGLDTVVEEG------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 146 vlkglgferkdftrqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES 198
Cdd:cd03244 137 ---------------GENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-240 |
5.48e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFS--DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeavIAYLPqhlLTQDKV 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYAlkDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT------VGGMV---LSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 --------TVFEETMKAFEEVTQMQKELDELNEQLTIRTDyetddymkLIERVselsekfysieetnyDAEVEKVlkglG 151
Cdd:PRK13635 77 wdvrrqvgMVFQNPDNQFVGATVQDDVAFGLENIGVPREE--------MVERV---------------DQALRQV----G 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 152 FErkDF-TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD-------IESIQWLEDfliNSAKAVMVISHD---R 220
Cdd:PRK13635 130 ME--DFlNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHDldeA 204
|
250 260
....*....|....*....|
gi 1525942895 221 AFVDnitnRTIEVTMGRIYD 240
Cdd:PRK13635 205 AQAD----RVIVMNKGEILE 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-203 |
6.74e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 5 NNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQH------LLTQDK 78
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarrigLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 VTVFEETMkafeevtqmqkeldelnEQLTIRTDYEtddYMKLIERVSELSEkfysieetnydAEVEKVLKGLGFerKDFT 158
Cdd:PRK10253 91 TTPGDITV-----------------QELVARGRYP---HQPLFTRWRKEDE-----------EAVTKAMQATGI--THLA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 159 RQTSE-FSGGWRMRIELAKILLKKPDLILLDEPTNHMDI-ESIQWLE 203
Cdd:PRK10253 138 DQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE 184
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-500 |
6.75e-08 |
|
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: 54.29 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTY--GDHVVfqKA----SMVIERGEKVAFVGKNGEGKSTMIKAIMN----------EIDFEGG--LKVGHNA-- 389
Cdd:COG0444 4 VRNLKVYFptRRGVV--KAvdgvSFDVRRGETLGLVGESGSGKSTLARAILGllpppgitsgEILFDGEdlLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 390 -----KIGYFAQNQAALLDENLTVFETIDQipltdgSIKIKDLLgafmfSGDDTTKKV-----KV--------------- 444
Cdd:COG0444 82 kirgrEIQMIFQDPMTSLNPVMTVGDQIAE------PLRIHGGL-----SKAEARERAielleRVglpdperrldryphe 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 445 LSGGEKTRlAMIK--LLLEPvNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:COG0444 151 LSGGMRQR-VMIAraLALEP-KLLIADEPTTALDVTIQaqilNLLKDLQRELGLAILFITHD 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-231 |
7.18e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaylpqHLLTQDkvt 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-------------LWQGEP--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 vfeetmkafeevtqMQKELDELNEQLT-------IRtdyetddymkliervSELS--E--KFYSIEETNYDAEV-----E 144
Cdd:PRK13538 65 --------------IRRQRDEYHQDLLylghqpgIK---------------TELTalEnlRFYQRLHGPGDDEAlwealA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 145 KVlkGL-GFErkDF-TRQtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKA---VMVISHD 219
Cdd:PRK13538 116 QV--GLaGFE--DVpVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQggmVILTTHQ 188
|
250
....*....|..
gi 1525942895 220 RAFVDNITNRTI 231
Cdd:PRK13538 189 DLPVASDKVRKL 200
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
330-505 |
8.73e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 53.42 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN---------EIDFEG----GLKVGHNAKIGYFAQ 396
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyevtsgTILFKGqdllELEPDERARAGLFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAALLDENLTVFETI-------------DQIPLTDGSIKIKDLLGAFMFSGDDTTKKVKV-LSGGEKTRLAMIKL-LLE 461
Cdd:TIGR01978 83 FQYPEEIPGVSNLEFLrsalnarrsargeEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMaLLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 462 PVnVLILDEPTNHLDMKTKDIIKD---ALKDFDGTLILVSHDRDFLD 505
Cdd:TIGR01978 163 PK-LAILDEIDSGLDIDALKIVAEginRLREPDRSFLIITHYQRLLN 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-59 |
8.95e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 8.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT 59
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE 69
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
330-495 |
9.86e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 52.93 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKST-------MIKAIMNEIDFEGG----LKVGHNAK--IGYFAQ 396
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTtfymivgLVKPDSGKILLDGQditkLPMHKRARlgIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 nQAALLdENLTVFETIDQI------PLTDGSIKIKDLLGAFmfsGDDTTKKVKV--LSGGEKTRLAMIK-LLLEPvNVLI 467
Cdd:cd03218 83 -EASIF-RKLTVEENILAVleirglSKKEREEKLEELLEEF---HITHLRKSKAssLSGGERRRVEIARaLATNP-KFLL 156
|
170 180 190
....*....|....*....|....*....|...
gi 1525942895 468 LDEPTNHLDMKT----KDIIKDaLKDFD-GTLI 495
Cdd:cd03218 157 LDEPFAGVDPIAvqdiQKIIKI-LKDRGiGVLI 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-502 |
9.91e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.63 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 339 DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN---------EIDfegGLKVGHNAK----------IGYFAQNQA 399
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllkpttgtvTVD---DITITHKTKdkyirpvrkrIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 400 ALLDENLTVFETID-----QIPLTDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNH 474
Cdd:PRK13646 96 SQLFEDTVEREIIFgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|..
gi 1525942895 475 LDMKTKDIIKDALKDF----DGTLILVSHDRD 502
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLqtdeNKTIILVSHDMN 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-259 |
1.09e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDK-- 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKrm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 VTVFEE-----TMKAFEEVTQMQKELDELNEQLtIRTDYetddYMKLiervselsekfysieetnydaevEKVlkGLgfe 153
Cdd:PRK11831 87 SMLFQSgalftDMNVFDNVAYPLREHTQLPAPL-LHSTV----MMKL-----------------------EAV--GL--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 154 RKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAV--MVISHDRAFVDNITNR 229
Cdd:PRK11831 134 RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIseLNSALGVtcVVVSHDVPEVLSIADH 213
|
250 260 270
....*....|....*....|....*....|
gi 1525942895 230 TIEVTMGRIYDYKAKYShyLQLRADRRIHQ 259
Cdd:PRK11831 214 AYIVADKKIVAHGSAQA--LQANPDPRVRQ 241
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
353-500 |
1.13e-07 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 53.28 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 353 GEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGGLKVGHNAKIgyfAQNQAALLDE------NLTVFETI--DQIPL 417
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGalrpdagTVDLAGVDLHGLSRRA---RARRVALVEQdsdtavPLTVRDVValGRIPH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 418 -------TDGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF 490
Cdd:TIGR03873 104 rslwagdSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVREL 183
|
170
....*....|...
gi 1525942895 491 DG---TLILVSHD 500
Cdd:TIGR03873 184 AAtgvTVVAALHD 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-520 |
1.16e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD--HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKVGH-----------NAKIGYFA 395
Cdd:PRK13635 8 VEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtITVGGmvlseetvwdvRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 396 QNQaalldENLTVFETID----------QIPLTDGSIKIKDLLG-----AFMfsgddtTKKVKVLSGGEKTRLAMIKLLL 460
Cdd:PRK13635 88 QNP-----DNQFVGATVQddvafgleniGVPREEMVERVDQALRqvgmeDFL------NREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 461 EPVNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHDRD----------------FLDGLVQKVFEFGNKRVR 520
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRrevlETVRQLKEQKGITVLSITHDLDeaaqadrvivmnkgeiLEEGTPEEIFKSGHMLQE 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
339-499 |
1.21e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 52.93 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 339 DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHNAK----------IGYfaqnqaalldenl 406
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeiLLDGVDIRdlnlrwlrsqIGL------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 407 tvfetIDQIP-LTDGSIKIKDLLGAFMFSGDDTTKKVKV------------------------LSGGEKTRLAMIKLLLE 461
Cdd:cd03249 82 -----VSQEPvLFDGTIAENIRYGKPDATDEEVEEAAKKanihdfimslpdgydtlvgergsqLSGGQKQRIAIARALLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1525942895 462 PVNVLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-195 |
1.27e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHlltQDKVTV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN---RHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEET-----MKAFEEVT---QMQKeldELNEQLTIRtdyeTDDYMKLIeRVSELSEkfysieetnydaevekvlkglgfe 153
Cdd:PRK09452 92 FQSYalfphMTVFENVAfglRMQK---TPAAEITPR----VMEALRMV-QLEEFAQ------------------------ 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 154 rkdftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK09452 140 -----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-197 |
1.27e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 5 NNISVSFGGTTL-FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT--GPKeavIAYLPQHLLTQDKVTV 81
Cdd:PRK13657 338 DDVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidGTD---IRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEETM---KAFEEVTQMQKElDELNEQLtiRTDYETDDYMKLIERvselsekfysiEETNYDAEVEkvlkglgfERKdft 158
Cdd:PRK13657 415 FQDAGlfnRSIEDNIRVGRP-DATDEEM--RAAAERAQAHDFIER-----------KPDGYDTVVG--------ERG--- 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 1525942895 159 rqtSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE 197
Cdd:PRK13657 470 ---RQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
349-505 |
1.45e-07 |
|
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: 54.02 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 349 VIERGEKVAFVGKNGEGKSTMIKAIMNEI-----DFEGglKVGHNAKIGYFAQNQ-----AALLDENLTVF---ETIDQI 415
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELkpnlgDYDE--EPSWDEVLKRFRGTElqdyfKKLANGEIKVAhkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 416 P-LTDGsiKIKDLL------GAFmfsgDDTTKK----------VKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLD-- 476
Cdd:COG1245 173 PkVFKG--TVRELLekvderGKL----DELAEKlglenildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiy 246
|
170 180 190
....*....|....*....|....*....|.
gi 1525942895 477 --MKTKDIIKDALKDfDGTLILVSHDRDFLD 505
Cdd:COG1245 247 qrLNVARLIRELAEE-GKYVLVVEHDLAILD 276
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.47e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFS--DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaYLPQHLLTQDK 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 vtvFEETMKAFEEVTQmqkelDELNEQLTIRTDYetdDYMKLIERVSELSEKFYSIeetnydaeVEKVLKGLG-FERKDF 157
Cdd:PRK13648 78 ---FEKLRKHIGIVFQ-----NPDNQFVGSIVKY---DVAFGLENHAVPYDEMHRR--------VSEALKQVDmLERADY 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 158 TRQTseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL--INSAKAVMVIS--HD 219
Cdd:PRK13648 139 EPNA--LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVrkVKSEHNITIISitHD 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
1.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKpttgnvtgpkeaviayLPQHLLTQDKVTV 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE----------------LESEVRVEGRVEF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 FEETmkafeeVTQMQKELDELNEQLTIRTDYETDDYMKLIERVSelsekfYSIE------ETNYDAEVEKVLKG--LGFE 153
Cdd:PRK14258 72 FNQN------IYERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVA------YGVKivgwrpKLEIDDIVESALKDadLWDE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 154 RKDFTRQTS-EFSGGWRMRIELAKILLKKPDLILLDEPTNHMD------IESIqwLEDFLINSAKAVMVISHDRAFVDNI 226
Cdd:PRK14258 140 IKHKIHKSAlDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRL 217
|
....
gi 1525942895 227 TNRT 230
Cdd:PRK14258 218 SDFT 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
328-503 |
1.70e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI-MNEIDFEGGLKVGH------------------- 387
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAGTIRVGDitidtarslsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 388 NAKIGYFAQNQAalLDENLTVFETIDQIPLT-------DGSIKIKDLLGAFMFSGDDTTKKvKVLSGGEKTRLAMIKLL- 459
Cdd:PRK11264 84 RQHVGFVFQNFN--LFPHRTVLENIIEGPVIvkgepkeEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALa 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525942895 460 LEPvNVLILDEPTNHLDmktKDIIKDALKDFDG------TLILVSHDRDF 503
Cdd:PRK11264 161 MRP-EVILFDEPTSALD---PELVGEVLNTIRQlaqekrTMVIVTHEMSF 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-239 |
2.05e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 21 TFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---------TGPKEAVIAYLpqhlltqdkvtvFEETmKAFEE 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPSRRPVSML------------FQEN-NLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 92 VTQMQkeldelNEQLTIRTDYETDDYMKliervselsekfysieetnydAEVEKVLKGLGFErkDF-TRQTSEFSGGWRM 170
Cdd:PRK10771 86 LTVAQ------NIGLGLNPGLKLNAAQR---------------------EKLHAIARQMGIE--DLlARLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 171 RIELAKILLKKPDLILLDEPTNHMD----IESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRIY 239
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-527 |
2.41e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGD-HVVFQKASMVIERGEKVAFVGKNGEGKST----------------MIKAimNEIDFEGGLKVGHNAKIG 392
Cdd:PRK13639 4 TRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTlflhfngilkptsgevLIKG--EPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 393 YFAQNQaallDENL---TVFETIDQIPLTDG------SIKIKDLLGAFMFSGDDTtKKVKVLSGGEKTRLAMIKLLLEPV 463
Cdd:PRK13639 82 IVFQNP----DDQLfapTVEEDVAFGPLNLGlskeevEKRVKEALKAVGMEGFEN-KPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 464 NVLILDEPTNHLDMKTKDIIKDALKDFDG---TLILVSHDRDFLDGLVQKVFEFGNKRV------REHFEDIK 527
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIikegtpKEVFSDIE 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
338-502 |
2.78e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 338 GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG--LKVGHN----------AKIGYFAQNQAALLDen 405
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGtlLFEGEDistlkpeiyrQQVSYCAQTPTLFGD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 406 lTVFETI-------DQIPLTDgsiKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMK 478
Cdd:PRK10247 96 -TVYDNLifpwqirNQQPDPA---IFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180
....*....|....*....|....*...
gi 1525942895 479 TK----DIIKDALKDFDGTLILVSHDRD 502
Cdd:PRK10247 172 NKhnvnEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
347-484 |
3.70e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.72 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDF----EGGLKV-GHNAK-IGYFAQNQAALLDEN------LTVFETIDq 414
Cdd:cd03233 27 SGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYnGIPYKeFAEKYPGEIIYVSEEdvhfptLTVRETLD- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 415 ipltdGSIKIKdllgafmfsGDDTtkkVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLD-MKTKDIIK 484
Cdd:cd03233 106 -----FALRCK---------GNEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDsSTALEILK 159
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-500 |
4.16e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---------TGPK---EAVIAYLPQ 71
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlylgkevtfNGPKssqEAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 hlltqdkvtvfeetmkafeevtqmqkeldELN--EQLTIRTDyetddymklIERVSELSEKFYSIEETNYDAEVEKVLKG 149
Cdd:PRK10762 87 -----------------------------ELNliPQLTIAEN---------IFLGREFVNRFGRIDWKKMYAEADKLLAR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LGFERKDFTRqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHM-DIESIQWLEdfLINSAKA----VMVISHDRAFVD 224
Cdd:PRK10762 129 LNLRFSSDKL-VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR--VIRELKSqgrgIVYISHRLKEIF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 225 NITNRtieVTMGRiydykakyshylqlradrrihqlkayeeqqrfiaDNQeFIDrfrgtysktlqvQSRVKMLEKLEVIE 304
Cdd:PRK10762 206 EICDD---VTVFR----------------------------------DGQ-FIA------------EREVADLTEDSLIE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 305 I---DEVDTSALRLKFPPsprsGQYPVMVEELTKTYGDHVVFQkasmvIERGEKVAFVGKNGEGKSTMIKAIM------- 374
Cdd:PRK10762 236 MmvgRKLEDQYPRLDKAP----GEVRLKVDNLSGPGVNDVSFT-----LRKGEILGVSGLMGAGRTELMKVLYgalprts 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 375 NEIDFEG----------GLKVGhnakIGYFAQNQAA---LLD----ENLTVfETIDQIPLTDGSIK-------IKDLLGA 430
Cdd:PRK10762 307 GYVTLDGhevvtrspqdGLANG----IVYISEDRKRdglVLGmsvkENMSL-TALRYFSRAGGSLKhadeqqaVSDFIRL 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 431 FMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF--DG-TLILVSHD 500
Cdd:PRK10762 382 FNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaEGlSIILVSSE 454
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
4.24e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTT-LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAViaylpqhlltqdkv 79
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tvfeeTMKAFEEVTQMQKELDELNEQLTIRTDYETDDYMKLIErvselsekfYSIEETNYDAEVEKVLKGLGFERKdFTR 159
Cdd:PRK13652 69 -----TKENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPIN---------LGLDEETVAHRVSSALHMLGLEEL-RDR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL 206
Cdd:PRK13652 134 VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFL 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-238 |
4.35e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV---TGPKEAVIaylpqhlltqdkvt 80
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagTAPLAEAR-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 vfEETMKAFEEVTQMQkeldelneqltirtdyetddYMKLIERVSeLSEKfysieeTNYDAEVEKVLKGLGFERKDfTRQ 160
Cdd:PRK11247 81 --EDTRLMFQDARLLP--------------------WKKVIDNVG-LGLK------GQWRDAALQALAAVGLADRA-NEW 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 161 TSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD----IESIQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMG 236
Cdd:PRK11247 131 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
..
gi 1525942895 237 RI 238
Cdd:PRK11247 211 KI 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
141-238 |
4.78e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 141 AEVEKVLKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDI----ESIQWLEDFLINSAKAVMVI 216
Cdd:PRK10261 441 ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFI 520
|
90 100
....*....|....*....|..
gi 1525942895 217 SHDRAFVDNITNRTIEVTMGRI 238
Cdd:PRK10261 521 SHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-241 |
4.85e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 50.49 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGG--TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV--------TGPKEAV---IAY 68
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeidgidisTIPLEDLrssLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 69 LPQhlltqdKVTVFEETMKAfeevtqmqkELDELNEqltirtdyetddymkliervselsekfYSieetnyDAEVEKVLK 148
Cdd:cd03369 87 IPQ------DPTLFSGTIRS---------NLDPFDE---------------------------YS------DEEIYGALR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 glgferkdFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESiqwleDFLIN-------SAKAVMVISHD-R 220
Cdd:cd03369 119 --------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-----DALIQktireefTNSTILTIAHRlR 185
|
250 260
....*....|....*....|.
gi 1525942895 221 AFVDniTNRTIEVTMGRIYDY 241
Cdd:cd03369 186 TIID--YDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
342-502 |
5.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.14 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTM-------IKAIMNEIDFEGGLKVGHN-----AKIGYFAQNQaalldENLTVF 409
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTIskiltglLKPQSGEIKIDGITISKENlkeirKKIGIIFQNP-----DNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 410 ETI-DQIP--LTDGSI---KIKDLLgafmfsgDDTTKKVKV----------LSGGEKTRLAMIKLL-LEPvNVLILDEPT 472
Cdd:PRK13632 99 ATVeDDIAfgLENKKVppkKMKDII-------DDLAKKVGMedyldkepqnLSGGQKQRVAIASVLaLNP-EIIIFDEST 170
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 473 NHLD----MKTKDIIKDALKDFDGTLILVSHDRD 502
Cdd:PRK13632 171 SMLDpkgkREIKKIMVDLRKTRKKTLISITHDMD 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-281 |
5.91e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTG--NVTGPKeavIAYLPQHLL 74
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQD---VATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKVTVFEETMKAFEEVTQMQKEldelnEQLTIRTDYETDDYMKLIERVSELSEKFysieetnydaevekvlkGLGfER 154
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAA-----QNVEVPAVYAGLERKQRLLRAQELLQRL-----------------GLE-DR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 155 KDFtrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES---IQWLEDFLINSAKAVMVISHDRAfVDNITNRTI 231
Cdd:PRK10535 138 VEY--QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVI 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 232 EVTMGRIY-DYKAKYSHYLQlradrrihqlKAYEEQQRFIADNQEFIDRFR 281
Cdd:PRK10535 215 EIRDGEIVrNPPAQEKVNVA----------GGTEPVVNTASGWRQFVSGFR 255
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-195 |
6.48e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 50.35 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 16 LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAkPTTGNVTGpkeaviaylpqhlltqdKVTVFEETMKAfeevTQM 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSG-----------------QILFNGQPRKP----DQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 96 QKE------LDELNEQLTIRtdyETDDYMKLIeRVSELSEKFYSIEEtnydAEVEkVLKGLGFERKDFTRQTSeFSGGWR 169
Cdd:cd03234 80 QKCvayvrqDDILLPGLTVR---ETLTYTAIL-RLPRKSSDAIRKKR----VEDV-LLRDLALTRIGGNLVKG-ISGGER 149
|
170 180
....*....|....*....|....*.
gi 1525942895 170 MRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:cd03234 150 RRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
326-502 |
7.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 326 YPVMVEELTKTYGDHV-VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKVGHNAKIGYFAQNQAALLDE 404
Cdd:PRK13636 4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 405 NLTVFETIDQiPLTDGSIKIKDLLGA--FMFSGDDTTKKVK-----------------VLSGGEKTRLAMIKLLLEPVNV 465
Cdd:PRK13636 84 VGMVFQDPDN-QLFSASVYQDVSFGAvnLKLPEDEVRKRVDnalkrtgiehlkdkpthCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525942895 466 LILDEPTNHLD-MKTKDIIK---DALKDFDGTLILVSHDRD 502
Cdd:PRK13636 163 LVLDEPTAGLDpMGVSEIMKllvEMQKELGLTIIIATHDID 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-238 |
8.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaylpqhllTQDKVTVFEETMKafeevtqmqke 98
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI----------------IIDGVDITDKKVK----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 99 LDELNEQLTIRTDY-ETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQTS-EFSGGWRMRIELAK 176
Cdd:PRK13637 78 LSDIRKKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPfELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 177 ILLKKPDLILLDEPTNHMD-------IESIQWLEDfliNSAKAVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-219 |
8.82e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaVIAYlpqhlltqdkvTVFEETMkafeevtqmQKE 98
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT-----IAGY-----------HITPETG---------NKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 99 LDELNEQLTIRTDY-ETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMRIELAKI 177
Cdd:PRK13641 80 LKKLRKKVSLVFQFpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1525942895 178 LLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKA---VMVISHD 219
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-298 |
9.03e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 31 ALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIaylpqhlltqdkvTVFEETMKAFEEVTQmqkeLDELNEQLTIRt 110
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-------------TNISDVHQNMGYCPQ----FDAIDDLLTGR- 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 111 dyetdDYMKLIERVSELSEKfysieetnydaEVEKV----LKGLGFERKDfTRQTSEFSGGWRMRIELAKILLKKPDLIL 186
Cdd:TIGR01257 2031 -----EHLYLYARLRGVPAE-----------EIEKVanwsIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 187 LDEPTNHMDIESIQWLEDF---LINSAKAVMVISHDRAFVDNITNR-TIEVT-----MGRIYDYKAKYshylqlrADRRI 257
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTivsIIREGRAVVLTSHSMEECEALCTRlAIMVKgafqcLGTIQHLKSKF-------GDGYI 2166
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1525942895 258 HQLKAYEEQQRFIADNQEFIDRFRGTYSKTLQVQSRVKMLE 298
Cdd:TIGR01257 2167 VTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQ 2207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
331-510 |
9.15e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 331 EELTKTY-GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNeIDFEGGLKV---GHNA-------------KIGY 393
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSAGKIwfsGHDItrlknrevpflrrQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 394 FAQNQAALLDEnlTVFETIdQIPLTdgsikikdLLGAfmfSGDDTTKKV-----KV------------LSGGEKTRLAMI 456
Cdd:PRK10908 84 IFQDHHLLMDR--TVYDNV-AIPLI--------IAGA---SGDDIRRRVsaaldKVglldkaknfpiqLSGGEQQRVGIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 457 KLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDFDG---TLILVSHDRdfldGLVQK 510
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDI----GLISR 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
347-476 |
1.12e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.20 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMNEIdfEGGLKVGHNAKI--------------GYFAQNQaaLLDENLTVFETI 412
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLngmpidakemraisAYVQQDD--LFIPTLTVREHL 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 413 ---------DQIPLTDGSIKIKDLLGAF-MFSGDDT----TKKVKVLSGGEKTRLAM-IKLLLEPVnVLILDEPTNHLD 476
Cdd:TIGR00955 121 mfqahlrmpRRVTKKEKRERVDEVLQALgLRKCANTrigvPGRVKGLSGGERKRLAFaSELLTDPP-LLFCDEPTSGLD 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-472 |
1.16e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT---GP------KEAV---IAYLPQ 71
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlgGDmadarhRRAVcprIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 72 HLltqdkvtvfeetmkafeevtqmQKELdelneqltirtdyetddYMKLiervselsekfySIEEtNYD--AEvekvLKG 149
Cdd:NF033858 84 GL----------------------GKNL-----------------YPTL------------SVFE-NLDffGR----LFG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 150 LG-FERK----DFTRQT--SEF--------SGGWRMRIELAKILLKKPDLILLDEPTNHMDIESiqwledflinsakavm 214
Cdd:NF033858 108 QDaAERRrridELLRATglAPFadrpagklSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS---------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 215 vishDRAFVDNItnrtievtmGRIydykakyshylqlRADRRihQLK-----AY-EEQQRF---IADN----------QE 275
Cdd:NF033858 172 ----RRQFWELI---------DRI-------------RAERP--GMSvlvatAYmEEAERFdwlVAMDagrvlatgtpAE 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 276 FIDRfrgTYSKTLQvQSRVKMLEklevieiDEVDTSALRLKFPP-SPRSGQYPVMV-EELTKTYG-----DHVVFQkasm 348
Cdd:NF033858 224 LLAR---TGADTLE-AAFIALLP-------EEKRRGHQPVVIPPrPADDDDEPAIEaRGLTMRFGdftavDHVSFR---- 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 349 vIERGEKVAFVGKNGEGKSTMIKaiM----------------NEIDfegglkvGHN----AKIGYFAqnQAALLDENLTV 408
Cdd:NF033858 289 -IRRGEIFGFLGSNGCGKSTTMK--MltgllpasegeawlfgQPVD-------AGDiatrRRVGYMS--QAFSLYGELTV 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 409 FETID------QIPLTDGSIKIKDLLGAFMFSG------DDttkkvkvLSGGEKTRL----AMIKlllEPvNVLILDEPT 472
Cdd:NF033858 357 RQNLElharlfHLPAAEIAARVAEMLERFDLADvadalpDS-------LPLGIRQRLslavAVIH---KP-ELLILDEPT 425
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-195 |
1.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.13 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVS------FGGTTLFsDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAylpqhllt 75
Cdd:PRK13649 3 INLQNVSYTyqagtpFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 76 QDKVTVFEETMKAFEEVTQMQKeldelnEQLTIRTdyetddymkLIERVSELSEKF-YSIEETNYDAEvEKvLKGLGFER 154
Cdd:PRK13649 74 TSKNKDIKQIRKKVGLVFQFPE------SQLFEET---------VLKDVAFGPQNFgVSQEEAEALAR-EK-LALVGISE 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525942895 155 KDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK13649 137 SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
330-499 |
1.22e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------NEIDFEG------GLKVGHNAKIGYFAQ 396
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyqpdsGEILLDGepvrfrSPRDAQAAGIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAalLDENLTVFETI--DQIPLTDGSI-------KIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLI 467
Cdd:COG1129 87 ELN--LVPNLSVAENIflGREPRRGGLIdwramrrRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1525942895 468 LDEPTNHLDMK-TK---DIIKDaLKDFDGTLILVSH 499
Cdd:COG1129 164 LDEPTASLTEReVErlfRIIRR-LKAQGVAIIYISH 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
350-543 |
1.31e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKVGHNAKIGYFAQNQ---AALLDENL---TVFETIDQIPLTDGSIK 423
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVSwifNATVRENIlfgSDFESERYWRAIDVTAL 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 424 IKDLlgaFMFSGDDTT---KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKT-----KDIIKDALKdfDGTLI 495
Cdd:PLN03232 720 QHDL---DLLPGRDLTeigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVahqvfDSCMKDELK--GKTRV 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 496 LVSHDRDFLDgLVQKVFEFGNKRVREH--FEDI--KGFLAYKKMDNLKEIEQ 543
Cdd:PLN03232 795 LVTNQLHFLP-LMDRIILVSEGMIKEEgtFAELskSGSLFKKLMENAGKMDA 845
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-83 |
1.35e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAV-----------IAYLPQH 72
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkVAYLPQQ 93
|
90
....*....|.
gi 1525942895 73 LLTQDKVTVFE 83
Cdd:PRK10575 94 LPAAEGMTVRE 104
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-195 |
1.46e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFGGTTLFSDVTFSINEN-------------DKIALMGKNGAGKSTILKIIAdvAKPTTGNVTGPkeaviaylpqh 72
Cdd:PLN03211 60 NIKRILGHKPKISDETRQIQERtilngvtgmaspgEILAVLGPSGSGKSTLLNALA--GRIQGNNFTGT----------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQD-KVTvfEETMKAFEEVTQMqkelDELNEQLTIRtdyETDDYMKLIERVSELSEKfysiEETNYdaeVEKVLKGLG 151
Cdd:PLN03211 127 ILANNrKPT--KQILKRTGFVTQD----DILYPHLTVR---ETLVFCSLLRLPKSLTKQ----EKILV---AESVISELG 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1525942895 152 FERKDFTRQTSEF----SGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PLN03211 191 LTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4-219 |
1.50e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 4 VNNISVsfgGTTLFSdVTFSINENDKIALMGKNGAGKSTILKIIADVAkPTTGNVT----------GPKEAVI-AYLPQH 72
Cdd:PRK03695 3 LNDVAV---STRLGP-LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQfagqpleawsAAELARHrAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 73 LLTQDKVTVFeetmkafeevtQMQkeldelneQLTIRTDYETDDYMKLIERVSELsekfysieetnydaevekvlkgLGF 152
Cdd:PRK03695 78 QTPPFAMPVF-----------QYL--------TLHQPDKTRTEAVASALNEVAEA----------------------LGL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 153 ERKdFTRQTSEFSGGWRMRIELAKILLK-----KPD--LILLDEPTNHMDIESIQWLeDFLIN----SAKAVMVISHD 219
Cdd:PRK03695 117 DDK-LGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAAL-DRLLSelcqQGIAVVMSSHD 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
330-501 |
1.58e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAImneidfeGGLKVGHNAKIGYFAQN--------QAAL 401
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLI-------AGLLNPEKGEILFERQSikkdlctyQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 402 --------LDENLTVFET-IDQIPLTDGSIKIKDLLGAFMFsGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:PRK13540 77 cfvghrsgINPYLTLRENcLYDIHFSPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 1525942895 473 NHLDMKTKDIIKDALKDF---DGTLILVSHDR 501
Cdd:PRK13540 156 VALDELSLLTIITKIQEHrakGGAVLLTSHQD 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-198 |
1.65e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 31 ALMGKNGAGKSTILKIIADvaKPTTGNVT-------GPK-----EAVIAYLPQHLLTQDKVTVfEETMKaFEEVTQMQKE 98
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVLAE--RVTTGVITggdrlvnGRPldssfQRSIGYVQQQDLHLPTSTV-RESLR-FSAYLRQPKS 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 99 LdelneqltirTDYETDDYMKLIERVSELsekfysieETNYDAEVEKVLKGLGFERkdftrqtsefsggwRMRIELAKIL 178
Cdd:TIGR00956 869 V----------SKSEKMEYVEEVIKLLEM--------ESYADAVVGVPGEGLNVEQ--------------RKRLTIGVEL 916
|
170 180
....*....|....*....|.
gi 1525942895 179 LKKPDLIL-LDEPTNHMDIES 198
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQT 937
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-219 |
1.86e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.80 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 18 SDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTgnvtgpkeaviayLPQHLLTQDKVTVFEETM-KAFEEVTQMQ 96
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-------------NPNSKITVDGITLTAKTVwDIREKVGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 97 KELDELNEQLTIrtdyeTDDYMKLIERVSELSEKFYSIeetnydaeVEKVLKGLGFerKDFTR-QTSEFSGGWRMRIELA 175
Cdd:PRK13640 91 QNPDNQFVGATV-----GDDVAFGLENRAVPRPEMIKI--------VRDVLADVGM--LDYIDsEPANLSGGQKQRVAIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1525942895 176 KILLKKPDLILLDEPTNHMDIES----IQWLEDFLINSAKAVMVISHD 219
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
352-511 |
2.06e-06 |
|
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: 47.74 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 352 RGEKVAFVGKNGEGKSTMIKAImneidfegglkvghnakiGYfaqnqAALLDENLTVFETIDQIPLTDGSIKIkdllgAF 431
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI------------------GL-----ALGGAQSATRRRSGVKAGCIVAAVSA-----EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 432 MFSgddttkkVKVLSGGEKTRLAMIKLL----LEPVNVLILDEPTNHLDMKTKDIIKDALKDF---DGTLILVSHDRDFL 504
Cdd:cd03227 72 IFT-------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPELA 144
|
....*..
gi 1525942895 505 DGLVQKV 511
Cdd:cd03227 145 ELADKLI 151
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-201 |
2.08e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.61 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 17 FSDVTFSINENDKI-ALMGKNGAGKSTILKIIADVAKPTTGNVT--------------GPKEAVIAYLPQH-LLTQDKVT 80
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLDdvkfrkllirngefGDSAKLILYYGTSrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMkafeevTQMQKELDELNEQLTIRTDY-ETDDYmkLIERVSELSEKFYSIEETNYDAeVEKVL-------KGLGF 152
Cdd:COG3950 94 KLERLK------EEYFSRLDGYDSLLDEDSNLrEFLEW--LREYLEDLENKLSDELDEKLEA-VREALnkllpdfKDIRI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 153 ERKDFTRQTSEFSGGWR--------------------MRIELAKILLKKPD----LILLDEPTNHMdieSIQW 201
Cdd:COG3950 165 DRDPGRLVILDKNGEELplnqlsdgersllalvgdlaRRLAELNPALENPLegegIVLIDEIDLHL---HPKW 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
342-499 |
2.30e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.49 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN---------EIDFEGGLKVGH---NAKIGYFAQNQ---AALLDENL 406
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptggqvLLDGVPLVQYDHhylHRQVALVGQEPvlfSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 407 TV---FETIDQIPLTDGSIKIKDLLGAFMfSGDDTT--KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD 481
Cdd:TIGR00958 576 AYgltDTPDEEIMAAAKAANAHDFIMEFP-NGYDTEvgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170
....*....|....*...
gi 1525942895 482 IIKDALKDFDGTLILVSH 499
Cdd:TIGR00958 655 LLQESRSRASRTVLLIAH 672
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
332-499 |
2.32e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 332 ELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM---------NEIDFEGGLKVGHNAK----IGYFAQNQ 398
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphgtyeGEIIFEGEELQASNIRdterAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 AALLDENLTVFETI--DQIPLTDGSI-------KIKDLLGAFMFSGDDTTkKVKVLSGGEKTRLAMIKLLLEPVNVLILD 469
Cdd:PRK13549 90 ELALVKELSVLENIflGNEITPGGIMdydamylRAQKLLAQLKLDINPAT-PVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190
....*....|....*....|....*....|....
gi 1525942895 470 EPTNHLDMKT----KDIIKDaLKDFDGTLILVSH 499
Cdd:PRK13549 169 EPTASLTESEtavlLDIIRD-LKAHGIACIYISH 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
2.42e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.07 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPttgNVTGPKEAVIAYLPQHLLTQDKVTV 81
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLEL---NEEARVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 82 feETMKAFEEVTQMQKELDELN--EQLTIRTDYEtddymKLIERVSELSEKfysieetnydaeVEKVLK--GLGFERKD- 156
Cdd:PRK14267 82 --EVRREVGMVFQYPNPFPHLTiyDNVAIGVKLN-----GLVKSKKELDER------------VEWALKkaALWDEVKDr 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 157 FTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK--AVMVISHDRAFVDNITNRTIEVT 234
Cdd:PRK14267 143 LNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLY 222
|
....
gi 1525942895 235 MGRI 238
Cdd:PRK14267 223 LGKL 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
330-499 |
2.60e-06 |
|
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: 49.08 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTY--GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKV-GHN-----------------A 389
Cdd:cd03289 5 VKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIdGVSwnsvplqkwrkafgvipQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 390 KIGYFAQNQAALLD--------------ENLTVFETIDQIPltdGSIKIKDLLGAFmfsgddttkkvkVLSGGEKTRLAM 455
Cdd:cd03289 85 KVFIFSGTFRKNLDpygkwsdeeiwkvaEEVGLKSVIEQFP---GQLDFVLVDGGC------------VLSHGHKQLMCL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525942895 456 IKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKD--FDGTLILVSH 499
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEH 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-220 |
3.05e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 5 NNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQdkVTVFEE 84
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ--VSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 85 TMKAFEEVTQmqkelDELNEQLTIRtdyetddymkliervselsekfysieetNYDAEVEKVLKGLG-FERKDFTRQTS- 162
Cdd:PRK10247 89 TPTLFGDTVY-----DNLIFPWQIR----------------------------NQQPDPAIFLDDLErFALPDTILTKNi 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 163 -EFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK----AVMVISHDR 220
Cdd:PRK10247 136 aELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-198 |
3.69e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.62 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 16 LFSDVTFSINENDKIALMGKNGAGKSTILKIIAdvAKPTTGNVTGpkEAVIAYLPQHlltqdkvtvfeetmKAFEEVTQM 95
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVITG--EILINGRPLD--------------KNFQRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 96 QKELDELNEQLTIRtdyetddymkliervselsekfysiEETNYDAevekVLKGLGFE-RKDFTrqtsefsggwrMRIEL 174
Cdd:cd03232 84 VEQQDVHSPNLTVR-------------------------EALRFSA----LLRGLSVEqRKRLT-----------IGVEL 123
|
170 180
....*....|....*....|....
gi 1525942895 175 AkillKKPDLILLDEPTNHMDIES 198
Cdd:cd03232 124 A----AKPSILFLDEPTSGLDSQA 143
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
290-504 |
4.04e-06 |
|
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: 49.94 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 290 VQSRVKMLEKLEVIEIDEVDTSALRLKfPPSPRSGqYPVMVEELTKTY--GDHVVFQKASMVIERGEKVAFVGKNGEGKS 367
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELEPDSIERR-TIKPGEG-NSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKS 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 368 TMIKAIMNEID-FEGglKVGHNAKIGYFAQN---QAALLDENLtVFETIDQIPLTDGSIKIKDLLG--AFMFSGDDTT-- 439
Cdd:TIGR00957 679 SLLSALLAEMDkVEG--HVHMKGSVAYVPQQawiQNDSLRENI-LFGKALNEKYYQQVLEACALLPdlEILPSGDRTEig 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 440 KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDFDGTL-----ILVSHDRDFL 504
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYL 825
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
352-508 |
4.05e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 352 RGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnakigyfaqnQAALLDENLTVFETIDQIpltdgsikikdllgaf 431
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG---------------GVIYIDGEDILEEVLDQL---------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 432 mfSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDII---------KDALKDFDGTLILVSHDRD 502
Cdd:smart00382 50 --LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelrllLLLKSEKNLTVILTTNDEK 127
|
....*.
gi 1525942895 503 FLDGLV 508
Cdd:smart00382 128 DLGPAL 133
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-195 |
4.34e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.87 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVN--NISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkEAVIAylpqhlltqdk 78
Cdd:PRK11000 1 MASVTlrNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG------DLFIG----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 vtvfEETMKafeEVTQMQKELDelneqlTIRTDYETDDYMKLIERVSeLSEKFYSIEETNYDAEVEKVLKGLGFErKDFT 158
Cdd:PRK11000 64 ----EKRMN---DVPPAERGVG------MVFQSYALYPHLSVAENMS-FGLKLAGAKKEEINQRVNQVAEVLQLA-HLLD 128
|
170 180 190
....*....|....*....|....*....|....*..
gi 1525942895 159 RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:PRK11000 129 RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
328-514 |
4.45e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASmVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlkvghnakigyfaqnqaalldenlt 407
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 vfetIDQIPLTDGSIKikdllgafmfsgddtTKKVKvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDAL 487
Cdd:cd03222 55 ----NDEWDGITPVYK---------------PQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|.
gi 1525942895 488 KDF----DGTLILVSHDRDFLDGLVQKVFEF 514
Cdd:cd03222 115 RRLseegKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-500 |
5.49e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.21 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 339 DHVVFQ----------KASMVIERGEKVAFVGKNGEGKSTMIKAIMneidfegGLKVGHNAKIGYfaqNQAALLDENLT- 407
Cdd:PRK13648 11 KNVSFQyqsdasftlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI-------GIEKVKSGEIFY---NNQAITDDNFEk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 408 -------VFETIDQIPLtdGSIKIKDL---LGAFMFSGDDTTKKVK-----------------VLSGGEKTRLAMIKLLL 460
Cdd:PRK13648 81 lrkhigiVFQNPDNQFV--GSIVKYDVafgLENHAVPYDEMHRRVSealkqvdmleradyepnALSGGQKQRVAIAGVLA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1525942895 461 EPVNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARqnllDLVRKVKSEHNITIISITHD 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-238 |
5.51e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.06 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSF-GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviayLPQHLLTQDkv 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV----------LVSGIDTGD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tvfeetmkaFEEVTQMQKELDelneqlTIRTDYETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKDFtR 159
Cdd:PRK13644 69 ---------FSKLQGIRKLVG------IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRH-R 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES-IQWLEDF--LINSAKAVMVISHDRAFVdNITNRTIEVTMG 236
Cdd:PRK13644 133 SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
..
gi 1525942895 237 RI 238
Cdd:PRK13644 212 KI 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-240 |
5.66e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqHLLTQDkVTVFEET 85
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---------------YRYSGD-VLLGGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 86 MKAFEEVTQMQKELDELNEQLTIRTDYETDDYMKLIErvselSEKFYSIEETNYDAEVEKVLKGLGFERKD-FTRQTSEF 164
Cdd:PRK14271 90 IFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVR-----AHKLVPRKEFRGVAQARLTEVGLWDAVKDrLSDSPFRL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 165 SGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK--AVMVISHDRAFVDNITNRTIEVTMGRIYD 240
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
328-502 |
5.95e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 48.26 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGD--HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAImneidfegglkvghnakigyfaqNQAALLDEN 405
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLI-----------------------NGLLLPDDN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 406 LTVFETIDQIPLTDGSI-KIKDLLGaFMFS-----------GDDTT-----------KKVKV------------------ 444
Cdd:PRK13640 63 PNSKITVDGITLTAKTVwDIREKVG-IVFQnpdnqfvgatvGDDVAfglenravprpEMIKIvrdvladvgmldyidsep 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 445 --LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHDRD 502
Cdd:PRK13640 142 anLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKKNNLTVISITHDID 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
330-522 |
6.39e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaIMN--EIDFEGGLKVGHN-----AKIGyfaQNQAALL 402
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNllETPDSGQLNIAGHqfdfsQKPS---EKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 403 DEN-------------LTVFETIDQIPL-------TDGSIKIKDLLGAFMFSgDDTTKKVKVLSGGEKTRLAMIK-LLLE 461
Cdd:COG4161 81 RQKvgmvfqqynlwphLTVMENLIEAPCkvlglskEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARaLMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 462 PvNVLILDEPTNHLDMK-TK---DIIKDaLKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREH 522
Cdd:COG4161 160 P-QVLLFDEPTAALDPEiTAqvvEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
330-499 |
7.36e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.56 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTY-GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-------EIDFEGG--LKVGHNA---KIGYFAQ 396
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypltegEIRLDGRplSSLSHSVlrqGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAALLD---ENLT---------VFETIDQIPLTDGSIKIKDLLGAFMFSGDDTtkkvkvLSGGEKTRLAMIKLLLEPVN 464
Cdd:PRK10790 423 DPVVLADtflANVTlgrdiseeqVWQALETVQLAELARSLPDGLYTPLGEQGNN------LSVGQKQLLALARVLVQTPQ 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 1525942895 465 VLILDEPTNHLDMKTKDIIKDALKDF--DGTLILVSH 499
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
328-501 |
7.59e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMN-EIDFEG-----GLKVGHNA----KIGYFAQN 397
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTEGqifidGEDVTHRSiqqrDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 398 QAAL----LDENLTVFETIDQIPLTDGSIKIKDLLGAFMFSG-DDttKKVKVLSGGEKTRLAMIK-LLLEPvNVLILDEP 471
Cdd:PRK11432 87 YALFphmsLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGfED--RYVDQISGGQQQRVALARaLILKP-KVLLFDEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1525942895 472 TNHLD------MKTKdiIKDALKDFDGTLILVSHDR 501
Cdd:PRK11432 164 LSNLDanlrrsMREK--IRELQQQFNITSLYVTHDQ 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
330-500 |
7.90e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 47.06 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVfqKASMVIERGEKVAFVGKNGEGKSTMIKAImneidfeGGLKVGHNAKIgyFAQNQ----------- 398
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLI-------AGFLPPDSGRI--LWNGQdltalppaerp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 399 -AALLDEN-----LTVFETI-----DQIPLTDGSI-KIKDLLgafmfsgddttKKVKV----------LSGGEKTRLAMI 456
Cdd:COG3840 73 vSMLFQENnlfphLTVAQNIglglrPGLKLTAEQRaQVEQAL-----------ERVGLaglldrlpgqLSGGQRQRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1525942895 457 KLLLEPVNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRqemlDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-507 |
8.21e-06 |
|
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: 47.36 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 349 VIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAK----IGYFAQNQ-----AALLDENLTVF---ETIDQIP 416
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG-KFDDPPDwdeiLDEFRGSElqnyfTKLLEGDVKVIvkpQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 417 LT-DGSI----KIKDLLGAFMFSGDDTT------KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----D 481
Cdd:cd03236 101 KAvKGKVgellKKKDERGKLDELVDQLElrhvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaR 180
|
170 180
....*....|....*....|....*.
gi 1525942895 482 IIKDALKDfDGTLILVSHDRDFLDGL 507
Cdd:cd03236 181 LIRELAED-DNYVLVVEHDLAVLDYL 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-282 |
8.55e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.31 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIadvakptTGNVTGPK--EAVIAYLPQHLLTQDK 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKsaGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 79 VTvfEETMKAFEEVTQMQKELDELN-----EQLTIRTDYETDDYMKLIERVSELSEKfysieetnydaEVEKVLKGLGFE 153
Cdd:PRK09984 77 LA--RDIRKSRANTGYIFQQFNLVNrlsvlENVLIGALGSTPFWRTCFSWFTREQKQ-----------RALQALTRVGMV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 154 RKDFTRqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIEsiqwledflinSAKAVMVISHDRAFVDNItnrTIEV 233
Cdd:PRK09984 144 HFAHQR-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPE-----------SARIVMDTLRDINQNDGI---TVVV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1525942895 234 TMGRIyDYKAKYSHylQLRADRRIHQLKAYEEQQrfiADNQEFIDRFRG 282
Cdd:PRK09984 209 TLHQV-DYALRYCE--RIVALRQGHVFYDGSSQQ---FDNERFDHLYRS 251
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
9.28e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.42 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTT---LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaYLPQHLLTQD 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI---------IIDGDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 78 KV--------TVFEETMKAFEEVTqmqkeldeLNEQLTIRTDYETDDYMKLIERVSELSEkfysieetnydaevekvLKG 149
Cdd:PRK13650 75 NVwdirhkigMVFQNPDNQFVGAT--------VEDDVAFGLENKGIPHEEMKERVNEALE-----------------LVG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 150 LgferKDF-TRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD----IESIQWLEDFLINSAKAVMVISHD 219
Cdd:PRK13650 130 M----QDFkEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
9.63e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.54 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTT-----LFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV------TGPKEAVIAYL 69
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 70 PQHLltQDKVTVFEETMKAFEEVTQMQkeldelnEQLTIRTDYETDDYMKLI------ERVSELSeKFYsieetnydaev 143
Cdd:PRK13631 101 TNPY--SKKIKNFKELRRRVSMVFQFP-------EYQLFKDTIEKDIMFGPValgvkkSEAKKLA-KFY----------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 144 ekvLKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDfLINSAKA----VMVISHD 219
Cdd:PRK13631 160 ---LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKAnnktVFVITHT 235
|
250
....*....|....*....
gi 1525942895 220 RAFVDNITNRTIEVTMGRI 238
Cdd:PRK13631 236 MEHVLEVADEVIVMDKGKI 254
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-218 |
1.19e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGG--TTLFSDVTFSINENDKIALMGKNGAGKSTIlkiiadvakpttgnvtgpkeaviaylpQHLLTQdkv 79
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTI---------------------------ANLLTR--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tvfeetmkaFEEVTQMQKELDELNEQltirtDYETDDYMKLIERVSE---------------LSEKFYSIEETNYDAE-- 142
Cdd:PRK11176 392 ---------FYDIDEGEILLDGHDLR-----DYTLASLRNQVALVSQnvhlfndtianniayARTEQYSREQIEEAARma 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 143 -----VEKVLKGL----GferkdftRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIES---IQWLEDFLiNSA 210
Cdd:PRK11176 458 yamdfINKMDNGLdtviG-------ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESeraIQAALDEL-QKN 529
|
....*...
gi 1525942895 211 KAVMVISH 218
Cdd:PRK11176 530 RTSLVIAH 537
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-504 |
1.32e-05 |
|
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: 46.56 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlKVGHNAK-----------------IGYFAQNQ---AALLDENLTV- 408
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-KVHWSNKnesepsfeatrsrnrysVAYAAQKPwllNATVEENITFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 409 --FETIDQIPLTDGSIKIKDLlgAFMFSGDDTT--KKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIK 484
Cdd:cd03290 103 spFNKQRYKAVTDACSLQPDI--DLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 180
|
170 180
....*....|....*....|....*
gi 1525942895 485 DA-----LKDFDGTLILVSHDRDFL 504
Cdd:cd03290 181 QEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
330-523 |
1.41e-05 |
|
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: 46.50 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKST---MIKAIM----NEIDFEG----GLKVGHNAK--IGYFAQ 396
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfyMIVGLVrpdaGKILIDGqditHLPMHERARlgIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQAAL----LDENL-TVFETIDQIPLTDGSIKIKDLLGAF--MFSGDdttKKVKVLSGGEKTRLAMIKLLLEPVNVLILD 469
Cdd:TIGR04406 84 EASIFrkltVEENImAVLEIRKDLDRAEREERLEALLEEFqiSHLRD---NKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 470 EPTNHLD----MKTKDIIKDaLKDFD-GTLI----------------LVSHDRDFLDGLVQKVfeFGNKRVREHF 523
Cdd:TIGR04406 161 EPFAGVDpiavGDIKKIIKH-LKERGiGVLItdhnvretldicdrayIISDGKVLAEGTPAEI--VANEKVRRVY 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
340-500 |
1.43e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 340 HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNeiDFEGGLKVGHNAKIGYFAQN---------------QAALLDE 404
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARVTGDVTLNgeplaaidaprlarlRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 405 NLTVFE-TIDQIPL--------TDGSIKIKD---------LLGAFMFSGDDTTkkvkVLSGGEKTRLAMIKLLLE----- 461
Cdd:PRK13547 92 AQPAFAfSAREIVLlgrypharRAGALTHRDgeiawqalaLAGATALVGRDVT----TLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 462 ----PVNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHD 500
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHD 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
330-500 |
1.50e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKA----SMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGglKV--------GHN--------- 388
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAvdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPG--RVmaeklefnGQDlqriseker 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 389 -----AKIGYFAQNQAALLDENLTV-FETIDQIPLTDGSIKIK------DLLGafMFSGDDTTKKVKV----LSGGEKTR 452
Cdd:PRK11022 84 rnlvgAEVAMIFQDPMTSLNPCYTVgFQIMEAIKVHQGGNKKTrrqraiDLLN--QVGIPDPASRLDVyphqLSGGMSQR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 453 LaMIKLLL--EPvNVLILDEPTNHLDMKTKDIIKDALKDF----DGTLILVSHD 500
Cdd:PRK11022 162 V-MIAMAIacRP-KLLIADEPTTALDVTIQAQIIELLLELqqkeNMALVLITHD 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
305-476 |
1.53e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 305 IDEVDTSALRLKFPPSPRSGQYPVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGlK 384
Cdd:PTZ00243 638 IVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG-R 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 385 VGHNAKIGYFAQnQA----ALLDENLTVFETIDQIPLTDgSIKIKDLLG--AFMFSGDDTT---KKVKvLSGGEKTRLAM 455
Cdd:PTZ00243 717 VWAERSIAYVPQ-QAwimnATVRGNILFFDEEDAARLAD-AVRVSQLEAdlAQLGGGLETEigeKGVN-LSGGQKARVSL 793
|
170 180
....*....|....*....|.
gi 1525942895 456 IKLLLEPVNVLILDEPTNHLD 476
Cdd:PTZ00243 794 ARAVYANRDVYLLDDPLSALD 814
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
445-504 |
1.62e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 445 LSGGEKT------RLAMIKLLLEPVNVLILDEPTNHLD----MKTKDIIKDALKDFDG--TLILVSHDRDFL 504
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrrTNLKDIIEYSLKDSSDipQVIMISHHRELL 873
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
445-501 |
1.67e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.65 E-value: 1.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 445 LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDfdgtlilVSHDR 501
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGR 521
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-200 |
1.69e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqhlltqdKVT 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG---------------------EIL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKafEEVTQMQKEL------DELNEQLTIRTDYetddymkliervselsekFYSIEETNYDAEVEKVLKGLGFER 154
Cdd:PRK13540 60 FERQSIK--KDLCTYQKQLcfvghrSGINPYLTLRENC------------------LYDIHFSPGAVGITELCRLFSLEH 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 155 K-DFTrqTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQ 200
Cdd:PRK13540 120 LiDYP--CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-191 |
1.71e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 5 NNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADV--------------AKPTTGNVTGPKEAVIAYLP 70
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegEELQASNIRDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 71 QHLLTQDKVTVFEETMkafeevtqMQKELdelneqltirTDYETDDYMKLIERVSELsekfysIEETNYDAEVE-KVlkg 149
Cdd:PRK13549 89 QELALVKELSVLENIF--------LGNEI----------TPGGIMDYDAMYLRAQKL------LAQLKLDINPAtPV--- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1525942895 150 lgferkdftrqtSEFSGGWRMRIELAKILLKKPDLILLDEPT 191
Cdd:PRK13549 142 ------------GNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-230 |
1.83e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIadvakpttgnvtgpkeaviayLPQHLLTQDKVT 80
Cdd:PTZ00265 1168 IMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL---------------------MRFYDLKNDHHI 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 81 VFEETMKafEEVTQMQKELDELNEQLTIRT---------------------------------DYETDDYMKLIERVSEL 127
Cdd:PTZ00265 1227 VFKNEHT--NDMTNEQDYQGDEEQNVGMKNvnefsltkeggsgedstvfknsgkilldgvdicDYNLKDLRNLFSIVSQE 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 128 SEKF-YSIEET----NYDAEVEKVLKGLGFERKDFTRQT-------------SEFSGGWRMRIELAKILLKKPDLILLDE 189
Cdd:PTZ00265 1305 PMLFnMSIYENikfgKEDATREDVKRACKFAAIDEFIESlpnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDE 1384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 190 PTNHMDIESIQWLEDFLIN----SAKAVMVISH--------DRAFVDNITNRT 230
Cdd:PTZ00265 1385 ATSSLDSNSEKLIEKTIVDikdkADKTIITIAHriasikrsDKIVVFNNPDRT 1437
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-218 |
1.90e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGGTTLFsDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV-------TGPKEAVIAYLPQHL 73
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncniNNIAKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 74 LTQDKVTVFeETMKAFEEVTQmqkeldelneqlTIRTDYETDDYMKLIERvseLSEKFYSIeetnydaevekvlkglgfe 153
Cdd:PRK13541 80 GLKLEMTVF-ENLKFWSEIYN------------SAETLYAAIHYFKLHDL---LDEKCYSL------------------- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1525942895 154 rkdftrqtsefSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI---NSAKAVMVISH 218
Cdd:PRK13541 125 -----------SSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmkaNSGGIVLLSSH 181
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
347-502 |
1.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 46.75 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTM-------IKAIMNEIDFEG----------GLKvGHNAKIGYFAQNQAALLDENlTVF 409
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLmqhfnalLKPSSGTITIAGyhitpetgnkNLK-KLRKKVSLVFQFPEAQLFEN-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 410 ETIDQIPL----TDGSIKIKDL--LGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDII 483
Cdd:PRK13641 105 KDVEFGPKnfgfSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180
....*....|....*....|..
gi 1525942895 484 KDALKDFDG---TLILVSHDRD 502
Cdd:PRK13641 185 MQLFKDYQKaghTVILVTHNMD 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-196 |
2.36e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 10 SFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpKEAVIAYLPQhlltqdkvtvFEETMKAf 89
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQ----------TSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 90 eevtqmqkeldELNEQLTIRTDYETDDYMKLIeRVSELSEKFYSIeetnydAEVEKVLKGLGferkdftrqTSEFSGGWR 169
Cdd:TIGR01271 502 -----------TIKDNIIFGLSYDEYRYTSVI-KACQLEEDIALF------PEKDKTVLGEG---------GITLSGGQR 554
|
170 180
....*....|....*....|....*..
gi 1525942895 170 MRIELAKILLKKPDLILLDEPTNHMDI 196
Cdd:TIGR01271 555 ARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
160-231 |
2.52e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE----SIQWLEDFLINSAKAVMVISHDRAFVDNITNRTI 231
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
350-502 |
2.54e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIKAI-------MNEIDFEGGLKVGHNA-----KIGYFAQNQaalldENLTVFETIDQ--- 414
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIdglleaeSGQIIIDGDLLTEENVwdirhKIGMVFQNP-----DNQFVGATVEDdva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 415 -------IPLTDGSIKIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----DII 483
Cdd:PRK13650 105 fglenkgIPHEEMKERVNEAL-ELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRleliKTI 183
|
170
....*....|....*....
gi 1525942895 484 KDALKDFDGTLILVSHDRD 502
Cdd:PRK13650 184 KGIRDDYQMTVISITHDLD 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
347-502 |
2.73e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVGHNA-----------KIGYFAQNQ-----AALLDENLTVF 409
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKIDGELltaenvwnlrrKIGMVFQNPdnqfvGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 410 ETIDQIPLTDGSIKIKD-LLGAFMFsgDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD----IIK 484
Cdd:PRK13642 107 MENQGIPREEMIKRVDEaLLAVNML--DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQeimrVIH 184
|
170
....*....|....*...
gi 1525942895 485 DALKDFDGTLILVSHDRD 502
Cdd:PRK13642 185 EIKEKYQLTVLSITHDLD 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-238 |
2.91e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.99 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 13 GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAvIAYLPQHLLtqdkvtvfeETMKAFEEV 92
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-IDYSRKGLM---------KLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 93 TQmqkeldELNEQLTIRTDYETDDY----MKLIERvsELSEKfysieetnydaeVEKVLKGLGFER-KDftRQTSEFSGG 167
Cdd:PRK13636 88 FQ------DPDNQLFSASVYQDVSFgavnLKLPED--EVRKR------------VDNALKRTGIEHlKD--KPTHCLSFG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 168 WRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAK----AVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-240 |
3.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSFGGTTLF-----SDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAylpqhlltq 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPA--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 dkvtvfeeTMKAFEEVTQMQKELD---ELNEQLTIRTDYETDDYMKLIERVSELSEKFYSIEEtnydaevekVLKGLGFE 153
Cdd:PRK13645 78 --------NLKKIKEVKRLRKEIGlvfQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPE---------LLKLVQLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 154 RKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESiqwLEDFL-------INSAKAVMVISHDRAFVDNI 226
Cdd:PRK13645 141 EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG---EEDFInlferlnKEYKKRIIMVTHNMDQVLRI 217
|
250
....*....|....
gi 1525942895 227 TNRTIEVTMGRIYD 240
Cdd:PRK13645 218 ADEVIVMHEGKVIS 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
330-522 |
3.30e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.39 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaIMN--EIDFEGGLKVGHNAKigYFAQN----QAALLD 403
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNllEMPRSGTLNIAGNHF--DFSKTpsdkAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 404 EN-------------LTVFETidqipLTDGSIKIKDLlgafmfSGDDTTKKVKV-----------------LSGGEKTRL 453
Cdd:PRK11124 82 RNvgmvfqqynlwphLTVQQN-----LIEAPCRVLGL------SKDQALARAEKllerlrlkpyadrfplhLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 454 AMIK-LLLEPvNVLILDEPTNHLD----MKTKDIIKDaLKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRVREH 522
Cdd:PRK11124 151 AIARaLMMEP-QVLLFDEPTAALDpeitAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
330-518 |
3.47e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MN----EIDFEGGLKV-GHNakIGYFAQNQAALL 402
Cdd:PRK14239 8 VSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdlnpEVTITGSIVYnGHN--IYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 403 DENLTVFETIDQIPLTD----------GSIKIKDLLGAFM---FSGDDTTKKVK--------VLSGGEKTRLAMIKLLLE 461
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIyenvvyglrlKGIKDKQVLDEAVeksLKGASIWDEVKdrlhdsalGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 462 PVNVLILDEPTNHLDMKTKDIIKD---ALKDfDGTLILVSH---------DRD--FLDGlvqKVFEFGNKR 518
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEEtllGLKD-DYTMLLVTRsmqqasrisDRTgfFLDG---DLIEYNDTK 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
337-504 |
3.73e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.77 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 337 YGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGGLKVGHNAKIGYFAQNQAALLDENLTVFETIDQ-I 415
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQqI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 416 PLTDGSIKIKDLLGAFMFSGDDTTKKV-----------------KVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMK 478
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVdealtlvdaqhfrhqpiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180
....*....|....*....|....*....
gi 1525942895 479 TKDIIKDALKDFDGT---LILVSHDRDFL 504
Cdd:PRK13638 171 GRTQMIAIIRRIVAQgnhVIISSHDIDLI 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-216 |
3.91e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF--GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKpTTGNVTGPKeaviaylpqhlLTQDKV 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-----------VSWNSV 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TVfEETMKAFEEVTQMQKELDElneqlTIRTDYetDDYmkliERVSElSEKFYSIEETNYDAEVEKVLKGLGFERKDftr 159
Cdd:TIGR01271 1286 TL-QTWRKAFGVIPQKVFIFSG-----TFRKNL--DPY----EQWSD-EEIWKVAEEVGLKSVIEQFPDKLDFVLVD--- 1349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 160 QTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVI 216
Cdd:TIGR01271 1350 GGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
340-499 |
4.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.46 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 340 HVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAiMNEIDFEGGLKVghnakigyFAQNQAALLDENL--------TVFET 411
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKH-MNALLIPSEGKV--------YVDGLDTSDEENLwdirnkagMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 412 ID-QIPLTdgsIKIKDLlgAFMFSG------------DDTTKKVK----------VLSGGEKTRLAMIKLLLEPVNVLIL 468
Cdd:PRK13633 94 PDnQIVAT---IVEEDV--AFGPENlgippeeirervDESLKKVGmyeyrrhaphLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1525942895 469 DEPTNHLD-------MKTkdiIKDALKDFDGTLILVSH 499
Cdd:PRK13633 169 DEPTAMLDpsgrrevVNT---IKELNKKYGITIILITH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
347-526 |
4.42e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIM-NEIDFEGGLKVGHNAKIgyFAQNQAAL------------LDENLTVFETI- 412
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSgNYQPDAGSILIDGQEMR--FASTTAALaagvaiiyqelhLVPEMTVAENLy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 413 -DQIPLTDGSIKIKDL----------LGAFMfsgdDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD 481
Cdd:PRK11288 102 lGQLPHKGGIVNRRLLnyeareqlehLGVDI----DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1525942895 482 I---IKDALKDfDGTLIL-VSHDRDFLDGLVQKVFEFGNKRVREHFEDI 526
Cdd:PRK11288 178 QlfrVIRELRA-EGRVILyVSHRMEEIFALCDAITVFKDGRYVATFDDM 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-218 |
4.64e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 44.84 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 17 FSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT----GPKEAVIAYLPQH--LLTQDKVtVFEETMKafe 90
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvDIRDLNLRWLRSQigLVSQEPV-LFDGTIA--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 91 evtqmqkeldelnEQLTIRTDYETDDymkLIERVSELSE--KFYSIEETNYDAEVEKvlKGlgferkdftrqtSEFSGGW 168
Cdd:cd03249 95 -------------ENIRYGKPDATDE---EVEEAAKKANihDFIMSLPDGYDTLVGE--RG------------SQLSGGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 169 RMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKA--VMVISH 218
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-219 |
5.29e-05 |
|
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: 44.94 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGnvtgpkeaviaylpqhlltqdkvTVFEETmkafEEVTQM-QK 97
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSG-----------------------KVLIDG----QDIAAMsRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 98 ELDELNEQlTIRTDYETddyMKLIERVSELSEKFYSIEETNYDAEV-----EKVLKGLGFErKDFTRQTSEFSGGWRMRI 172
Cdd:cd03294 95 ELRELRRK-KISMVFQS---FALLPHRTVLENVAFGLEVQGVPRAEreeraAEALELVGLE-GWEHKYPDELSGGMQQRV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 173 ELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI----NSAKAVMVISHD 219
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPLIRREMQDELLrlqaELQKTIVFITHD 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
443-499 |
6.11e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 443 KVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDF----DGTLILVSH 499
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-218 |
7.38e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 7 ISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV--------TGPKEAVIAYLpQHL--LTQ 76
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktatRGDRSRFMAYL-GHLpgLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 77 DKVTVfeetmkafeevtqmqKELDELNEQLTIRTDYETDDYMKLIervselsekfysieetnydaevekvlkGLGFERKD 156
Cdd:PRK13543 96 DLSTL---------------ENLHFLCGLHGRRAKQMPGSALAIV---------------------------GLAGYEDT 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 157 FTRQtseFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL---INSAKAVMVISH 218
Cdd:PRK13543 134 LVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsahLRGGGAALVTTH 195
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
328-502 |
8.27e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQ-----KASMVIERGEKVAFVGKNGEGKSTMIK------------AIMNEIDFEGGLKVGHNAK 390
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 391 -----IGYFAQNQAALLDENlTVFETIDQIPLTDGS------IKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLL 459
Cdd:PRK13645 87 rlrkeIGLVFQFPEYQLFQE-TIEKDIAFGPVNLGEnkqeayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1525942895 460 LEPVNVLILDEPTNHLDMKTKDIIKDAL----KDFDGTLILVSHDRD 502
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMD 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
333-477 |
9.20e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 333 LTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-LKV-GHNAKIGYFAQNQAAL-----LDEN 405
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGqIQIdGKTATRGDRSRFMAYLghlpgLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 406 LTVFETI-----------DQIPltDGSIKIKDLLGAfmfsgDDTTkkVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNH 474
Cdd:PRK13543 97 LSTLENLhflcglhgrraKQMP--GSALAIVGLAGY-----EDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
...
gi 1525942895 475 LDM 477
Cdd:PRK13543 168 LDL 170
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-218 |
9.64e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.31 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNISVSFGG------TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVtgpkeaviaYLpQHLL 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------YV-DGLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 75 TQDKVTVFEETMKAfEEVTQmqkeldELNEQLtIRTDYETDdymklierVSELSEKFySIEETNYDAEVEKVLKGLG-FE 153
Cdd:PRK13633 74 TSDEENLWDIRNKA-GMVFQ------NPDNQI-VATIVEED--------VAFGPENL-GIPPEEIRERVDESLKKVGmYE 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 154 RKDFTRQTseFSGGWRMRIELAKILLKKPDLILLDEPTNHMD----IESIQWLEDFLINSAKAVMVISH 218
Cdd:PRK13633 137 YRRHAPHL--LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
444-499 |
9.66e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.12 E-value: 9.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1525942895 444 VLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDFDGTLILVSH 499
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
330-499 |
9.68e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 44.26 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI--MNeiDFEGGLKV-------GHN------------ 388
Cdd:COG1117 14 VRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMN--DLIPGARVegeilldGEDiydpdvdvvelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 389 AKIGYFAQ-----------N-------------------------QAALLDEnltvfetidqipltdgsikIKDLLGAFM 432
Cdd:COG1117 92 RRVGMVFQkpnpfpksiydNvayglrlhgikskseldeiveeslrKAALWDE-------------------VKDRLKKSA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 433 FSgddttkkvkvLSGGEKTRLAMIKLL-LEPvNVLILDEPTNHLD----MKTKDIIKDaLKDfDGTLILVSH 499
Cdd:COG1117 153 LG----------LSGGQQQRLCIARALaVEP-EVLLMDEPTSALDpistAKIEELILE-LKK-DYTIVIVTH 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
328-505 |
1.12e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.73 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 328 VMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEGG-----------LKVGHNAK--IGYF 394
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedislLPLHARARrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 395 AQNQA-----ALLDENLTVFETIDQIPLTDGSIKIKDLLGAFMFSGDDTTKKvKVLSGGEKTRLAMIKLLLEPVNVLILD 469
Cdd:PRK10895 84 PQEASifrrlSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1525942895 470 EPTNHLD----MKTKDIIKDaLKDFDGTLILVSHD-RDFLD 505
Cdd:PRK10895 163 EPFAGVDpisvIDIKRIIEH-LRDSGLGVLITDHNvRETLA 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
327-476 |
1.16e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 327 PVMVEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEIDFEG--GLKVGHNAKI--------GYFAQ 396
Cdd:PLN03211 68 KPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPtkqilkrtGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 397 NQaaLLDENLTVFETIDQIPL----TDGSIKIKDLLGAFMFSGDDTTKK---------VKVLSGGEKTRLAMIKLLLEPV 463
Cdd:PLN03211 148 DD--ILYPHLTVRETLVFCSLlrlpKSLTKQEKILVAESVISELGLTKCentiignsfIRGISGGERKRVSIAHEMLINP 225
|
170
....*....|...
gi 1525942895 464 NVLILDEPTNHLD 476
Cdd:PLN03211 226 SLLILDEPTSGLD 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-58 |
1.38e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 1 MINVNNISVSFG-GTTLF--------SDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV 58
Cdd:PRK15112 4 LLEVRNLSKTFRyRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-219 |
1.55e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 30 IALMGKNGAGKSTILKIIADVakpttgnVTGPKEAVIAYLPQHLLTQDKVT----VFEETMKAFEeVTQMQKELDE-LNE 104
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYA-------LYGKARSRSKLRSDLINVGSEEAsvelEFEHGGKRYR-IERRQGEFAEfLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 105 QLTIRTD-----YETDDYMKLIERVSELSEkfySIEETNYDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMRIELAKILl 179
Cdd:COG0419 98 KPSERKEalkrlLGLEIYEELKERLKELEE---ALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1525942895 180 kkpDLIlLDepTNHMDIESIQWLEDFLinsaKAVMVISHD 219
Cdd:COG0419 174 ---SLI-LD--FGSLDEERLERLLDAL----EELAIITHV 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
445-501 |
1.66e-04 |
|
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: 44.43 E-value: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 445 LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDALKDfdgtlilVSHDR 501
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE-------VARGR 544
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-59 |
1.78e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.91 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 1 MINVNNISVSF----GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVT 59
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL 63
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
445-502 |
1.81e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 1.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 445 LSGGEKTRLAMIKLL-LEPvNVLILDEPTNHLD-MKTKDIIK--DALKDFDGTLILVSHDRD 502
Cdd:PRK13651 166 LSGGQKRRVALAGILaMEP-DFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHDLD 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
347-502 |
1.90e-04 |
|
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: 43.22 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 347 SMVIERGEKVAFVGKNGEGKSTMIKAIMN-EIDFEGGLKV--------GHNAKIGYfaQNQAAL----LDEN--LTVFET 411
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILegkqitepGPDRMVVF--QNYSLLpwltVRENiaLAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 412 IDQIPLTDGSIKIKDLLgAFMFSGDDTTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKDAL---- 487
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHI-ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiw 161
|
170
....*....|....*
gi 1525942895 488 KDFDGTLILVSHDRD 502
Cdd:TIGR01184 162 EEHRVTVLMVTHDVD 176
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
165-238 |
2.28e-04 |
|
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: 42.03 E-value: 2.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 165 SGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSA---KAVMVISHDRAFVDNITNRtIEVtM--GRI 238
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDR-ILV-MyeGRI 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-50 |
2.58e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 2.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1525942895 6 NISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADV 50
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV 50
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-218 |
2.84e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 1 MINVNNIS-VSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQhlltqdkv 79
Cdd:TIGR00954 451 GIKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ-------- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 tvfEETMKafeevtqmqkeLDELNEQLtIRTDyetddymklieRVSELSEKFYSieetnyDAEVEKVL----------KG 149
Cdd:TIGR00954 523 ---RPYMT-----------LGTLRDQI-IYPD-----------SSEDMKRRGLS------DKDLEQILdnvqlthileRE 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 150 LGFER----KDftrqtsEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIEsiqwLEDFLINSAK----AVMVISH 218
Cdd:TIGR00954 571 GGWSAvqdwMD------VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCRefgiTLFSVSH 637
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-61 |
3.15e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 3.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 1 MINVNNISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIAdvakpttGNVTGP 61
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALA-------GDLTGG 54
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-58 |
3.56e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 3.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1525942895 6 NISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV 58
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-219 |
3.64e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkeaviaylpqhlltQDKVTVFEETMKAFEEVTQMQke 98
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL----------------IDGVDIAKISDAELREVRRKK-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 99 ldelneqltIRTDYETddyMKLIERVSELSEKFYSIEETNYDAEVEK-----VLKGLGFERKDFTrQTSEFSGGWRMRIE 173
Cdd:PRK10070 108 ---------IAMVFQS---FALMPHMTVLDNTAFGMELAGINAEERRekaldALRQVGLENYAHS-YPDELSGGMRQRVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1525942895 174 LAKILLKKPDLILLDEPTNHMDIESIQWLEDFLI----NSAKAVMVISHD 219
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVklqaKHQRTIVFISHD 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
330-373 |
6.02e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.84 E-value: 6.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1525942895 330 VEELTKTYGDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAI 373
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL 52
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-195 |
8.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.62 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 20 VTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEAVIAYLPQHLLTQDKVtVFEETMKAFEEVTqmqkel 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGM-VFQNPDNQFVGAT------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 100 deLNEQLTIRTDYETDDYMKLIERVSELSekfysieetnydaevekvlkgLGFERKDF-TRQTSEFSGGWRMRIELAKIL 178
Cdd:PRK13642 99 --VEDDVAFGMENQGIPREEMIKRVDEAL---------------------LAVNMLDFkTREPARLSGGQKQRVAVAGII 155
|
170
....*....|....*..
gi 1525942895 179 LKKPDLILLDEPTNHMD 195
Cdd:PRK13642 156 ALRPEIIILDESTSMLD 172
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
331-519 |
8.89e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 41.33 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 331 EELTKTY-GDHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKaimneiDFEGGLKvghnAKIGYFAQNQAALLDENL--- 406
Cdd:PRK13652 7 RDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFR------HFNGILK----PTSGSVLIRGEPITKENIrev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 407 -----TVFETID-QI--PLTDGSIKikdlLGAFMFSGDDTTKKVKV-------------------LSGGEKTRLAMIKLL 459
Cdd:PRK13652 77 rkfvgLVFQNPDdQIfsPTVEQDIA----FGPINLGLDEETVAHRVssalhmlgleelrdrvphhLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525942895 460 LEPVNVLILDEPTNHLD-MKTKDII---KDALKDFDGTLILVSHDRDFLDGLVQKVFEFGNKRV 519
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDpQGVKELIdflNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-196 |
9.47e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.38 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 13 GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpKEAVIAYLPQhlltqdkvtvFEETMKAfeev 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQ----------FSWIMPG---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 93 tqmqkeldELNEQLTIRTDYETDDYMKLIeRVSELSEKFYSIEETNYDAEVEKVLKglgferkdftrqtseFSGGWRMRI 172
Cdd:cd03291 113 --------TIKENIIFGVSYDEYRYKSVV-KACQLEEDITKFPEKDNTVLGEGGIT---------------LSGGQRARI 168
|
170 180
....*....|....*....|....
gi 1525942895 173 ELAKILLKKPDLILLDEPTNHMDI 196
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-500 |
1.04e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.19 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 339 DHVVFQKASMVIERGEKVAFVGKNGEGKSTMIKAIMNEID-FEGGLKVghNAKIGYFAQN-----------------QAA 400
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKV--DGKVLYFGKDifqidaiklrkevgmvfQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 401 LLDENLTVFETIdQIPLTDGSIKIKDLLGAFMfsgDDTTKKVKV--------------LSGGEKTRLAMIKLLLEPVNVL 466
Cdd:PRK14246 100 NPFPHLSIYDNI-AYPLKSHGIKEKREIKKIV---EECLRKVGLwkevydrlnspasqLSGGQQQRLTIARALALKPKVL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1525942895 467 ILDEPTNHLDMKTKDIIKDALKDFDG--TLILVSHD 500
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
442-500 |
1.10e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 442 VKVLSGGEKTRLAMIKLLlepvnVLILDepTNHLDMKTKDIIKDALKDfdgtLILVSHD 500
Cdd:COG0419 156 IETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
165-224 |
1.20e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.28 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 165 SGGWRM------RIELAKILLKKPDLILLDEPTNHMDIESIQW-LEDfLINSAKA-----VMVISHDRAFVD 224
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAE-IIEERKSqknfqLIVITHDEELVD 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-507 |
1.30e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 40.11 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 342 VFQKASMVIERGEKVAFVGKNGEGKSTMIKAIM-------NEIDFEG----GLKVG--HNAKIGYFA---QNQAALLDen 405
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFglrppasGEITLDGkpvtRRSPRdaIRAGIAYVPedrKREGLVLD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 406 LTVFETIdqipltdgsikikdLLGAFmfsgddttkkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKD 485
Cdd:cd03215 93 LSVAENI--------------ALSSL-------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180
....*....|....*....|....*
gi 1525942895 486 ALKDF--DGT-LILVSHDRDFLDGL 507
Cdd:cd03215 146 LIRELadAGKaVLLISSELDELLGL 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
165-238 |
1.40e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.35 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1525942895 165 SGGWRMRIELAKILLKKPDLILLDEPTNHMDIES---IQWLEDFLINSAKAVMVISHDRAFVDNITNRTIEVTMGRI 238
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-67 |
1.80e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 1.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1525942895 19 DVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKE-AVIA 67
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIA 91
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
350-502 |
1.80e-03 |
|
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: 39.93 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 350 IERGEKVAFVGKNGEGKSTMIkaiMNEIDFEGGLKvgHNAKIGYFAQNQAALLD-------ENLTVFETIDQIPL----- 417
Cdd:cd03270 18 IPRNKLVVITGVSGSGKSSLA---FDTIYAEGQRR--YVESLSAYARQFLGQMDkpdvdsiEGLSPAIAIDQKTTsrnpr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 418 -TDGSI-KIKDLLGaFMFSGDDTTKKVKVL-----------------SGGEKTRLAMIKLL-LEPVNVL-ILDEPTNHLD 476
Cdd:cd03270 93 sTVGTVtEIYDYLR-LLFARVGIRERLGFLvdvglgyltlsrsaptlSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLH 171
|
170 180
....*....|....*....|....*....
gi 1525942895 477 MKTKDIIKDALK---DFDGTLILVSHDRD 502
Cdd:cd03270 172 PRDNDRLIETLKrlrDLGNTVLVVEHDED 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
349-502 |
1.85e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.39 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 349 VIERGEKVAFVGKNGEGKSTMIKAiMNEI--DFEGGLKVGHNA---------------KIGY---FAQNQaaLLDEnlTV 408
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQH-LNGLlqPTSGTVTIGERVitagkknkklkplrkKVGIvfqFPEHQ--LFEE--TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 409 FETIDQIPLT------DGSIKIKDLLGAFMFSGDDTTKKVKVLSGGEKTRLAMIKLL-LEPvNVLILDEPTNHLDMKTKD 481
Cdd:PRK13634 104 EKDICFGPMNfgvseeDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLaMEP-EVLVLDEPTAGLDPKGRK 182
|
170 180
....*....|....*....|....*
gi 1525942895 482 IIKDAL----KDFDGTLILVSHDRD 502
Cdd:PRK13634 183 EMMEMFyklhKEKGLTTVLVTHSME 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-58 |
1.95e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 1 MINVNNISVSFGG----TTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNV 58
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
409-499 |
1.99e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 409 FETIDQIPLTDGSIK--IKDLLGAF-----MFSGDDTTKkvkvLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKD 481
Cdd:PTZ00265 541 YQTIKDSEVVDVSKKvlIHDFVSALpdkyeTLVGSNASK----LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
90 100
....*....|....*....|..
gi 1525942895 482 IIKDALKDFDGT----LILVSH 499
Cdd:PTZ00265 617 LVQKTINNLKGNenriTIIIAH 638
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-219 |
2.40e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 134 IEETNYDAEV---------EKV--LKGLGFERKDFTRQTSEFSGGWRMRIELAKILL---KKPDLILLDEPTNHM---DI 196
Cdd:PRK00635 769 LEMTAYEAEKffldepsihEKIhaLCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDI 848
|
90 100
....*....|....*....|...
gi 1525942895 197 ESIQWLEDFLINSAKAVMVISHD 219
Cdd:PRK00635 849 KALIYVLQSLTHQGHTVVIIEHN 871
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-223 |
2.64e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 15 TLFSDVTFSINENDKIALMGKNGAGKSTILKIIADvakpTTGNVTGPKEAVIAY--LPQHlltqdkvtvfeETMKAFEEV 92
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS----NTDGFHIGVEGVITYdgITPE-----------EIKKHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 93 TQMQKELDELNEQLTIrtdYETDDYMKLIE----RVSELSEKFYSIEETNYdaevekVLKGLGFerkDFTRQT---SEF- 164
Cdd:TIGR00956 140 VVYNAETDVHFPHLTV---GETLDFAARCKtpqnRPDGVSREEYAKHIADV------YMATYGL---SHTRNTkvgNDFv 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 165 ---SGGWRMRIELAKILLKKPDLILLDEPTNHMDieSIQWLEdfLINSAKAVMVISHDRAFV 223
Cdd:TIGR00956 208 rgvSGGERKRVSIAEASLGGAKIQCWDNATRGLD--SATALE--FIRALKTSANILDTTPLV 265
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-206 |
2.65e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.77 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 6 NISVSFGGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTgpkEAVIAYLPQHLLTQ--DKVTVFE 83
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRV---EGKVTFHGKNLYAPdvDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 84 ETMKAFEEVTQMQKELdelneqltirtdYETDDYMKLIERVselsekfysieETNYDAEVEKVLK--GLGFERKDFTRQT 161
Cdd:PRK14243 92 RIGMVFQKPNPFPKSI------------YDNIAYGARINGY-----------KGDMDELVERSLRqaALWDEVKDKLKQS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1525942895 162 -SEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFL 206
Cdd:PRK14243 149 gLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELM 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
446-518 |
3.06e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 446 SGGEKTRLaMIK--LLLEPvNVLILDEPTNHLDMKTKDIIKDAL----KDFDGTLILVSHDRDFLDGLVQKVF------- 512
Cdd:PRK09473 163 SGGMRQRV-MIAmaLLCRP-KLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITHDLGVVAGICDKVLvmyagrt 240
|
....*..
gi 1525942895 513 -EFGNKR 518
Cdd:PRK09473 241 mEYGNAR 247
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-194 |
3.10e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 17 FSDVTFSINEnDKIALMGKNGAGKSTILKIIADVAKPTTG------------NVTGPKEAVIAYLPQHLLtqdkvTVFEE 84
Cdd:COG3593 14 IKDLSIELSD-DLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgdDPDLPEIEIELTFGSLLS-----RLLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 85 TMKAfEEVTQMQKELDELNEQLtirtDYETDDYMKLIERVSELSEKFYSIEETNYDAEVEKVLKGLGFERKD-FTRQTSE 163
Cdd:COG3593 88 LLKE-EDKEELEEALEELNEEL----KEALKALNELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDgKELPLDR 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1525942895 164 FSGG--WRMRIELAKILL-----KKPDLILLDEPTNHM 194
Cdd:COG3593 163 LGSGfqRLILLALLSALAelkraPANPILLIEEPEAHL 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
445-502 |
3.56e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.83 E-value: 3.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525942895 445 LSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTK----DIIKDAlKDFDGTLILVSHDRD 502
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhemmQLILDA-KANNKTVFVITHTME 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-488 |
4.09e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 349 VIERGEKVAFVGKNGEGKSTMIKAIMNEIDfegGLKVGHNAKIGY----------FAQNQAALLDEN------LTVFETI 412
Cdd:TIGR00956 83 LIKPGELTVVLGRPGSGCSTLLKTIASNTD---GFHIGVEGVITYdgitpeeikkHYRGDVVYNAETdvhfphLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 413 D-----QIPLTDGSI--------KIKDLLGAFMfsGDDTTKKVKV-------LSGGEKTRLAMIKLLLEPVNVLILDEPT 472
Cdd:TIGR00956 160 DfaarcKTPQNRPDGvsreeyakHIADVYMATY--GLSHTRNTKVgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170
....*....|....*..
gi 1525942895 473 NHLDMKTK-DIIKdALK 488
Cdd:TIGR00956 238 RGLDSATAlEFIR-ALK 253
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-216 |
4.34e-03 |
|
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: 39.07 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 2 INVNNISVSF--GGTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKpTTGNVTGPKeaviaylpqhlLTQDKV 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-----------VSWNSV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 80 TVfEETMKAFEEVTQ--------MQKELDELNEQltirTDYEtddymklIERVSelsekfysiEETNYDAEVEKVLKGLG 151
Cdd:cd03289 71 PL-QKWRKAFGVIPQkvfifsgtFRKNLDPYGKW----SDEE-------IWKVA---------EEVGLKSVIEQFPGQLD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 152 FERKDftrQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIESIQWLEDFLINSAKAVMVI 216
Cdd:cd03289 130 FVLVD---GGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVI 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-224 |
4.36e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.46 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 149 GLGFERKDftRQTSEFSGGWRMRIELAKILLK--KPDLILLDEPTNHMDIESI-QWLEDF--LINSAKAVMVISHDRAFV 223
Cdd:cd03238 75 GLGYLTLG--QKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDInQLLEVIkgLIDLGNTVILIEHNLDVL 152
|
.
gi 1525942895 224 D 224
Cdd:cd03238 153 S 153
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
445-505 |
4.46e-03 |
|
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: 39.67 E-value: 4.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 445 LSGGEKTRlAMIK--LLLEPvNVLILDEPTNHLDMKTK----DIIKDALKDFDGTLILVSHD----RDFLD 505
Cdd:COG4172 157 LSGGQRQR-VMIAmaLANEP-DLLIADEPTTALDVTVQaqilDLLKDLQRELGMALLLITHDlgvvRRFAD 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
159-195 |
4.77e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.33 E-value: 4.77e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1525942895 159 RQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMD 195
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
360-498 |
5.48e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 360 GKNGEGKSTMIKAIMNEIDFEGGLKVGHNAKI--------GYFAQNQAALLDenLTVFETI-------DQIPLTDGSI-- 422
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpycTYIGHNLGLKLE--MTVFENLkfwseiyNSAETLYAAIhy 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1525942895 423 -KIKDLLgafmfsgddtTKKVKVLSGGEKTRLAMIKLLLEPVNVLILDEPTNHLDMKTKDIIKD--ALKDFDGTLILVS 498
Cdd:PRK13541 111 fKLHDLL----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNliVMKANSGGIVLLS 179
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
445-524 |
5.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 445 LSGGEKT------RLAMIKLLLEPVNVLILDEPTNHLD----MKTKDIIKDALKDFDgTLILVSHD---RDFLDGLVQKV 511
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIP-QVIIVSHDeelKDAADYVIRVS 867
|
90
....*....|...
gi 1525942895 512 FEFGNKRVREHFE 524
Cdd:PRK03918 868 LEGGVSKVEVVSL 880
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-71 |
7.24e-03 |
|
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: 37.83 E-value: 7.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1525942895 2 INVNNISVSFG-----GTTLFSDVTFSINENDKIALMGKNGAGKSTILKIIADVAKPTTGNVTGPKEavIAYLPQ 71
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQ 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
118-258 |
9.85e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.97 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525942895 118 MKLIERVSELSEKFYSIeetnyDAEVEKVLKGLGFERKDFTRQTSEFSGGWRMRIELAKILLKKPDLILLDEPTNHMDIE 197
Cdd:smart00382 20 RALARELGPPGGGVIYI-----DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525942895 198 SIQWLEDFLINSAKAVMVISHDRAFVDnITNRTIEVTmgriydykakySHYLQLRADRRIH 258
Cdd:smart00382 95 QEALLLLLEELRLLLLLKSEKNLTVIL-TTNDEKDLG-----------PALLRRRFDRRIV 143
|
|
| |
