|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-557 |
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: 562.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlPLDQWGWMGQQTEADEAVFTHAY 88
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLRIGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 VEEGCPEHYAAKRRLKELEAQMQDaaapcMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGRELWDQPLGQLSGG 168
Cdd:COG0488 82 VLDGDAELRALEAELEELEAKLAE-----PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 169 QKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTGCRKYRGGYTE 248
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 249 YTRQKELELRTQEQLYRKQQLLREQLEESIRTYRQwfhqgekNAQMAevpiqrgyfqgragahvSRMNAKMKELERLEgn 328
Cdd:COG0488 237 YLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRA-------KARKA-----------------KQAQSRIKALEKLE-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 329 RVEKPREAAHLKVKLSASDFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAG 408
Cdd:COG0488 291 REEPPRRDKTVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 409 KVRQHPQTSIGYFSQELEHLDDGVTLLDSLLTL-PAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSG 487
Cdd:COG0488 371 TVKLGETVKIGYFDQHQEELDPDKTVLDELRDGaPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 488 ANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERSpIAFSGTYDEYAE 557
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGV-REYPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-557 |
1.50e-99 |
|
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: 314.18 E-value: 1.50e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtleLDKGSVERRLPLDQW--GWMGQQTEADEAVFTHAYVEEGC 93
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKDFNGEARPQPGIkvGYLPQEPQLDPTKTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 PEHYAAKRRLKELEAQMQDAAAPcMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGRelWDQPLGQLSGGQKTRA 173
Cdd:TIGR03719 94 AEIKDALDRFNEISAKYAEPDAD-FDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPP--WDADVTKLSGGERRRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTGCRKYRGGYTEYTRQK 253
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 254 E--LELRTQEQLYRKQQLLREqLEesirtyrqWFHQGEKNAQmaevpiqrgyfqgragahvSRMNAKMKELERLEGNRVE 331
Cdd:TIGR03719 251 QkrLEQEEKEESARQKTLKRE-LE--------WVRQSPKGRQ-------------------AKSKARLARYEELLSQEFQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 332 KPREAAHLKV----KLSAsdfasrSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAA 407
Cdd:TIGR03719 303 KRNETAEIYIppgpRLGD------KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 408 GKVRQHPQTSIGYFSQELEHLDDGVTL-------LDsLLTLpAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAF 480
Cdd:TIGR03719 377 GTIEIGETVKLAYVDQSRDALDPNKTVweeisggLD-IIKL-GKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHL 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 481 LKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERSPIAFSGTYDEYAE 557
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEE 531
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-562 |
1.24e-89 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 287.56 E-value: 1.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-----ER--RLPLDQWGWMgQQ 76
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsldpnERlgKLRQDQFAFE-EF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 TEADEAVFTHAyveegcpEHYAAKrrlkeleaQMQDA--AAPCMESllADYQEAAE---RYMGLDGYHWETQVERKLLQL 151
Cdd:PRK15064 80 TVLDTVIMGHT-------ELWEVK--------QERDRiyALPEMSE--EDGMKVADlevKFAEMDGYTAEARAGELLLGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 152 GLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCL 231
Cdd:PRK15064 143 GIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 232 VELTPTGCRKYRGGYTEYtrqkeLELRTQeqlyrkqqlLREQLEESirtyrqwfhQGEKNAQMAEvpIQRgyFQGRAGAH 311
Cdd:PRK15064 223 ADLDYGELRVYPGNYDEY-----MTAATQ---------ARERLLAD---------NAKKKAQIAE--LQS--FVSRFSAN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 312 VSRmnAK-----MKELERLEGNRVeKPREAAHLKVKLSASDFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLG 386
Cdd:PRK15064 276 ASK--AKqatsrAKQIDKIKLEEV-KPSSRQNPFIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 387 PNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEH-LDDGVTLLD--SLLTLPAMTQTQARTILGCFLFSGEEV 463
Cdd:PRK15064 353 ENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdFENDLTLFDwmSQWRQEGDDEQAVRGTLGRLLFSQDDI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 464 RKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAER 543
Cdd:PRK15064 433 KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
570
....*....|....*....
gi 1844953743 544 SpIAFSGTYDEYaeasLAS 562
Cdd:PRK15064 513 V-VDFSGTYEEY----LRS 526
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-601 |
4.42e-89 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 289.16 E-value: 4.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 18 PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER-------RLPldqwgwmgQQTEADEAVFTHAYVE 90
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivaRLQ--------QDPPRNVEGTVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 EGCpEHYAAKrrLKELEAQMQDAAAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGRelwDQPLGQLSGGQK 170
Cdd:PRK11147 89 EGI-EEQAEY--LKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP---DAALSSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 171 TRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTGCRKYRGGYTEYT 250
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 251 RQKELELRTQEqlyrkqqllrEQLEESIRTYRQ---WFHQGEKnaqmaevpIQRGYFQGRAGAhvsrmnakMKELERLEG 327
Cdd:PRK11147 243 LEKEEALRVEE----------LQNAEFDRKLAQeevWIRQGIK--------ARRTRNEGRVRA--------LKALRRERS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 328 NRVEKPReaahlKVKLSASDfASRS--LV-RLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQ 404
Cdd:PRK11147 297 ERREVMG-----TAKMQVEE-ASRSgkIVfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 405 PAAGKVRQHPQTSIGYFSQELEHLDDGVTLLDSLltlpA------MTQTQARTILGC---FLFSGEEVRKRIGDLSMGER 475
Cdd:PRK11147 371 ADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNL----AegkqevMVNGRPRHVLGYlqdFLFHPKRAMTPVKALSGGER 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 476 CRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERSPIAFSGTY--- 552
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYhda 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 553 ------------DEYAEASLASESSPEQLARA------NERRQLElTLAQLMSEgawsPENAPAQLQ 601
Cdd:PRK11147 527 rqqqaqylalkqPAVKKKEEAAAPKAETVKRSskklsyKLQRELE-QLPQLLED----LEAEIEALQ 588
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-557 |
6.80e-87 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 280.85 E-value: 6.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtleLDKGSV-ERRL-PLDQWGWMGQQTEADEAVFTHAYVEEGC 93
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKEFEgEARPaPGIKVGYLPQEPQLDPEKTVRENVEEGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 PEHYAAKRRLKELEAQMQDAAAPcMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGRelWDQPLGQLSGGQKTRA 173
Cdd:PRK11819 96 AEVKAALDRFNEIYAAYAEPDAD-FDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPP--WDAKVTKLSGGERRRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTGCRKYRGGYTEYTRQK 253
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 254 E--LELRTQEQLYRKQQLLREqLEesirtyrqWFHQGEKnAQmaevpiqrgyfQGRAGAHVSR---MNAK--MKELERLE 326
Cdd:PRK11819 253 AkrLAQEEKQEAARQKALKRE-LE--------WVRQSPK-AR-----------QAKSKARLARyeeLLSEeyQKRNETNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 327 ---------GNRVekpREAAHLkvklsasdfaSRSlvrleraafrYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLK 397
Cdd:PRK11819 312 ifippgprlGDKV---IEAENL----------SKS----------FGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 398 LLVGELQPAAGKVRQHPQTSIGYFSQELEHLDDGVTL-------LDsLLTLpAMTQTQARTILGCFLFSGEEVRKRIGDL 470
Cdd:PRK11819 369 MITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVweeisggLD-IIKV-GNREIPSRAYVGRFNFKGGDQQKKVGVL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 471 SMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERSPIAFSG 550
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEG 526
|
....*..
gi 1844953743 551 TYDEYAE 557
Cdd:PRK11819 527 NFQEYEE 533
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-555 |
9.84e-76 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 253.94 E-value: 9.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 27 VNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrLPLD-QWGWMGQQTEADEaVFTHAYVEEGcpehyaaKRRLKE 105
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYT--FPGNwQLAWVNQETPALP-QPALEYVIDG-------DREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 106 LEAQMQDAAApcmeslLADYQEAAERYMGLDGYH-WETQVERKLLQLGLG--RELWDQPLGQLSGGQKTRAQLARLMVRE 182
Cdd:PRK10636 94 LEAQLHDANE------RNDGHAIATIHGKLDAIDaWTIRSRAASLLHGLGfsNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 183 PQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTGCRKYRGGYTEYTRQKELELRTQEQ 262
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 263 LYRKQQLLREQLEESIRTYRQWFHQGeKNAQmaevpiqrgyfqgragahvsrmnAKMKELERLE---GNRVEKPreaahL 339
Cdd:PRK10636 248 MYESQQERVAHLQSYIDRFRAKATKA-KQAQ-----------------------SRIKMLERMEliaPAHVDNP-----F 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 340 KVKLSASDFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIG 419
Cdd:PRK10636 299 HFSFRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 420 YFSQ-ELEHLDDGVTLLDSLLTL-PAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPT 497
Cdd:PRK10636 379 YFAQhQLEFLRADESPLQHLARLaPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 498 NYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKlATKLLWLSAERSPIAFSGTYDEY 555
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGALVVVSHDRHLLRS-TTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-555 |
7.26e-64 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 223.58 E-value: 7.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAgtLELDKG--------SVERRLpldqwgwMGQQTEADEAVF--- 84
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGipkncqilHVEQEV-------VGDDTTALQCVLntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 ---THAYVEEGcpeHYAAKRRLKELEAQMQDAAAPCMESLLAD-----YQEAAERYMGLDGYHWETQVERKLLQLGLGRE 156
Cdd:PLN03073 260 ierTQLLEEEA---QLVAQQRELEFETETGKGKGANKDGVDKDavsqrLEEIYKRLELIDAYTAEARAASILAGLSFTPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 157 LWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTP 236
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 237 TGCRKYRGGYTEYTRQKELELRTQEQLYRKQQLLREQLEESIRTYRQwfhqgekNAQMAevpiqrgyfqgragahvSRMN 316
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRY-------NAKRA-----------------SLVQ 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 317 AKMKELERLEgnRVEKPREAAHLKVKL-SASDFASRSLVRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTT 394
Cdd:PLN03073 473 SRIKALDRLG--HVDAVVNDPDYKFEFpTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKST 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 395 LLKLLVGELQPAAGKVRQHPQTSIGYFSQ-ELEHLDDGVT-LLDSLLTLPAMTQTQARTILGCFLFSGEEVRKRIGDLSM 472
Cdd:PLN03073 551 ILKLISGELQPSSGTVFRSAKVRMAVFSQhHVDGLDLSSNpLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSG 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 473 GERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKlATKLLWLSAERSPIAFSGTY 552
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG-SVDELWVVSEGKVTPFHGTF 709
|
...
gi 1844953743 553 DEY 555
Cdd:PLN03073 710 HDY 712
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-252 |
9.88e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 199.91 E-value: 9.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 3 LLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmGQQTEadea 82
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------GETVK---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 vftHAYVeegcpehyaakrrlkeleAQMQDAAAPCMeSLLADYQEAAErymglDGYhwETQVeRKLLQ-LGLGRELWDQP 161
Cdd:COG0488 380 ---IGYF------------------DQHQEELDPDK-TVLDELRDGAP-----GGT--EQEV-RGYLGrFLFSGDDAFKP 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 162 LGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTGCRK 241
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
250
....*....|.
gi 1844953743 242 YRGGYTEYTRQ 252
Cdd:COG0488 510 YPGGYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
354-540 |
5.62e-54 |
|
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: 180.72 E-value: 5.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQelehlddgvt 433
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 434 lldslltlpamtqtqartilgcflfsgeevrkrigdLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALL 513
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180
....*....|....*....|....*..
gi 1844953743 514 RYPGAMVIVSHDRFFIRKLATKLLWLS 540
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELE 141
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
356-580 |
4.60e-53 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 189.89 E-value: 4.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 356 LERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEhLDDGVTLL 435
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP-LDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 436 D-----------------SLLTLPAMT----------------------QTQARTILGCFLFSGEEVRKRIGDLSMGERC 476
Cdd:COG0488 80 DtvldgdaelraleaeleELEAKLAEPdedlerlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 477 RLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERSpIAFSGTYDEYA 556
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL-TLYPGNYSAYL 238
|
250 260
....*....|....*....|....
gi 1844953743 557 EASLASEsspEQLARANERRQLEL 580
Cdd:COG0488 239 EQRAERL---EQEAAAYAKQQKKI 259
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-238 |
3.96e-50 |
|
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: 170.32 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqWGwmgqqteadeAVF 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------WG----------STV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAYVEegcpehyaakrrlkeleaqmqdaaapcmeslladyqeaaerymgldgyhwetqverkllqlglgrelwdqplgQ 164
Cdd:cd03221 64 KIGYFE-------------------------------------------------------------------------Q 70
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTPTG 238
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-256 |
9.36e-40 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 152.74 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldQW------GWMGQQTEADea 82
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------KWsenaniGYYAQDHAYD-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 vfthayveegcpehYAAKRRLKELEAQmqdaaapcmeslladyqeaaerymgldgyhWETQVERKLLQLG-LGRELWDQ- 160
Cdd:PRK15064 395 --------------FENDLTLFDWMSQ------------------------------WRQEGDDEQAVRGtLGRLLFSQd 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 161 ----PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVELTP 236
Cdd:PRK15064 431 dikkSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITP 510
|
250 260
....*....|....*....|
gi 1844953743 237 TGCRKYRGGYTEYTRQKELE 256
Cdd:PRK15064 511 DGVVDFSGTYEEYLRSQGIE 530
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-229 |
1.54e-35 |
|
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: 132.60 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQ-QTEADEA 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL---------WNGEpIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 VFTH-AYVeegcpEHYAA-KRRLkeleaqmqdaaapcmeSLLadyqEAAERYMGLDGYHW-ETQVERKLLQLGLGReLWD 159
Cdd:COG4133 73 YRRRlAYL-----GHADGlKPEL----------------TVR----ENLRFWAALYGLRAdREAIDEALEAVGLAG-LAD 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYP---GTVVFVSHDRHFMDRVAT 229
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARV 199
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-231 |
1.15e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.97 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER--RLPLDQWGWMG---QQTEADEAV-FTha 87
Cdd:COG1121 16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgKPPRRARRRIGyvpQRAEVDWDFpIT-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 88 yVEE----GCPEHYAAKRRLKEleaqmqdaaapcmesllADYQeaaerymgldgyhwetQVERKLLQLGLGrELWDQPLG 163
Cdd:COG1121 94 -VRDvvlmGRYGRRGLFRRPSR-----------------ADRE----------------AVDEALERVGLE-DLADRPIG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWL-----EvwLRAYPGTVVFVSHD----RHFMDRVAtCL 231
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALyellrE--LRREGKTILVVTHDlgavREYFDRVL-LL 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-228 |
3.72e-32 |
|
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: 124.77 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQW---------GWMGQQTEADE 81
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV--LLdgrDLASLsrrelarriAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AvFThayVEE----GCPEHYAAKRRLKEleaqmQDAAApcmeslladyqeaaerymgldgyhwetqVERKLLQLGLGrEL 157
Cdd:COG1120 89 G-LT---VRElvalGRYPHLGLFGRPSA-----EDREA----------------------------VEEALERTGLE-HL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 158 WDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEV---WLRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:COG1120 131 ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHqLEVLELlrrLARERGRTVVMVLHDlnlaARYADRLV 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
353-543 |
5.44e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.19 E-value: 5.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR----------QHPQTSIGYFS 422
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdarEDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 423 QELEhLDDGVTLLDSL-----LTLPAMTQTQARTILGCFLFSGEEvRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPT 497
Cdd:COG4133 82 HADG-LKPELTVRENLrfwaaLYGLRADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1844953743 498 NYLDIDSRERIEQALLRYP--GAMVIV-SHDRFFIRklATKLLWLSAER 543
Cdd:COG4133 160 TALDAAGVALLAELIAAHLarGGAVLLtTHQPLELA--AARVLDLGDFK 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-567 |
6.61e-30 |
|
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: 123.86 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAG--KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLElDKGSVERRLPLDqwgwmGQQ-T 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP-HGGRISGEVLLD-----GRDlL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 EADEAVfthayveegcpehyaakrRLKELEAQMQDA-AAPCMESLLADYQEAAERyMGLDGYHWETQVERKLLQLGLGRe 156
Cdd:COG1123 75 ELSEAL------------------RGRRIGMVFQDPmTQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLER- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 157 LWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLV 232
Cdd:COG1123 135 RLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 233 ELtptgcrkYRGgyteytrqKELELRTQEQLYRKQQLLreqleesirtyrqwfhqgeknaqmAEVPiqrgyfqgragahv 312
Cdd:COG1123 215 VM-------DDG--------RIVEDGPPEEILAAPQAL------------------------AAVP-------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 313 srmnakmkeleRLEGNRVEKPREAAhlkvklsasdfASRSLVRLERAAFRYGER---ELFA--ELSLSVDRGDRLAVLGP 387
Cdd:COG1123 242 -----------RLGAARGRAAPAAA-----------AAEPLLEVRNLSKRYPVRgkgGVRAvdDVSLTLRRGETLGLVGE 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 388 NGSGKTTLLKLLVGELQPAAGKVR-------------------------QHPQTSigyfsqelehLDDGVTLLDSLltlp 442
Cdd:COG1123 300 SGSGKSTLARLLLGLLRPTSGSILfdgkdltklsrrslrelrrrvqmvfQDPYSS----------LNPRMTVGDII---- 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 443 amtqtqARTILGCFLFSGEEVRKRIGDLSmgERCRL--AFLKLY---FSG---------------ANLLVLDEPTNYLDI 502
Cdd:COG1123 366 ------AEPLRLHGLLSRAERRERVAELL--ERVGLppDLADRYpheLSGgqrqrvaiaralalePKLLILDEPTSALDV 437
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 503 DSRERIEQALL----RYPGAMVIVSHDRFFIRKLATKLLWLSA----ERSPIA--FSGTYDEYAEASLASESSPE 567
Cdd:COG1123 438 SVQAQILNLLRdlqrELGLTYLFISHDLAVVRYIADRVAVMYDgrivEDGPTEevFANPQHPYTRALLAAVPSLD 512
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-231 |
2.22e-29 |
|
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: 115.71 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER--RLPLDQW---GWMGQQTEAD--- 80
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgKPLEKERkriGYVPQRRSIDrdf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 ----EAVfthayVEEGCPEHYAAKRRLKEleaqmqdaaapcmesllADYQEaaerymgldgyhwetqVERKLLQLGLGrE 156
Cdd:cd03235 84 pisvRDV-----VLMGLYGHKGLFRRLSK-----------------ADKAK----------------VDEALERVGLS-E 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 157 LWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVwLRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:cd03235 125 LADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHDlglvLEYFDRVL 203
|
...
gi 1844953743 229 tCL 231
Cdd:cd03235 204 -LL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
349-572 |
5.92e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 5.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------QHPQTSIGYFS 422
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 423 QELEhLDDG--VTLLDsLLTLPAMTQtqartiLGCFLFSGEEVR-----------------KRIGDLSMGERCRLAFLKL 483
Cdd:COG1121 82 QRAE-VDWDfpITVRD-VVLMGRYGR------RGLFRRPSRADReavdealervgledladRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 484 YFSGANLLVLDEPTNYLDIDSRERIEQALLRYPG---AMVIVSHDRFFIRKLATKLLWLSaeRSPIAFsGTYDEYAeasl 560
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLN--RGLVAH-GPPEEVL---- 226
|
250
....*....|..
gi 1844953743 561 asesSPEQLARA 572
Cdd:COG1121 227 ----TPENLSRA 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-228 |
9.64e-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: 114.95 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV---------ERRLPLDQWGWMG 74
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 75 QqteadeavfthayvEEGCPEHYAAKRRLKELEAQMqdaaapcmeslladyqeaaerymGLDGYHWETQVERKLLQLGLG 154
Cdd:COG4555 81 D--------------ERGLYDRLTVRENIRYFAELY-----------------------GLFDEELKKRIEELIELLGLE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 155 RELwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLE---VWLRAYPGTVVFVSHDRHFMDRVA 228
Cdd:COG4555 124 EFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLReilRALKKEGKTVLFSSHIMQEVEALC 199
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
355-539 |
2.13e-28 |
|
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: 111.18 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigyFsqelehldDGVTL 434
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------I--------DGKDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 435 LDSLLtlpamtqtqartilgcflfsgEEVRKRIG---DLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQA 511
Cdd:cd00267 64 AKLPL---------------------EELRRRIGyvpQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 512 LLRY--PGAMVI-VSHDRFFIRKLATKLLWL 539
Cdd:cd00267 123 LRELaeEGRTVIiVTHDPELAELAADRVIVL 153
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-236 |
2.96e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.22 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV----ERRLPLDQWGWMGQqtead 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEWRRQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 eaVfthAYVeegcpehyaakrrlkeleaqMQDAAapcmesLLADY-QEAAERYMGLDGYHWETQVERKLL-QLGLGRELW 158
Cdd:COG4619 76 --V---AYV--------------------PQEPA------LWGGTvRDNLPFPFQLRERKFDRERALELLeRLGLPPDIL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 159 DQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVEL 234
Cdd:COG4619 125 DKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
..
gi 1844953743 235 TP 236
Cdd:COG4619 205 EA 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-229 |
5.88e-27 |
|
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: 108.71 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEA---------VFTHa 87
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL---------VDGKDLTKLSLkelrrkvglVFQN- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 88 yveegcPEHYAAKRRLKEleaqmqDAAAPCmESLLADYQEAAERymgldgyhwetqVERKLLQLGLgRELWDQPLGQLSG 167
Cdd:cd03225 84 ------PDDQFFGPTVEE------EVAFGL-ENLGLPEEEIEER------------VEEALELVGL-EGLRDRSPFTLSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEvWLRAYPGTVVFVSHDRHFMDRVAT 229
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGrrelLELLK-KLKAEGKTIIIVTHDLDLLLELAD 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
352-524 |
5.90e-26 |
|
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: 107.09 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGK----------------VRQHpq 415
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 416 tsIGYFSQELEH-LDDGVTLLDSLLT-----------LPAMTQTQARTILGcfLFSGEEVRKR-IGDLSMGERCRL---- 478
Cdd:COG1119 80 --IGLVSPALQLrFPRDETVLDVVLSgffdsiglyrePTDEQRERARELLE--LLGLAHLADRpFGTLSQGEQRRVliar 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 479 AFLKlyfsgaN--LLVLDEPTNYLDIDSRERIEQAL--LRYPG--AMVIVSH 524
Cdd:COG1119 156 ALVK------DpeLLILDEPTAGLDLGARELLLALLdkLAAEGapTLVLVTH 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
355-539 |
1.05e-25 |
|
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: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---QHPQTS---IGYFSQeLEHL 428
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKErkrIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 DDG--VTLLDSLLT--------LPAMTQTQARTILGCFLFSG-EEVRKR-IGDLSMGERCRLAFLKLYFSGANLLVLDEP 496
Cdd:cd03235 80 DRDfpISVRDVVLMglyghkglFRRLSKADKAKVDEALERVGlSELADRqIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844953743 497 TNYLDIDSRERIEQAL--LRYPG-AMVIVSHDRFFIRKLATKLLWL 539
Cdd:cd03235 160 FAGVDPKTQEDIYELLreLRREGmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-227 |
1.07e-25 |
|
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: 105.49 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEA---------VFTH 86
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL---------VDGKDITKKNLrelrrkvglVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 87 ayveegcPEHyaakrrlkeleaQMqdaaapCMESLladYQEAA--ERYMGLDGYHWETQVERKLLQLGLgRELWDQPLGQ 164
Cdd:COG1122 84 -------PDD------------QL------FAPTV---EEDVAfgPENLGLPREEIRERVEEALELVGL-EHLADRPPHE 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHD----RHFMDRV 227
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDldlvAELADRV 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-220 |
2.49e-25 |
|
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: 102.90 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmgqqteadeavfthayveeGC 93
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL----LD-----------------------GK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 P-EHYAAKRRLKELeaqmqdaaapcmeSLLAdyqeaaerymgldgyhwetQVerkLLQLGLGrELWDQPLGQLSGGQKTR 172
Cdd:cd03214 62 DlASLSPKELARKI-------------AYVP-------------------QA---LELLGLA-HLADRPFNELSGGERQR 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 173 AQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHD 220
Cdd:cd03214 106 VLLARALAQEPPILLLDEPTSHLDIAHqielLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
361-539 |
2.61e-25 |
|
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: 102.86 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---QHPQTS-------IGYFSQELEhLDD 430
Cdd:cd03230 8 KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgKDIKKEpeevkrrIGYLPEEPS-LYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GVTLLDSLltlpamtqtqartilgcflfsgeevrkrigDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQ 510
Cdd:cd03230 87 NLTVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|..
gi 1844953743 511 ALLRY---PGAMVIVSHDRFFIRKLATKLLWL 539
Cdd:cd03230 137 LLRELkkeGKTILLSSHILEEAERLCDRVAIL 168
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
354-554 |
2.80e-25 |
|
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: 104.34 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsIgyfsqelehldDGV 432
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL------V-----------DGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 TLLDSLLtlpamtqTQARTILGcFLF-------------------------SGEEVRKRIGD-----------------L 470
Cdd:COG1122 64 DITKKNL-------RELRRKVG-LVFqnpddqlfaptveedvafgpenlglPREEIRERVEEalelvglehladrppheL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 471 SMGERCRLAFLklyfsGA-----NLLVLDEPTNYLDIDSRERIEQALLRYPGA---MVIVSHDRFFIRKLATKLLWLSAE 542
Cdd:COG1122 136 SGGQKQRVAIA-----GVlamepEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDG 210
|
250
....*....|..
gi 1844953743 543 RspIAFSGTYDE 554
Cdd:COG1122 211 R--IVADGTPRE 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
372-498 |
3.65e-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: 101.57 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-----------RQHPQTSIGYFSQELeHLDDGVTLLDSL-- 438
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDP-QLFPRLTVRENLrl 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 439 -LTLPAMTQT-------QARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:pfam00005 83 gLLLKGLSKRekdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-220 |
4.27e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.99 E-value: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwmgqqteadeaVF 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR--------------------VL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAYVEEgcpeHYAAKRRLKeleAQMQDAAAPcmESL-LADYQEAAERYMGLDGYHWETQVERKLLQLGLGrELWDQPLG 163
Cdd:COG1131 61 GEDVARD----PAEVRRRIG---YVPQEPALY--PDLtVRENLRFFARLYGLPRKEARERIDELLELFGLT-DAADRKVG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW-----LRAYPGTVVFVSHD 220
Cdd:COG1131 131 TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR--ELWellreLAAEGKTVLLSTHY 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
354-524 |
9.35e-25 |
|
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: 100.92 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsIGyfSQELEHLDDG 431
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlkDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------ID--GVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VtlLDSLLTLpaMTQTqartilgCFLFSGeEVRKRIgdLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQA 511
Cdd:cd03228 73 S--LRKNIAY--VPQD-------PFLFSG-TIRENI--LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170
....*....|....*
gi 1844953743 512 LLRYPG--AMVIVSH 524
Cdd:cd03228 139 LRALAKgkTVIVIAH 153
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-252 |
3.74e-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: 101.80 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEY----AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQtea 79
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT---------FDGRP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 deavfthayveegcpehyAAKRRLKELEAQM----QDAAA---PCM--ESLLAdyqEAAeRYMGLDgyHWETQVERKLLQ 150
Cdd:COG1124 69 ------------------VTRRRRKAFRRRVqmvfQDPYAslhPRHtvDRILA---EPL-RIHGLP--DREERIAELLEQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 151 LGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHD----RH 222
Cdd:COG1124 125 VGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDlavvAH 204
|
250 260 270
....*....|....*....|....*....|....
gi 1844953743 223 FMDRVAT----CLVELTPTGcRKYRGGYTEYTRQ 252
Cdd:COG1124 205 LCDRVAVmqngRIVEELTVA-DLLAGPKHPYTRE 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
361-557 |
5.07e-24 |
|
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: 101.09 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR----------QHPQTSIGYFSQELEhLDD 430
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepREARRQIGVLPDERG-LYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GVTLLDSLL---TLPAMTQTQART----ILGCFLFSgEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDID 503
Cdd:COG4555 88 RLTVRENIRyfaELYGLFDEELKKrieeLIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 504 SRERIEQALLRY--PGAMVIVS-HDRFFIRKLATKLLWLSAERspIAFSGTYDEYAE 557
Cdd:COG4555 167 ARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGK--VVAQGSLDELRE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-221 |
8.25e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 99.90 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER------RLPLDQ--WGWMGQqteaD 80
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtGVPPERrnIGMVFQ----D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAYVEEGCpeHYAAKRRLKELEaqmqdaaapcmeslladyqeaaerymgldgyHWETQVERKLLQLGLGRELwDQ 160
Cdd:cd03259 81 YALFPHLTVAENI--AFGLKLRGVPKA-------------------------------EIRARVRELLELVGLEGLL-NR 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 161 PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHDR 221
Cdd:cd03259 127 YPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-229 |
1.49e-23 |
|
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: 105.02 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 3 LLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwMGqqteadEA 82
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE----------IG------ET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 VFThAYVEegcpehyaakrrlkeleaQMQDAAAPCMESlladYQEAAErymGLDgyhwetqverkLLQLGlGREL----- 157
Cdd:TIGR03719 385 VKL-AYVD------------------QSRDALDPNKTV----WEEISG---GLD-----------IIKLG-KREIpsray 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 158 --------WDQ--PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRV 227
Cdd:TIGR03719 427 vgrfnfkgSDQqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
..
gi 1844953743 228 AT 229
Cdd:TIGR03719 507 AT 508
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-228 |
2.60e-23 |
|
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: 96.55 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTeadeavfthay 88
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------IDGKDI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 veegcpehyaAKRRLKELEAQMqdaaapcmeslladyqeaaerymgldGYhwetqverkllqlglgrelwdqpLGQLSGG 168
Cdd:cd00267 64 ----------AKLPLEELRRRI--------------------------GY-----------------------VPQLSGG 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 169 QKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHD----RHFMDRVA 228
Cdd:cd00267 85 QRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDpelaELAADRVI 151
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
355-539 |
2.95e-23 |
|
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: 98.10 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYGE-RELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQH--------PQTSIGYFSQEL 425
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakeRRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 426 EHLDDGVTLLDSL---LTLPAMTQTQARTILGCF-LFSGEEVRKRigDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:cd03226 81 DYQLFTDSVREELllgLKELDAGNEQAETVLKDLdLYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1844953743 502 IDSRERIEQALLRYPG---AMVIVSHDRFFIRKLATKLLWL 539
Cdd:cd03226 159 YKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLL 199
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-222 |
3.94e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlPLDQWGWMGQQTEADEA--VFTHAYVEE 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-GGARVAYVPQRSEVPDSlpLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 92 GCPEHYAAKRRLKEleaqmQDAAApcmeslladyqeaaerymgldgyhwetqVERKLLQLGLgRELWDQPLGQLSGGQKT 171
Cdd:NF040873 81 GRWARRGLWRRLTR-----DDRAA----------------------------VDDALERVGL-ADLAGRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 172 RAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHDRH 222
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-227 |
4.92e-23 |
|
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: 103.30 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQW----GWMGQQTeadeAVFt 85
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlSDLDPASWrrqiAWVPQNP----YLF- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 86 HAYVEE----GCPEhyAAkrrlkelEAQMQDAAapcmeslladyqEAAerymGLDGYhwetqVERklLQLGLgrelwDQP 161
Cdd:COG4988 424 AGTIREnlrlGRPD--AS-------DEELEAAL------------EAA----GLDEF-----VAA--LPDGL-----DTP 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 162 LG----QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASlEW--LEVWLRAYPG-TVVFVSHDRH---FMDRV 227
Cdd:COG4988 467 LGeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET-EAeiLQALRRLAKGrTVILITHRLAllaQADRI 541
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-221 |
5.64e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.61 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKamNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmgqqteaD 80
Cdd:COG1118 1 MSIEVR--NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV----LN-----------G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAYVEE---G-CPEHYAAKRRLKELEaqmQDAAApcMESLLADYQEAAERymgldgyhwetqVER--KLLQL-GL 153
Cdd:COG1118 64 RDLFTNLPPRErrvGfVFQHYALFPHMTVAE---NIAFG--LRVRPPSKAEIRAR------------VEEllELVQLeGL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 154 GRELwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLR----AYPGTVVFVSHDR 221
Cdd:COG1118 127 ADRY---P-SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQ 194
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-228 |
1.38e-22 |
|
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: 96.39 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGK----PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER-----RLPLDQWGWMGQ 75
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 76 QteadEAVFTHAYVEEGCpehyaakrrlkELEAQMQDAAApcmesllADYQEAAERYM---GLDGYhwetqvERKLlqlg 152
Cdd:cd03293 81 Q----DALLPWLTVLDNV-----------ALGLELQGVPK-------AEARERAEELLelvGLSGF------ENAY---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 153 lgrelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA---ASL--EWLEVWLRAYPgTVVFVSHDRH---FM 224
Cdd:cd03293 129 --------P-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLqeELLDIWRETGK-TVLLVTHDIDeavFL 198
|
....*
gi 1844953743 225 -DRVA 228
Cdd:cd03293 199 aDRVV 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-530 |
1.68e-22 |
|
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: 101.42 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGT--LELDKGSVERRLPL-DQWGWMGQQTEADE 81
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 --AVFTHAYVEE-----GCPEHYaaKRRLKELEAQM--QDAAAPCMESLLADYQEAAERYmgldGYHWETQVER-----K 147
Cdd:TIGR03269 81 pcPVCGGTLEPEevdfwNLSDKL--RRRIRKRIAIMlqRTFALYGDDTVLDNVLEALEEI----GYEGKEAVGRavdliE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLG-----LGRELwdqplgqlSGGQKTRAQLARLMVREPQLLLLDEPTNHLD--AASL--EWLEVWLRAYPGTVVFVS 218
Cdd:TIGR03269 155 MVQLShrithIARDL--------SGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqTAKLvhNALEEAVKASGISMVLTS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 219 HdrhfmdrvatclveltptgcrkyrggYTEytrqkelelrtqeqlyrkqqllreqLEESIRTYRQWFHQGE--KNAQMAE 296
Cdd:TIGR03269 227 H--------------------------WPE-------------------------VIEDLSDKAIWLENGEikEEGTPDE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 297 VpiqrgyfqgragahVSRMNAKMKELERLEGNRVEKPReaahLKVKLSASDFAS--RSLVR-LERAAFRYGERELFAels 373
Cdd:TIGR03269 256 V--------------VAVFMEGVSEVEKECEVEVGEPI----IKVRNVSKRYISvdRGVVKaVDNVSLEVKEGEIFG--- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 374 lsvdrgdrlaVLGPNGSGKTTLLKLLVGELQPAAGKV------------------RQHPQTSIGYFSQELEhLDDGVTLL 435
Cdd:TIGR03269 315 ----------IVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpdgRGRAKRYIGILHQEYD-LYPHRTVL 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 436 DSL-----LTLP-AMTQTQARTILGCFLFSGEEVR----KRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD---- 501
Cdd:TIGR03269 384 DNLteaigLELPdELARMKAVITLKMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitk 463
|
570 580 590
....*....|....*....|....*....|....*.
gi 1844953743 502 -------IDSRERIEQALlrypgamVIVSHDRFFIR 530
Cdd:TIGR03269 464 vdvthsiLKAREEMEQTF-------IIVSHDMDFVL 492
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
355-537 |
4.10e-22 |
|
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: 94.84 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV---------------RQHpqts 417
Cdd:cd03225 1 ELKNLSFSYPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkelRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 418 IGYFSQELEHLDDGVTLLDSL------LTLPAmTQTQARTILGCFLFSGEEVRKR-IGDLSMGERCRLAFLKLYFSGANL 490
Cdd:cd03225 77 VGLVFQNPDDQFFGPTVEEEVafglenLGLPE-EEIEERVEEALELVGLEGLRDRsPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1844953743 491 LVLDEPTNYLDIDSRERIEQALLRYPGA---MVIVSHDRFFIRKLATKLL 537
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVI 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-234 |
4.11e-22 |
|
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: 93.62 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwmgqqteadeaVF 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------------------VL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAYVEegcpEHYAAKRRLkeleaqmqdAAAPcmeslladyQEAAerymgldGYHWETqverkllqlglGRELwdqpLgQ 164
Cdd:cd03230 61 GKDIKK----EPEEVKRRI---------GYLP---------EEPS-------LYENLT-----------VREN----L-K 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW-----LRAYPGTVVFVSHDRHFMDRVATCLVEL 234
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR--EFWellreLKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
362-525 |
6.99e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 6.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEhLDDgvtlldsllTL 441
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE-VPD---------SL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 PAmtqTQARTI-LGCFLFSG-----------------EEV------RKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPT 497
Cdd:NF040873 71 PL---TVRDLVaMGRWARRGlwrrltrddraavddalERVgladlaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 498 NYLDIDSRERIEQALLRYPG---AMVIVSHD 525
Cdd:NF040873 148 TGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-220 |
7.12e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.54 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGK----PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-----ERRLPLDQWGWMGQqtea 79
Cdd:COG1116 12 GVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkPVTGPGPDRGVVFQ---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEAVFTHAYVEE----GcpehyaakrrlkeLEAQMQDAAapcmesllaDYQEAAERY---MGLDGYhwetqvERKLlqlg 152
Cdd:COG1116 88 EPALLPWLTVLDnvalG-------------LELRGVPKA---------ERRERARELlelVGLAGF------EDAY---- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 153 lgrelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA---ASL-EWL-EVWlRAYPGTVVFVSHD 220
Cdd:COG1116 136 --------P-HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERLqDELlRLW-QETGKTVLFVTHD 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-232 |
7.27e-22 |
|
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: 99.84 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQW----GWMGQQTeadeAVF 84
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlRDLDEDDLrrriAVVPQRP----HLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 tHAYVEE----GCPEhyAAkrrlkelEAQMQDAAapcmeslladyqEAAerymGLDgyHWetqverkLLQLGLGrelWDQ 160
Cdd:COG4987 422 -DTTLREnlrlARPD--AT-------DEELWAAL------------ERV----GLG--DW-------LAALPDG---LDT 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 161 PLG----QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVWLRAYPG-TVVFVSHDRHFMDRVATCLV 232
Cdd:COG4987 464 WLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLERMDRILV 541
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-352 |
8.55e-22 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 99.64 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqQTEADEAVFTHaY 88
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------------GTKLEVAYFDQ-H 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 VEEGCPEhyaakrrlKELEAQMQDAAAPCME--------SLLADYQEAAERYMgldgyhwetqverkllqlglgrelwdQ 160
Cdd:PRK11147 391 RAELDPE--------KTVMDNLAEGKQEVMVngrprhvlGYLQDFLFHPKRAM--------------------------T 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 161 PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVAT-CLVELTPTGC 239
Cdd:PRK11147 437 PVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTeCWIFEGNGKI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 240 RKYRGGYTEYTRQkelelrtQEQLYRKQQLLREQLEESirtyrqwfhQGEKNAQMAEVPIQRGYFQGRagaHVSRMNAKM 319
Cdd:PRK11147 517 GRYVGGYHDARQQ-------QAQYLALKQPAVKKKEEA---------AAPKAETVKRSSKKLSYKLQR---ELEQLPQLL 577
|
330 340 350
....*....|....*....|....*....|...
gi 1844953743 320 KELErlegnrvekpREAAHLKVKLSASDFASRS 352
Cdd:PRK11147 578 EDLE----------AEIEALQAQVADADFFSQP 600
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-193 |
1.54e-21 |
|
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: 91.17 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 20 FEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV----------ERRLPLDQWGWMGQqteaDEAVFTHAYV 89
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddERKSLRKEIGYVFQ----DPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 90 EEgcpehyaakrrlkeleaqmQDAAAPCMESLLADYQEAaerymgldgyhwetQVERKLLQLGLGrELWDQPLG----QL 165
Cdd:pfam00005 77 RE-------------------NLRLGLLLKGLSKREKDA--------------RAEEALEKLGLG-DLADRPVGerpgTL 122
|
170 180
....*....|....*....|....*...
gi 1844953743 166 SGGQKTRAQLARLMVREPQLLLLDEPTN 193
Cdd:pfam00005 123 SGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-219 |
2.23e-21 |
|
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: 92.42 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDQWGWMGQQTEADEAVfthayveegcpe 95
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR----WNGTPLAEQRDEPHENI------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 HYAA-----KRRLKELE-----AQMQDAAAPCMESLLADyqeaaeryMGLDGYHwetqverkllqlglgrelwDQPLGQL 165
Cdd:TIGR01189 76 LYLGhlpglKPELSALEnlhfwAAIHGGAQRTIEDALAA--------VGLTGFE-------------------DLPAAQL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 166 SGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAY---PGTVVFVSH 219
Cdd:TIGR01189 129 SAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
353-525 |
2.85e-21 |
|
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: 93.57 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--QHPQTS---------IGYF 421
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldGRDLASlsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQELEhLDDGVTLLD----------SLLTLP----------AMTQTQArtilgcflfsgEEVRKR-IGDLSMGERCRLAF 480
Cdd:COG1120 81 PQEPP-APFGLTVRElvalgryphlGLFGRPsaedreaveeALERTGL-----------EHLADRpVDELSGGERQRVLI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 481 LKLYFSGANLLVLDEPTNYLDIdsRERIE-----QALLRYPGAMVI-VSHD 525
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDL--AHQLEvlellRRLARERGRTVVmVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
355-525 |
3.11e-21 |
|
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: 91.34 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLdDGVTL 434
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------LDGKDLASL-SPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 435 LDSLLTLPamtqtQARTILGCFLFSGeevrKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQ---A 511
Cdd:cd03214 72 ARKIAYVP-----QALELLGLAHLAD----RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEllrR 142
|
170
....*....|....*
gi 1844953743 512 LLRYPGAMVI-VSHD 525
Cdd:cd03214 143 LARERGKTVVmVLHD 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-228 |
4.65e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 95.16 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV------------ERRlPLdqwGWMGQq 76
Cdd:COG3842 10 NVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgrdvtglppEKR-NV---GMVFQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 teaDEAVFTHAYVEE---------GCPEHyAAKRRLKELEAQMQdaaapcmeslLADYqeaAERYmgldgyhwetqverk 147
Cdd:COG3842 85 ---DYALFPHLTVAEnvafglrmrGVPKA-EIRARVAELLELVG----------LEGL---ADRY--------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 llqlglgrelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAY----PGTVVFVSHDRH- 222
Cdd:COG3842 133 -------------P-HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQEe 198
|
....*....
gi 1844953743 223 ---FMDRVA 228
Cdd:COG3842 199 alaLADRIA 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-219 |
5.32e-21 |
|
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: 92.45 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtleldkgsverrlplDQWgwmgqQTEADEA-VFTHAYVEEG 92
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG---------------DLP-----PTYGNDVrLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 CPEHyaaKRRLKELEAQMQD---AAAPCMESLLADYQEAAERYMGLDgyhwETQVER--KLL-QLGLGrELWDQPLGQLS 166
Cdd:COG1119 73 VWEL---RKRIGLVSPALQLrfpRDETVLDVVLSGFFDSIGLYREPT----DEQRERarELLeLLGLA-HLADRPFGTLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 167 GGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSH 219
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-232 |
6.24e-21 |
|
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: 90.32 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE-----------RRLPLDQ-WGW 72
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltdledELPPLRRrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 73 MGQQTeadeAVFTHAYVEEgcpehyaakrrlkeleaqmqdaaapcmeslladyqeaaerymgldgyhwetqverkllQLG 152
Cdd:cd03229 81 VFQDF----ALFPHLTVLE----------------------------------------------------------NIA 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 153 LGrelwdqplgqLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA---SLEWLEVWLRAYPG-TVVFVSHDRHFMDRVA 228
Cdd:cd03229 99 LG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRALLKSLQAQLGiTVVLVTHDLDEAARLA 168
|
....
gi 1844953743 229 TCLV 232
Cdd:cd03229 169 DRVV 172
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
322-554 |
1.58e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 96.06 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 322 LERLeGNRVEKPREAAHLKVKLSASDFASRslVRLERAAFRYGERE--LFAELSLSVDRGDRLAVLGPNGSGKTTLLKLL 399
Cdd:COG2274 445 LERL-DDILDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 400 VGELQPAAGKV-------RQHPQTS----IGYFSQElEHLDDGvTLLDSL-LTLPAMTQTQARTILgcfLFSG--EEVRK 465
Cdd:COG2274 522 LGLYEPTSGRIlidgidlRQIDPASlrrqIGVVLQD-VFLFSG-TIRENItLGDPDATDEEIIEAA---RLAGlhDFIEA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 466 -------RIGD----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPG--AMVIVSHDRFFIRkL 532
Cdd:COG2274 597 lpmgydtVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIR-L 675
|
250 260
....*....|....*....|..
gi 1844953743 533 ATKLLWLSAERspIAFSGTYDE 554
Cdd:COG2274 676 ADRIIVLDKGR--IVEDGTHEE 695
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-528 |
1.96e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 95.19 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQElEHLDDGVTLL-------- 435
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQE-PQLDPEKTVRenveegva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 436 -----------------------DSLLTLPAMTQT---------------QARTILGCFlfSGEEvrkRIGDLSMGERCR 477
Cdd:PRK11819 97 evkaaldrfneiyaayaepdadfDALAAEQGELQEiidaadawdldsqleIAMDALRCP--PWDA---KVTKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 478 LAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFF 528
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYF 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
355-524 |
1.98e-20 |
|
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: 88.81 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYG--ERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQhpqtsigyfsqelehldDGV 432
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-----------------DGA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 TLldslltlpamtQTQARTILGCF---------LFSGeEVRKRIgdLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDID 503
Cdd:cd03246 65 DI-----------SQWDPNELGDHvgylpqddeLFSG-SIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|....
gi 1844953743 504 SRERIEQALLRYPGAM---VIVSH 524
Cdd:cd03246 131 GERALNQAIAALKAAGatrIVIAH 154
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
362-523 |
2.01e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.51 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR----------QHPQTSIGYFSQELEhLDDG 431
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpAEVRRRIGYVPQEPA-LYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLLDSLLTL-------PAMTQTQARTILGcfLFSGEEVR-KRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDID 503
Cdd:COG1131 88 LTVRENLRFFarlyglpRKEARERIDELLE--LFGLTDAAdRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180
....*....|....*....|..
gi 1844953743 504 SRERIEQALLRY--PGAMVIVS 523
Cdd:COG1131 166 ARRELWELLRELaaEGKTVLLS 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-236 |
2.17e-20 |
|
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: 90.19 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYA-----GK--PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlplDQWGW- 72
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqgGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR---HDGGWv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 73 -MGQqteadeavfthayveegcpehyAAKRRLKELEAQM-------------QDAAAPCMESLLA---DYQEAAERymgl 135
Cdd:COG4778 78 dLAQ----------------------ASPREILALRRRTigyvsqflrviprVSALDVVAEPLLErgvDREEARAR---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 136 dgyhwetqVERKLLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVwLRAYP 211
Cdd:COG4778 132 --------ARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARG 202
|
250 260
....*....|....*....|....*
gi 1844953743 212 GTVVFVSHDRHFMDRVATCLVELTP 236
Cdd:COG4778 203 TAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-219 |
2.21e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEAV 83
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL---------WQGEPIRRQRDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 FTHAYVEEGcpeHYAA-KRRLKELEAqmqdaaapcmeslLADYQEAAERYMgldgyhwETQVERKLLQLGL-GRElwDQP 161
Cdd:PRK13538 72 YHQDLLYLG---HQPGiKTELTALEN-------------LRFYQRLHGPGD-------DEALWEALAQVGLaGFE--DVP 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 162 LGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYP---GTVVFVSH 219
Cdd:PRK13538 127 VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-229 |
2.83e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.80 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwMGQQTEAdeavf 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK----------IGETVKL----- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 thAYVEegcpehyaakrrlkeleaQMQDAaapcmeslLAD----YQEAAErymGLDgyhwetqverkLLQLGlGREL--- 157
Cdd:PRK11819 390 --AYVD------------------QSRDA--------LDPnktvWEEISG---GLD-----------IIKVG-NREIpsr 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 158 ----------WDQ--PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMD 225
Cdd:PRK11819 427 ayvgrfnfkgGDQqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLD 506
|
....
gi 1844953743 226 RVAT 229
Cdd:PRK11819 507 RIAT 510
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
5.62e-20 |
|
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: 89.27 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQ-TEA 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL---------VDGQDiTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEavfthayveegcpehyaakRRLKELEAQM----QDAA------------APCMESLLADYQEAAERymgldgyhwetq 143
Cdd:COG1127 73 SE-------------------KELYELRRRIgmlfQGGAlfdsltvfenvaFPLREHTDLSEAEIREL------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLgRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD---AASLEWLEVWLR-AYPGTVVFVSH 219
Cdd:COG1127 122 VLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRdELGLTSVVVTH 200
|
250
....*....|...
gi 1844953743 220 DRHFM----DRVA 228
Cdd:COG1127 201 DLDSAfaiaDRVA 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-559 |
8.15e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 93.33 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 30 GERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqQTEADEAVfthayveegcpEHYaakrRLKELEAQ 109
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEE------------EPSWDEVL-----------KRF----RGTELQNY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 110 MQDaaapcmeslLAD----------YQEAAERYmgLDGYHWE--TQV-ERKLL-----QLGLgRELWDQPLGQLSGGQKT 171
Cdd:PRK13409 152 FKK---------LYNgeikvvhkpqYVDLIPKV--FKGKVREllKKVdERGKLdevveRLGL-ENILDRDISELSGGELQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 172 RAQLARLMVREPQLLLLDEPTNHLD------AASLewlevwLRAY-PG-TVVFVSHDRHFMDRVATCLVEL--------- 234
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLDirqrlnVARL------IRELaEGkYVLVVEHDLAVLDYLADNVHIAygepgaygv 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 235 --TPTGCRKyrgGYTEYtrqkelelrtqeqlyrkqqlLREQL-EESIRtYRQWfhqgeknaqmaevPIQrgyFQGRAgah 311
Cdd:PRK13409 294 vsKPKGVRV---GINEY--------------------LKGYLpEENMR-IRPE-------------PIE---FEERP--- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 312 vsrmnakmkelerlegnrvekPREAAHLKVKLSASDFASRslvrleraafrYGERELFAELSlSVDRGDRLAVLGPNGSG 391
Cdd:PRK13409 331 ---------------------PRDESERETLVEYPDLTKK-----------LGDFSLEVEGG-EIYEGEVIGIVGPNGIG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 392 KTTLLKLLVGELQPAAGKVrqHPQTSIGYFSQELEHlddgvtllDSLLTLPAMTQTQARTILGCFLFSgEEVR------- 464
Cdd:PRK13409 378 KTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKP--------DYDGTVEDLLRSITDDLGSSYYKS-EIIKplqlerl 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 465 --KRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRY----PGAMVIVSHDRFFIRKLATKLlw 538
Cdd:PRK13409 447 ldKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRL-- 524
|
570 580
....*....|....*....|.
gi 1844953743 539 lsaerspIAFSGTYDEYAEAS 559
Cdd:PRK13409 525 -------MVFEGEPGKHGHAS 538
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-227 |
8.45e-20 |
|
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: 88.32 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAG----KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQWgwmg 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdiSKLSEKEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 75 qqteadeavfthayveegcpehyAAKRR------------LKELEAQmQDAAAPCMeslladyqeaaerYMGLDGYHWET 142
Cdd:cd03255 77 -----------------------AAFRRrhigfvfqsfnlLPDLTAL-ENVELPLL-------------LAGVPKKERRE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 143 QVERKLLQLGLGRELwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVS 218
Cdd:cd03255 120 RAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVT 198
|
250
....*....|..
gi 1844953743 219 HDR---HFMDRV 227
Cdd:cd03255 199 HDPelaEYADRI 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-228 |
1.18e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 88.33 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------------RRLPLD-QWGWMGQ 75
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaELYRLRrRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 76 QTeadeAVFTHAYVEE--GCP--EHyaakrrLKELEAQMQDAAAPCMESLladyqeaaerymGLDGYHwetqverkllql 151
Cdd:cd03261 85 SG----ALFDSLTVFEnvAFPlrEH------TRLSEEEIREIVLEKLEAV------------GLRGAE------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 152 glgrelwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEVWLR---AYPGTVVFVSHDRHFM--- 224
Cdd:cd03261 131 -------DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlkkELGLTSIMVTHDLDTAfai 203
|
....*
gi 1844953743 225 -DRVA 228
Cdd:cd03261 204 aDRIA 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-219 |
1.49e-19 |
|
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: 87.16 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 7 AMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsverRLPLDQWGWMGQQTEADEAVfth 86
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG----RVLLNGGPLDFQRDSIARGL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 87 ayveegcpeHYAAKrrlkeleaqmqdaaAPCMESLLAdyqeAAERYMGLDGYHWETQVERKLLQLGLGrELWDQPLGQLS 166
Cdd:cd03231 76 ---------LYLGH--------------APGIKTTLS----VLENLRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLS 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 167 GGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYP---GTVVFVSH 219
Cdd:cd03231 128 AGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-226 |
1.99e-19 |
|
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: 91.96 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGK-PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQW----GWMGQqteadea 82
Cdd:TIGR02857 331 YPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvplADADADSWrdqiAWVPQ------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 vftHAYVEEGCpehYAAKRRLKELEAqmqDAAApcmeslladYQEAAERyMGLDGYhwetqveRKLLQLGLGRELWDQPL 162
Cdd:TIGR02857 404 ---HPFLFAGT---IAENIRLARPDA---SDAE---------IREALER-AGLDEF-------VAALPQGLDTPIGEGGA 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 163 GqLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVSHDRHFMDR 226
Cdd:TIGR02857 458 G-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAAL 522
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-227 |
2.08e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 92.59 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQW-GWMGqqteadeAVFTHA 87
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlRQIDPASLrRQIG-------VVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 88 YVEEGCpehyaakrrLKE-LeaQMQDAAAPcmeslLADYQEAAERyMGLDGYhwetqVERklLQLGLgrelwDQPLG--- 163
Cdd:COG2274 559 FLFSGT---------IREnI--TLGDPDAT-----DEEIIEAARL-AGLHDF-----IEA--LPMGY-----DTVVGegg 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 164 -QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRayPGTVVFVSHDRHFMDRV 227
Cdd:COG2274 610 sNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLK--GRTVIIIAHRLSTIRLA 676
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-220 |
3.62e-19 |
|
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: 87.01 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWMGQQTEADEA-- 82
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI----------LFGGEDATDVPvq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 ------VFthayveegcpEHYAAKRRLKELE-----AQMQDAAAPCMESLLADYQEAAERYMGLDGyhwetqverkllql 151
Cdd:cd03296 73 ernvgfVF----------QHYALFRHMTVFDnvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDW-------------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 152 glgreLWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHD 220
Cdd:cd03296 129 -----LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHD 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-234 |
3.66e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.16 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTeadeavfthayveegcpehyAAKRR 102
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL---------LNGKPI--------------------KAKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LKELEAQMQDAaapcmesllaDYQ-----EAAERYMGLDGYHWETQVERKLLQ-LGLGRELWDQPLgQLSGGQKTRAQLA 176
Cdd:cd03226 70 RKSIGYVMQDV----------DYQlftdsVREELLLGLKELDAGNEQAETVLKdLDLYALKERHPL-SLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 177 RLMVREPQLLLLDEPTNHLDAASLEWLEVWLR--AYPGTVVFV-SHDRHFMDRVATCLVEL 234
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRelAAQGKAVIViTHDYEFLAKVCDRVLLL 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
356-524 |
6.03e-19 |
|
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: 85.49 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 356 LERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV----------RQHPQTSIGYfsqeL 425
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaeqRDEPHENILY----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 426 EHLdDGV----TLLDSLLTLPAMTQTQARTI---LGCFLFSGEEVRKrIGDLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:TIGR01189 79 GHL-PGLkpelSALENLHFWAAIHGGAQRTIedaLAAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 1844953743 499 YLDIDSRERIEQAL---LRYPGAMVIVSH 524
Cdd:TIGR01189 157 ALDKAGVALLAGLLrahLARGGIVLLTTH 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
352-558 |
7.24e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.39 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-----------RQHPQ----- 415
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlQQDPPrnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 416 TSIGYFSQEL----EHLDDGVTLLDSLLTLPA------MTQTQAR-TILGCFLFSG--EEVRKRIG--------DLSMGE 474
Cdd:PRK11147 82 TVYDFVAEGIeeqaEYLKRYHDISHLVETDPSeknlneLAKLQEQlDHHNLWQLENriNEVLAQLGldpdaalsSLSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 475 RCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLsaERSPIA-FSGTYD 553
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL--DRGKLVsYPGNYD 239
|
....*
gi 1844953743 554 EYAEA 558
Cdd:PRK11147 240 QYLLE 244
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-228 |
9.63e-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: 85.64 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQ----VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQ-TE 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalddVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII---------FDGKDlLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 ADEAVFthayveegcpehyaaKRRLKELEAQMQDAAA---PCM-------ESLLA----DYQEAAERYMGLdgyhwetqv 144
Cdd:cd03257 72 LSRRLR---------------KIRRKEIQMVFQDPMSslnPRMtigeqiaEPLRIhgklSKKEARKEAVLL--------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 145 erKLLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHD 220
Cdd:cd03257 128 --LLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHD 205
|
250
....*....|..
gi 1844953743 221 ----RHFMDRVA 228
Cdd:cd03257 206 lgvvAKIADRVA 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-220 |
1.33e-18 |
|
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: 85.37 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV----ERRLPLD----QWGWMGQq 76
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPphkrPVNTVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 teaDEAVFTHAYVEEgcpeHYAAKRRLKELEAQMQDAAApcmeslladyqEAAERYMGLDGYhwetqvERKLLQlglgre 156
Cdd:cd03300 80 ---NYALFPHLTVFE----NIAFGLRLKKLPKAEIKERV-----------AEALDLVQLEGY------ANRKPS------ 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 157 lwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHD 220
Cdd:cd03300 130 -------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-227 |
1.40e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.10 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEY----AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQ 76
Cdd:COG1136 1 MSPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL---------IDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 T----EADEAVFthayveegcpehyaakRR------------LKELEAQmQDAAAPCMeslLA--DYQEAAERYMGLdgy 138
Cdd:COG1136 72 IsslsERELARL----------------RRrhigfvfqffnlLPELTAL-ENVALPLL---LAgvSRKERRERAREL--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 139 hwetqverkLLQLGLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTV 214
Cdd:COG1136 129 ---------LERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTI 198
|
250
....*....|....*.
gi 1844953743 215 VFVSHDRH---FMDRV 227
Cdd:COG1136 199 VMVTHDPElaaRADRV 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
352-525 |
1.40e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.55 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELeHLDDG 431
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL-YLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLLDSLL-----------TLPAMTQTQARTILgcflfsgeevRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYL 500
Cdd:PRK09544 82 LPLTVNRFlrlrpgtkkedILPALKRVQAGHLI----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180
....*....|....*....|....*....
gi 1844953743 501 DIDSR----ERIEQALLRYPGAMVIVSHD 525
Cdd:PRK09544 152 DVNGQvalyDLIDQLRRELDCAVLMVSHD 180
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-224 |
1.92e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 89.53 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKP-LFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqQTEADEAVFTHAYVE-- 90
Cdd:PLN03073 518 YPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR------------SAKVRMAVFSQHHVDgl 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 --EGCPEHYAAKrrlkeleaqmqdaaapCMESLLadyqeaaerymgldgyhwETQVERKLLQLGLGRELWDQPLGQLSGG 168
Cdd:PLN03073 586 dlSSNPLLYMMR----------------CFPGVP------------------EQKLRAHLGSFGVTGNLALQPMYTLSGG 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 169 QKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFM 224
Cdd:PLN03073 632 QKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLI 687
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
362-555 |
2.48e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 88.69 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQE--------LEHLDDG-- 431
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQEtpalpqpaLEYVIDGdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 ---------------------VTLLDSLLTLPAMT-QTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGAN 489
Cdd:PRK10636 90 eyrqleaqlhdanerndghaiATIHGKLDAIDAWTiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 490 LLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAErSPIAFSGTYDEY 555
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ-SLFEYTGNYSSF 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
349-554 |
2.75e-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: 88.28 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-----------QHPQT 416
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdldpASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 417 SIGYFSQElEHLDDGvTLLDSL-LTLPAMTQTQARTIL---GCflfsGEEVRK-------RIGD----LSMGERCRLAFL 481
Cdd:COG4988 412 QIAWVPQN-PYLFAG-TIRENLrLGRPDASDEELEAALeaaGL----DEFVAAlpdgldtPLGEggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 482 KLYFSGANLLVLDEPTNYLDIDSRERIEQALLRY-PGAMVI-VSHDRFFIRkLATKLLWLSAERspIAFSGTYDE 554
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGRTVIlITHRLALLA-QADRILVLDDGR--IVEQGTHEE 557
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
364-523 |
3.18e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--QHPQTSIGYFSQE--LEHLD---DGVTLLD 436
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldGGDIDDPDVAEAChyLGHRNamkPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 437 SLL---TLPAMTQTQARTILGCFLFSGEEVRKrIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALL 513
Cdd:PRK13539 93 NLEfwaAFLGGEELDIAAALEAVGLAPLAHLP-FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
170
....*....|..
gi 1844953743 514 RY--PGAMVIVS 523
Cdd:PRK13539 172 AHlaQGGIVIAA 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-199 |
3.24e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEaDEAVFTHAyveegcpe 95
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK---------LDGGDID-DPDVAEAC-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 HYAAKRrlkeleaqmqDAaapCMESLLAdyQEAAERYMGLDGYHwETQVERKLLQLGLGReLWDQPLGQLSGGQKTRAQL 175
Cdd:PRK13539 76 HYLGHR----------NA---MKPALTV--AENLEFWAAFLGGE-ELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVAL 138
|
170 180
....*....|....*....|....
gi 1844953743 176 ARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAA 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
364-523 |
3.77e-18 |
|
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: 82.93 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQT---SIGYFSQELE---HLDDGVTLLDS 437
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfQRDSIARGLLylgHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 438 LLTL----PAMTQTQARTILGCFLFSGEEVRKrIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALL 513
Cdd:cd03231 91 LENLrfwhADHSDEQVEEALARVGLNGFEDRP-VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|..
gi 1844953743 514 RY--PGAMVIVS 523
Cdd:cd03231 170 GHcaRGGMVVLT 181
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-228 |
4.46e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQW---------G 71
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV--RLngrPLADWspaelarrrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 72 WMGQQTEADEAvFT-HAYVEEGCPEHYAAKRRLKEL-EAQMQdaaapcmeslLADYQEAAERYmgldgYHwetqverkll 149
Cdd:PRK13548 80 VLPQHSSLSFP-FTvEEVVAMGRAPHGLSRAEDDALvAAALA----------QVDLAHLAGRD-----YP---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 150 qlglgrelwdqplgQLSGGQKTRAQLARLMVR------EPQLLLLDEPTNHLDAA----SLEWLEVWLRAYPGTVVFVSH 219
Cdd:PRK13548 134 --------------QLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAhqhhVLRLARQLAHERGLAVIVVLH 199
|
250
....*....|...
gi 1844953743 220 D----RHFMDRVA 228
Cdd:PRK13548 200 DlnlaARYADRIV 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
354-541 |
4.54e-18 |
|
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: 82.23 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVrqhpqtsigYFsqelehldDGVT 433
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI---------LI--------DGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 434 LLDSLLTLPAmtqtqARTILGCF-----LFSGEEVRKRIG-DLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRER 507
Cdd:cd03229 64 LTDLEDELPP-----LRRRIGMVfqdfaLFPHLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 1844953743 508 IeQALLR-----YPGAMVIVSHDRFFIRKLATKLLWLSA 541
Cdd:cd03229 139 V-RALLKslqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-227 |
5.00e-18 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 83.95 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYA-GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEAdeavftha 87
Cdd:COG3638 7 NLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIL---------VDGQDVTA-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 88 yveegcpehyAAKRRLKELEAQM----QD------------------AAAPCMESLL-----ADYQEAAErymgldgyhw 140
Cdd:COG3638 70 ----------LRGRALRRLRRRIgmifQQfnlvprlsvltnvlagrlGRTSTWRSLLglfppEDRERALE---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 141 etqverkLL-QLGLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEVwL----RAYPGTV 214
Cdd:COG3638 130 -------ALeRVGLA-DKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDpKTARQVMDL-LrriaREDGITV 200
|
250
....*....|....*..
gi 1844953743 215 VFVSHD----RHFMDRV 227
Cdd:COG3638 201 VVNLHQvdlaRRYADRI 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-275 |
6.11e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.53 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRLPLdQWGWMGQ-QTE---A 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI-KLGYFAQhQLEflrA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEAvfthayveegcPEHYAAKRRLKELEAQMQDaaapcmeslladyqeaaerYMGLDGYHWETQVErkllqlglgrelwd 159
Cdd:PRK10636 391 DES-----------PLQHLARLAPQELEQKLRD-------------------YLGGFGFQGDKVTE-------------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 160 qPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCL-------V 232
Cdd:PRK10636 427 -ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLylvhdgkV 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 233 ELTPTGCRKYRGGYTEYTRQ------------------------KELELRTQEQLYRKQ-QLLREQLE 275
Cdd:PRK10636 506 EPFDGDLEDYQQWLSDVQKQenqtdeapkennansaqarkdqkrREAELRTQTQPLRKEiARLEKEME 573
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
372-554 |
6.35e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSigyfsqelehlddgvtlldSLLTL-----PAMTq 446
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS-------------------ALLELgagfhPELT- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 447 tqAR-------TILGcflFSGEEVRKR---------IGD--------LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDI 502
Cdd:COG1134 105 --GReniylngRLLG---LSRKEIDEKfdeivefaeLGDfidqpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 503 D----SRERIEQaLLRYPGAMVIVSHDRFFIRKLATKLLWLSAERspIAFSGTYDE 554
Cdd:COG1134 180 AfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR--LVMDGDPEE 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
354-524 |
6.52e-18 |
|
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: 83.02 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRY--GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-------RQ-HPQT---SIGY 420
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdiRQlDPADlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 421 FSQELeHLDDGvTLLDSL-LTLPAMTQT---QARTILGCFLFSGE-------EVRKRIGDLSMGERCRLAFLKLYFSGAN 489
Cdd:cd03245 83 VPQDV-TLFYG-TLRDNItLGAPLADDErilRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1844953743 490 LLVLDEPTNYLDIDSRERIEQALLRYPG--AMVIVSH 524
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-220 |
1.01e-17 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 82.93 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRLPLDQWGWMGQQTEADEAVF 84
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRI--RLNGQDATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 thayveegcpEHYAAKRRLKeleaqMQDAAAPCMESLLADYQEAAERymgldgyhwetqVErKLLQLGLGRELWDQPLGQ 164
Cdd:TIGR00968 79 ----------QHYALFKHLT-----VRDNIAFGLEIRKHPKAKIKAR------------VE-ELLELVQLEGLGDRYPNQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHD 220
Cdd:TIGR00968 131 LSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDevhvTTVFVTHD 190
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
364-541 |
1.03e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLDD------------- 430
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIRRQRDeyhqdllylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GV----TLLDSLLTLPAMTQTQ----ARTILGCFLFSG-EEVrkRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:PRK13538 84 GIktelTALENLRFYQRLHGPGddeaLWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1844953743 502 IDSRERIEQALLRY--PGAMVIV-SHDRFFIRKLATKLLWLSA 541
Cdd:PRK13538 162 KQGVARLEALLAQHaeQGGMVILtTHQDLPVASDKVRKLRLGQ 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-219 |
1.10e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 82.25 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQW---------GWMGQqteadEAVFTHAYVE 90
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV--LLdgtDIRQLdpadlrrniGYVPQ-----DVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 E----GCPehYAAKRRLkeleaqMQDAAAPCMESLLADYQeaaeryMGLDgyhwetqverklLQLGLGrelwdqplGQ-L 165
Cdd:cd03245 96 DnitlGAP--LADDERI------LRAAELAGVTDFVNKHP------NGLD------------LQIGER--------GRgL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 166 SGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVSH 219
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-228 |
1.18e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.86 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQWgwmgqqteadeavfthayve 90
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV--RLngrPLAAW-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 egCPEHYAAKRrlkeleAQMQDAAapcmeSLLADY--QEAAEryMGLDGYHWETQVERKLLQLGLGR----ELWDQPLGQ 164
Cdd:COG4559 69 --SPWELARRR------AVLPQHS-----SLAFPFtvEEVVA--LGRAPHGSSAAQDRQIVREALALvglaHLAGRSYQT 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 165 LSGGQKTRAQLARLMV-------REPQLLLLDEPTNHLDAA-SLEWLEVwLRAY---PGTVVFVSHD----RHFMDRVA 228
Cdd:COG4559 134 LSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAhQHAVLRL-ARQLarrGGGVVAVLHDlnlaAQYADRIL 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-227 |
1.46e-17 |
|
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: 82.10 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQWGWMG-----QQT 77
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgediTGLPPHEIARLGigrtfQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 EadeaVFTHAYVEEGCpehyaakrrlkELEAQMQDAAAPCMESLLADYQEAAERymgldgyhwetqVERKLLQLGLGrEL 157
Cdd:cd03219 85 R----LFPELTVLENV-----------MVAAQARTGSGLLLARARREEREARER------------AEELLERVGLA-DL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 158 WDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPT---NHLDAASLEWLEVWLRAYPGTVVFVSHDrhfMDRV 227
Cdd:cd03219 137 ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD---MDVV 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-228 |
1.59e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 82.88 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQ-----VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEA 79
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKkalddVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVT---------IDGRDITA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEavfthayveegcpehyaaKRRLKEL-----------EAQmqdaaapcmesLLAD--YQEAA--ERYMGLDGYHWETQV 144
Cdd:TIGR04521 72 KK------------------KKKLKDLrkkvglvfqfpEHQ-----------LFEEtvYKDIAfgPKNLGLSEEEAEERV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 145 ERKLLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHD 220
Cdd:TIGR04521 123 KEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrkeiLDLFKRLHKEKGLTVILVTHS 202
|
....*...
gi 1844953743 221 rhfMDRVA 228
Cdd:TIGR04521 203 ---MEDVA 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
362-525 |
1.63e-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: 81.78 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV----------RQHPQTSIGYFSQeleH-- 427
Cdd:cd03263 9 TYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQ---Fda 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 428 LDDGVTLLDsLLTLPAM------TQTQARTILGCFLFSGEEVR-KRIGDLSMGERCRL----AFLklyfSGANLLVLDEP 496
Cdd:cd03263 86 LFDELTVRE-HLRFYARlkglpkSEIKEEVELLLRVLGLTDKAnKRARTLSGGMKRKLslaiALI----GGPSVLLLDEP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 497 TNYLDIDSRERIEQALLRYPG--AMVIVSHD 525
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-537 |
1.68e-17 |
|
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: 85.99 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 30 GERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlPLDqwgWmgqqteaDEAVfthayveegcpEHYaakrRLKELEAQ 109
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDE--EPS---W-------DEVL-----------KRF----RGTELQDY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 110 MQDaaapcmeslLAD----------YQEAAERYmgLDGYHWE--TQV-ERKLL-----QLGLgRELWDQPLGQLSGGQKT 171
Cdd:COG1245 152 FKK---------LANgeikvahkpqYVDLIPKV--FKGTVREllEKVdERGKLdelaeKLGL-ENILDRDISELSGGELQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 172 RAQLARLMVREPQLLLLDEPTNHLD------AASLewlevwLR--AYPG-TVVFVSHDRHFMDRVATcLVELT------- 235
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDiyqrlnVARL------IRelAEEGkYVLVVEHDLAILDYLAD-YVHILygepgvy 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 236 -----PTGCRK----YRGGYteytrqkelelrtqeqlyrkqqlLREqleESIRtYRQWfhqgeknaqmaevPIQrgyFqg 306
Cdd:COG1245 293 gvvskPKSVRVginqYLDGY-----------------------LPE---ENVR-IRDE-------------PIE---F-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 307 ragahvsrmnakmkelerlegnRVEKPREAAHLKVKLSASDFASRslvrleraafrYGERELFAElSLSVDRGDRLAVLG 386
Cdd:COG1245 328 ----------------------EVHAPRREKEEETLVEYPDLTKS-----------YGGFSLEVE-GGEIREGEVLGIVG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 387 PNGSGKTTLLKLLVGELQPAAGKVrqHPQTSIGYFSQELEHLDDG--VTLLDSLLTlpamtqtqarTILGCFLFSGEEVR 464
Cdd:COG1245 374 PNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGtvEEFLRSANT----------DDFGSSYYKTEIIK 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 465 ---------KRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRY-----PGAMViVSHDRFFIR 530
Cdd:COG1245 442 plgleklldKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrgKTAMV-VDHDIYLID 520
|
....*..
gi 1844953743 531 KLATKLL 537
Cdd:COG1245 521 YISDRLM 527
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-227 |
1.87e-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: 80.12 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQWGwmgqqteadEAVfthAYV 89
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlRDLDLESLR---------KNI---AYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 90 EegcpehyaakrrlkeleaqmQDAAapcmeslladyqeaaerymgldgyhwetqverkllqlglgreLWDQPLGQ--LSG 167
Cdd:cd03228 82 P--------------------QDPF------------------------------------------LFSGTIREniLSG 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVwLRAYPG--TVVFVSHDRH---FMDRV 227
Cdd:cd03228 100 GQRQRIAIARALLRDPPILILDEATSALDPETeALILEA-LRALAKgkTVIVIAHRLStirDADRI 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-220 |
2.02e-17 |
|
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: 81.19 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 22 QVELEVNaGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-------------------ERRLpldqwGWMGQQTeadeA 82
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinlppqQRKI-----GLVFQQY----A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 VFTHAYVEEGCPehYAAKRRLkelEAQMQDaaapCMESLLAdyqeaaerYMGLDgyhwetqverkllqlglgrELWDQPL 162
Cdd:cd03297 86 LFPHLNVRENLA--FGLKRKR---NREDRI----SVDELLD--------LLGLD-------------------HLLNRYP 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRA----YPGTVVFVSHD 220
Cdd:cd03297 130 AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-227 |
2.94e-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: 80.79 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQtEADEAVF 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL---------FDGKP-LDIAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAYVeegcPEHYAAKRRLKELEAQMQDAAapcmeslLADY--QEAAERymgldgyhwetqVERKLLQLGLGrELWDQPL 162
Cdd:cd03269 71 RIGYL----PEERGLYPKMKVIDQLVYLAQ-------LKGLkkEEARRR------------IDEWLERLELS-EYANKRV 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHDrhfMDRV 227
Cdd:cd03269 127 EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQ---MELV 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-220 |
3.12e-17 |
|
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: 80.76 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV---ERRL----PLDQWGWMGQQteaDE 81
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyigGRDVtdlpPKDRDIAMVFQ---NY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVFTHAYVEEgcpeHYA-----AKRRLKELEAQMQDAAapcmeslladyqeaaerymgldgyhwetqverKLLQLGlgrE 156
Cdd:cd03301 82 ALYPHMTVYD----NIAfglklRKVPKDEIDERVREVA--------------------------------ELLQIE---H 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 157 LWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAslewLEVWLRA--------YPGTVVFVSHD 220
Cdd:cd03301 123 LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK----LRVQMRAelkrlqqrLGTTTIYVTHD 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
349-526 |
4.33e-17 |
|
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: 84.65 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-----------QHPQT 416
Cdd:TIGR02857 317 APASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadaDSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 417 SIGYFSQeLEHLDDGvTLLDSLL------TLPAMTQTQARTILGCFLFS-GEEVRKRIGD----LSMGERCRLAFLKLYF 485
Cdd:TIGR02857 397 QIAWVPQ-HPFLFAG-TIAENIRlarpdaSDAEIREALERAGLDEFVAAlPQGLDTPIGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1844953743 486 SGANLLVLDEPTNYLDIDSRERIEQALLRYPG--AMVIVSHDR 526
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-232 |
6.38e-17 |
|
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: 79.57 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEAVF 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---------FDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 TH--AYVEEgcPEHYAakrrlkELEAqmqdaaapcMESLladyqEAAERYMGLDgyhwETQVERKLLQLGLgRELWDQPL 162
Cdd:cd03268 72 RRigALIEA--PGFYP------NLTA---------RENL-----RLLARLLGIR----KKRIDEVLDVVGL-KDSAKKKV 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYP---GTVVFVSHDRHFMDRVATCLV 232
Cdd:cd03268 125 KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRIG 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
339-550 |
6.63e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 79.88 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 339 LKVKLSASDFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTS- 417
Cdd:cd03220 8 KSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSs 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 418 ---IGY-FSQELEHLDDgVTLLDSLLtlpAMTQTQARTILG-CFLFS--GEEVRKRIGDLSMGERCRLAFLKLYFSGANL 490
Cdd:cd03220 88 llgLGGgFNPELTGREN-IYLNGRLL---GLSRKEIDEKIDeIIEFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 491 LVLDEPTNYLD----IDSRERIEQaLLRYPGAMVIVSHDRFFIRKLATKLLWLsaERSPIAFSG 550
Cdd:cd03220 164 LLIDEVLAVGDaafqEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVL--EKGKIRFDG 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-220 |
7.41e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 3 LLIKamNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtleLDKGSverrlpldqwgwmGQQTEADEA 82
Cdd:PRK11247 13 LLLN--AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG---LETPS-------------AGELLAGTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 VFTHAYVEEgcpehyaakrRLkeleaQMQDAaapcmeSLLADYQEAAERYMGLDGyHWETQVERKLLQLGLGRELWDQPl 162
Cdd:PRK11247 75 PLAEAREDT----------RL-----MFQDA------RLLPWKKVIDNVGLGLKG-QWRDAALQALAAVGLADRANEWP- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAasLEWLE-------VWLRaYPGTVVFVSHD 220
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDA--LTRIEmqdliesLWQQ-HGFTVLLVTHD 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
349-554 |
7.58e-17 |
|
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: 80.41 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHL 428
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL--------VDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 DD----------GV-----TLLDSL-----LTLP-----AMTQTQARTILGCFLfsgEEV------RKRIGDLSMGERCR 477
Cdd:COG1127 73 SEkelyelrrriGMlfqggALFDSLtvfenVAFPlrehtDLSEAEIRELVLEKL---ELVglpgaaDKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 478 LAFlklyfsgA-------NLLVLDEPTNYLDIDSRERIEQaLLR-----YPGAMVIVSHDRFFIRKLATKLLWLSAERsp 545
Cdd:COG1127 150 VAL-------AralaldpEILLYDEPTAGLDPITSAVIDE-LIRelrdeLGLTSVVVTHDLDSAFAIADRVAVLADGK-- 219
|
....*....
gi 1844953743 546 IAFSGTYDE 554
Cdd:COG1127 220 IIAEGTPEE 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-238 |
8.59e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLiKAMNVMKEYAGKPLF---------EQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwg 71
Cdd:PRK10419 1 MTLL-NVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 72 WMGQQTEADEAvfthayveegcpEHYAAKRRlkelEAQM--QDA--AAPCMESLLADYQEAAERYMGLDGYHWETQVERK 147
Cdd:PRK10419 71 WRGEPLAKLNR------------AQRKAFRR----DIQMvfQDSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVwLRAYPGTV-VFVSHD-- 220
Cdd:PRK10419 135 LRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKK-LQQQFGTAcLFITHDlr 213
|
250 260
....*....|....*....|....
gi 1844953743 221 --RHFMDRVAT----CLVELTPTG 238
Cdd:PRK10419 214 lvERFCQRVMVmdngQIVETQPVG 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
371-559 |
9.28e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 80.14 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGD-----RLAVLGPNGSGKTTLLKLLVGELQPAAGKVrQHPQTSIGYFSQELEHLDDG-VTLLDSLLTLPAM 444
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGtVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 445 TQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRY-----PGAM 519
Cdd:cd03237 91 THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaenneKTAF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1844953743 520 ViVSHDRFFIRKLATKLlwlsaerspIAFSGTYDEYAEAS 559
Cdd:cd03237 171 V-VEHDIIMIDYLADRL---------IVFEGEPSVNGVAN 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
360-540 |
2.11e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.35 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 360 AFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--QHPQTS------IGYFSQeLEHLDDG 431
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidGKTATRgdrsrfMAYLGH-LPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLLDSLLTL-------PAMTQTQARTILGCFLFSGEEVRKrigdLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDS 504
Cdd:PRK13543 97 LSTLENLHFLcglhgrrAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1844953743 505 ---RERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLS 540
Cdd:PRK13543 173 itlVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-199 |
2.13e-16 |
|
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: 79.15 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYA-GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqqteadeav 83
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 fthayveEGCPEHYAAKRRLKELEAQM----QDAAapcmeslLADYQEAAER-YMGLDGYH--W----------ETQVER 146
Cdd:cd03256 61 -------DGTDINKLKGKALRQLRRQIgmifQQFN-------LIERLSVLENvLSGRLGRRstWrslfglfpkeEKQRAL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 147 KLL-QLGLgRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03256 127 AALeRVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPAS 179
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-220 |
2.36e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.89 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWMGQQ----TEADE--- 81
Cdd:COG3839 8 NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI----------LIGGRdvtdLPPKDrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 -------AVFTHAYVEE--GcpehYAAKRRlKELEAQMQDAAapcmeslladyQEAAERyMGLDGYhwetqVERKllqlg 152
Cdd:COG3839 78 amvfqsyALYPHMTVYEniA----FPLKLR-KVPKAEIDRRV-----------REAAEL-LGLEDL-----LDRK----- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 153 lgrelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAslewLEVWLRA--------YPGTVVFVSHD 220
Cdd:COG3839 131 --------P-KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK----LRVEMRAeikrlhrrLGTTTIYVTHD 193
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-228 |
2.43e-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: 79.31 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQWGWMG-----QQTeadeAVFTHAYVEE 91
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrdiTGLPPHRIARLGiartfQNP----RLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 92 ----GCpeHYAAKRRLKeleaqmqdAAAPCMESLLADYQEAAERymgldgyhwetqVERKLLQLGLGrELWDQPLGQLSG 167
Cdd:COG0411 99 nvlvAA--HARLGRGLL--------AALLRLPRARREEREARER------------AEELLERVGLA-DRADEPAGNLSY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPT---NHLDAASLEWLEVWLRAYPG-TVVFVSHDRHFM----DRVA 228
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVmglaDRIV 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
362-523 |
2.83e-16 |
|
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: 77.64 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQhpqtsigyFSQELEHLDDGVTLLDSLLTL 441
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF--------DGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 PA----MTQTQARTILGCFL-FSGEEV-------------RKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDID 503
Cdd:cd03268 81 PGfypnLTARENLRLLARLLgIRKKRIdevldvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180
....*....|....*....|..
gi 1844953743 504 SRERIEQALLRYP--GAMVIVS 523
Cdd:cd03268 161 GIKELRELILSLRdqGITVLIS 182
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
15-227 |
2.83e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 82.61 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-------------ERRlplDQWGWMGQqteaDE 81
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgvdirqidpaDLR---RNIGYVPQ----DP 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVFthayveegcpehYAAKRrlkelEAQMQDAAAPCMESLLadyqEAAERyMGLDGYhwetqveRKLLQLGLgrelwDQP 161
Cdd:TIGR03375 549 RLF------------YGTLR-----DNIALGAPYADDEEIL----RAAEL-AGVTEF-------VRRHPDGL-----DMQ 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 162 LGQ----LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVSHDRHFMDRV 227
Cdd:TIGR03375 595 IGErgrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSLLDLV 666
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
347-514 |
4.37e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.46 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 347 DFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR----------QHPQT 416
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 417 SIGYFSQeLEHLDDGVTLLDSLLTLP---AMTQTQARTILGCFL-FSGEEVR--KRIGDLSMGERCRLAFLKLYFSGANL 490
Cdd:PRK13537 81 RVGVVPQ-FDNLDPDFTVRENLLVFGryfGLSAAAARALVPPLLeFAKLENKadAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180
....*....|....*....|....*...
gi 1844953743 491 LVLDEPTNYLDIDSR----ERIEQALLR 514
Cdd:PRK13537 160 LVLDEPTTGLDPQARhlmwERLRSLLAR 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-230 |
7.34e-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: 77.37 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 12 KEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVeRRLPLDQWgwmgqqteadeavfthayveE 91
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-RVAGLVPW--------------------K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 92 GCPEHyaaKRRLKELEAQMQDAA--APCMESlladYQEAAERYmGLDGYHWETQVER--KLLQLGlgrELWDQPLGQLSG 167
Cdd:cd03267 88 RRKKF---LRRIGVVFGQKTQLWwdLPVIDS----FYLLAAIY-DLPPARFKKRLDElsELLDLE---ELLDTPVRQLSL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAY----PGTVVFVSHDrhfMDRVATC 230
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY---MKDIEAL 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-226 |
8.28e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.63 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYA-GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPldqwgwmgqqt 77
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlSRLK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 eadeavfthayveegcpehyaaKRRLKELEAQM----QDAaapcmeSLLADyQEAAE------RYMGLDGYHWETQVERK 147
Cdd:COG2884 71 ----------------------RREIPYLRRRIgvvfQDF------RLLPD-RTVYEnvalplRVTGKSRKEIRRRVREV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLGLGRELWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEVW--LRAYPGTVVFVSHDRHFM 224
Cdd:COG2884 122 LDLVGLSDKAKALP-HELSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSWEIMELLeeINRRGTTVLIATHDLELV 200
|
..
gi 1844953743 225 DR 226
Cdd:COG2884 201 DR 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-228 |
8.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEqVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwmgqqtEADEAVFTHAYVEEGC 93
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT---------------VGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 PEHYAAKRRLKELEAQMQDaaapcmESLLADYQEAAERYmGLDGYHWETQVERKLLQLGLGRELWDQPLGQLSGGQKTRA 173
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFE------ETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLD-AASLEWLEVW--LRAYPGTVVFVShdrHFMDRVA 228
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDpKARIEMMQLFesIHQSGQTVVLVT---HLMDDVA 208
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
16-220 |
9.79e-16 |
|
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: 77.55 E-value: 9.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqTEADEAVFTHAyveegcpe 95
Cdd:TIGR03873 13 GRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTV---------------DLAGVDLHGLS-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 HYAAKRRLKELEaQMQDAAAPC-MESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGrELWDQPLGQLSGGQKTRAQ 174
Cdd:TIGR03873 70 RRARARRVALVE-QDSDTAVPLtVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVH 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1844953743 175 LARLMVREPQLLLLDEPTNHLD-AASLEWLEVwLR--AYPG-TVVFVSHD 220
Cdd:TIGR03873 148 VARALAQEPKLLLLDEPTNHLDvRAQLETLAL-VRelAATGvTVVAALHD 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
361-514 |
1.49e-15 |
|
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: 75.04 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERE--LFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVrqhpqtsigYFSQELEHlddgvTLLDSL 438
Cdd:cd03247 8 FSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVS-----DLEKAL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 439 LTLPAMTQTQArtilgcFLFSGeEVRKRIGD-LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDidsrERIEQALLR 514
Cdd:cd03247 74 SSLISVLNQRP------YLFDT-TLRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTVGLD----PITERQLLS 139
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-220 |
1.90e-15 |
|
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: 79.33 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwGWMGQQTEADEAVFTHAYVEegcpe 95
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT----LD--GVPVSSLDQDEVRRRVSVCA----- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 hyaakrrlkeleaqmQDA---AAPCMESLLADYQEAAERymgldgyhwetQVERKLLQLGLGRELWDQPLG--------- 163
Cdd:TIGR02868 416 ---------------QDAhlfDTTVRENLRLARPDATDE-----------ELWAALERVGLADWLRALPDGldtvlgegg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 164 -QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA-ASLEWLEVWLRAYPG-TVVFVSHD 220
Cdd:TIGR02868 470 aRLSGGERQRLALARALLADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
362-540 |
2.02e-15 |
|
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: 75.83 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtSIGY--FSQELEHLD---------- 429
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLvpWKRRKKFLRrigvvfgqkt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 430 ---------DGVTLLDSLLTLPAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYL 500
Cdd:cd03267 105 qlwwdlpviDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 501 DIDSRERIEQALLRY---PGAMVIV-SHDRFFIRKLATKLLWLS 540
Cdd:cd03267 185 DVVAQENIRNFLKEYnreRGTTVLLtSHYMKDIEALARRVLVID 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
354-526 |
4.85e-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: 74.48 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-------QHP--QTSIGYFSQE 424
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtGVPpeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 425 ---LEHLddgvTLLDSL---LTLPAM--TQTQARTILGCFLFSGEEVRKR-IGDLSMGERCRLAFLKLYFSGANLLVLDE 495
Cdd:cd03259 81 yalFPHL----TVAENIafgLKLRGVpkAEIRARVRELLELVGLEGLLNRyPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1844953743 496 PTNYLDIDSRERIEQALLRYPGA----MVIVSHDR 526
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElgitTIYVTHDQ 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
354-554 |
5.34e-15 |
|
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: 74.85 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHpQTSIGYFSQ-ELEHLDD-- 430
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEaELYRLRRrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GV-----TLLDSL-------LTLPAMTQTQARTILGCFLFSGEEV------RKRIGDLSMGERCRLAFLKLYFSGANLLV 492
Cdd:cd03261 80 GMlfqsgALFDSLtvfenvaFPLREHTRLSEEEIREIVLEKLEAVglrgaeDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 493 LDEPTNYLDIDSRERIEQALLRYPGAM----VIVSHDRFFIRKLATKLLWLSAERspIAFSGTYDE 554
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGK--IVAEGTPEE 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-219 |
5.41e-15 |
|
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: 73.02 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQWGWM--GQQTeadeavfthAYV 89
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--RLdgaDISQWDPNelGDHV---------GYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 90 eegcpehyaakrrlkeleaqMQDAaapcmeslladyqeaaerymgldgyhwetqverkllqlglgrELWDQPLGQ--LSG 167
Cdd:cd03246 82 --------------------PQDD------------------------------------------ELFSGSIAEniLSG 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLE---VWLRAYPGTVVFVSH 219
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAH 154
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
362-523 |
6.17e-15 |
|
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: 73.85 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-------QHPQTSIGYFSQElEHLDDGVTL 434
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEE-RGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 435 LDSLL---TLPAMTQTQARTILGCFLFS---GEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERI 508
Cdd:cd03269 88 IDQLVylaQLKGLKKEEARRRIDEWLERlelSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170
....*....|....*..
gi 1844953743 509 EQAL--LRYPGAMVIVS 523
Cdd:cd03269 168 KDVIreLARAGKTVILS 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-221 |
6.48e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.66 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG-------TLELDKGSVERRLPLD-QWGWMGQQ 76
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsgHIRFHGTDVSRLHARDrKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 TeadeAVFTHAYVEEGC------------PEHYAAKRRLKELEAQMQdaaapcMESLladyqeaAERYmgldgyhwetqv 144
Cdd:PRK10851 83 Y----ALFRHMTVFDNIafgltvlprrerPNAAAIKAKVTQLLEMVQ------LAHL-------ADRY------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 145 erkllqlglgrelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLR----AYPGTVVFVSHD 220
Cdd:PRK10851 134 ----------------P-AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlheELKFTSVFVTHD 196
|
.
gi 1844953743 221 R 221
Cdd:PRK10851 197 Q 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-199 |
6.55e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.90 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQW----GWMGQQTeadeAVFt 85
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdiRDLTLESLrrqiGVVPQDT----FLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 86 HAYVEE----GCPEhyAAkrrlkelEAQMQDAAApcmeslLAdyqEAAERYMGL-DGYhwETQV-ERkllqlGlgrelwd 159
Cdd:COG1132 427 SGTIREniryGRPD--AT-------DEEVEEAAK------AA---QAHEFIEALpDGY--DTVVgER-----G------- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1844953743 160 qplGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:COG1132 475 ---VNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
356-507 |
9.42e-15 |
|
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: 73.38 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 356 LERAAFRYGERELFAELSLSVDRGdRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-------QHPQT---SIGYFSQEL 425
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlKQPQKlrrRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 426 EhLDDGVT---LLDSLLTLPAMTQTQARTILgCFLFS----GEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:cd03264 82 G-VYPNFTvreFLDYIAWLKGIPSKEVKARV-DEVLElvnlGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
....*....
gi 1844953743 499 YLDIDSRER 507
Cdd:cd03264 160 GLDPEERIR 168
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
357-508 |
1.03e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 73.56 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 357 ERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGK-------VRQHPQT---SIGYFSQELE 426
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREvrrRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 427 hLDDGVTLLDSLLtlpamtqTQARtILGcflFSGEEVRKRIGDLsmgercrLAFLKL---------YFSGA--------- 488
Cdd:cd03265 84 -VDDELTGWENLY-------IHAR-LYG---VPGAERRERIDEL-------LDFVGLleaadrlvkTYSGGmrrrleiar 144
|
170 180
....*....|....*....|....*.
gi 1844953743 489 ------NLLVLDEPTNYLDIDSRERI 508
Cdd:cd03265 145 slvhrpEVLFLDEPTIGLDPQTRAHV 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-228 |
1.82e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 73.14 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV------------ERRlpldQWGWMGQqteaDEAVFTHAYVE 90
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditnlppEKR----DISYVPQ----NYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 EGCPehYAAKRRL---KELEAQMQDAAapcmeslladyqeaaeRYMGLDgyhwetqverkllqlglgrELWDQPLGQLSG 167
Cdd:cd03299 90 KNIA--YGLKKRKvdkKEIERKVLEIA----------------EMLGID-------------------HLLNRKPETLSG 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:cd03299 133 GEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
372-554 |
2.21e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 72.85 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-----------------------QHPQTsigyfsqeLEHL 428
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiarlgigrtfQIPRL--------FPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 ddgvTLLDSLLtLPAMTQTQARTILGCFLFSGEEVRKRI-----------------GDLSMGERCRLAFLKLYFSGANLL 491
Cdd:cd03219 91 ----TVLENVM-VAAQARTGSGLLLARARREEREARERAeellervgladladrpaGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 492 VLDEPTNYLDIDSRERIEQAL--LRYPG-AMVIVSHDRFFIRKLATKLLWLSAERspIAFSGTYDE 554
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIreLRERGiTVLLVEHDMDVVMSLADRVTVLDQGR--VIAEGTPDE 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-234 |
2.23e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.57 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERR----LPLD-QWGWMGQQTEADEAVFTHAYveegcpehY 97
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsSLLGlGGGFNPELTGRENIYLNGRL--------L 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 98 AAKRRlkeleaqmqdaaapCMESLLADYQEAAErymgldgyhwetqverkllqLGlgrELWDQPLGQLSGGQKTRAQLAR 177
Cdd:cd03220 113 GLSRK--------------EIDEKIDEIIEFSE--------------------LG---DFIDLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 178 LMVREPQLLLLDEPTNHLDAA----SLEWLEVWLRAyPGTVVFVSHDRHFMDRVATCLVEL 234
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-221 |
2.27e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.98 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQ---QTEAD 80
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM----LD-----GQditHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 E----------AVFTHAYVEegcpEHYAAKRRLKELEAqmQDAAAPCMESLladyqeaaerymgldgyhwetqverKLLQ 150
Cdd:PRK09452 85 NrhvntvfqsyALFPHMTVF----ENVAFGLRMQKTPA--AEITPRVMEAL-------------------------RMVQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 151 LglgRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-----AASLEwLEVWLRAYPGTVVFVSHDR 221
Cdd:PRK09452 134 L---EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkQMQNE-LKALQRKLGITFVFVTHDQ 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
354-524 |
2.31e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.97 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-------RQHPQTS----IGYF 421
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdiRDLTLESlrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQElehlddgVTLLDslltlpamtqtqaRTI-----LGCFLFSGEEVRK--------------------RIGD----LSM 472
Cdd:COG1132 420 PQD-------TFLFS-------------GTIrenirYGRPDATDEEVEEaakaaqahefiealpdgydtVVGErgvnLSG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 473 GERCRL----AFLKlyfsGANLLVLDEPTNYLDIDSRERIEQALLRY-PGAMVIV-SH 524
Cdd:COG1132 480 GQRQRIaiarALLK----DPPILILDEATSALDTETEALIQEALERLmKGRTTIViAH 533
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-228 |
2.47e-14 |
|
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: 72.18 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTEADEA-- 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII----ID-----GLKLTDDKKni 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 ---------VFthayveegcpEHYAAKRRLKELEAQMQdaaAPcMESLLADYQEAAERYMGLdgyhwetqverkLLQLGL 153
Cdd:cd03262 72 nelrqkvgmVF----------QQFNLFPHLTVLENITL---AP-IKVKGMSKAEAEERALEL------------LEKVGL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 154 gRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASL-EWLEVWLR-AYPG-TVVFVSHDRHFMDRVA 228
Cdd:cd03262 126 -ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgEVLDVMKDlAEEGmTMVVVTHEMGFAREVA 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-196 |
2.58e-14 |
|
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: 72.23 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGeRIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQ-QTEADEAV 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIR---------IDGQdVLKQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 FTH-AYV--EEGCPEHYAAKRRLkeleaqmqdaaapcmesllaDYQEAAErymGLDGYHWETQVERKLLQLGLGRELwDQ 160
Cdd:cd03264 71 RRRiGYLpqEFGVYPNFTVREFL--------------------DYIAWLK---GIPSKEVKARVDEVLELVNLGDRA-KK 126
|
170 180 190
....*....|....*....|....*....|....*.
gi 1844953743 161 PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
366-532 |
2.85e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 366 RELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGeLQPAA-GKVRQHPQTSIGYFSQELeHLDDGvTLLDSLL---TL 441
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGsGRIARPAGARVLFLPQRP-YLPLG-TLREALLypaTA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 PAMTQTQARTILgcflfsgEEVR-----KRIGD-------LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIE 509
Cdd:COG4178 453 EAFSDAELREAL-------EAVGlghlaERLDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170 180
....*....|....*....|....*....
gi 1844953743 510 QALL-RYPGAMVI-VSH----DRFFIRKL 532
Cdd:COG4178 526 QLLReELPGTTVIsVGHrstlAAFHDRVL 554
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
372-537 |
3.03e-14 |
|
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: 72.54 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLDDGVTLL----------DSLLTL 441
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII--------FDGKDLLKLSRRLRKIrrkeiqmvfqDPMSSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 -PAMT-QTQ-ARTILGCFLFSGEEVRKRIGDLsmgERCRL----AFLKLY---FSG------------AN---LLVLDEP 496
Cdd:cd03257 96 nPRMTiGEQiAEPLRIHGKLSKKEARKEAVLL---LLVGVglpeEVLNRYpheLSGgqrqrvaiaralALnpkLLIADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 497 TNYLDIDSRERIEQALLR----YPGAMVIVSHDRFFIRKLATKLL 537
Cdd:cd03257 173 TSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-228 |
3.08e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.48 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLfeQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQ---QTEADEA--- 82
Cdd:COG3840 6 DLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL---------WNGQdltALPPAERpvs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 -------VFTHAYVEEGC-----PehyaakrRLKELEAQMQDAaapcmeslladyQEAAERyMGLDGYhwetqVERKllq 150
Cdd:COG3840 75 mlfqennLFPHLTVAQNIglglrP-------GLKLTAEQRAQV------------EQALER-VGLAGL-----LDRL--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 151 lglgrelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA----SLEWLEVWLRAYPGTVVFVSHD----RH 222
Cdd:COG3840 127 ----------P-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGLTVLMVTHDpedaAR 195
|
....*.
gi 1844953743 223 FMDRVA 228
Cdd:COG3840 196 IADRVL 201
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-220 |
3.60e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.74 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTL---------------ELDKGSVERRlpldQWGWMGQqte 78
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLspafsasgevllngrRLTALPAEQR----RIGILFQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 aDEAVFTHAYVEE----GCPEHYAAKRRLKELEAQMQDAaapcmeslladyqeaaerymGLDGYHwetqverkllqlglg 154
Cdd:COG4136 84 -DDLLFPHLSVGEnlafALPPTIGRAQRRARVEQALEEA--------------------GLAGFA--------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 155 relwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVW----LRAYPGTVVFVSHD 220
Cdd:COG4136 128 ----DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHD 193
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
363-502 |
5.76e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 363 YGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQEL---------EHL-DDGV 432
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrlallpqHHLtPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 TLL--------------------DSLLTLPAMTQTQARTIlgcflfsgeeVRKRIGDLSMGERCRlAFLKLYFS-GANLL 491
Cdd:PRK11231 92 TVRelvaygrspwlslwgrlsaeDNARVNQAMEQTRINHL----------ADRRLTDLSGGQRQR-AFLAMVLAqDTPVV 160
|
170
....*....|.
gi 1844953743 492 VLDEPTNYLDI 502
Cdd:PRK11231 161 LLDEPTTYLDI 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
352-525 |
8.46e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.84 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRY--GERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEH 427
Cdd:COG1136 3 PLLELRNLTKSYgtGEGEVTAlrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL--------IDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 428 LDDGV----------------TLLDSL-----LTLPAM--------TQTQARTILgcflfsgEEV------RKRIGDLSM 472
Cdd:COG1136 75 LSERElarlrrrhigfvfqffNLLPELtalenVALPLLlagvsrkeRRERARELL-------ERVglgdrlDHRPSQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 473 GERCRLAF---LklyfsgAN---LLVLDEPTNYLDIDSRERIEQALLRY---PG-AMVIVSHD 525
Cdd:COG1136 148 GQQQRVAIaraL------VNrpkLILADEPTGNLDSKTGEEVLELLRELnreLGtTIVMVTHD 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-227 |
9.21e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQ-TEADEAV 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL---------WDGEPlDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 FthAYVeegcPE--------------HYAAkrRLKeleaQMQDAAApcmeslladyQEAAERYMgldgyhwetqvERkll 149
Cdd:COG4152 73 I--GYL----PEerglypkmkvgeqlVYLA--RLK----GLSKAEA----------KRRADEWL-----------ER--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 150 qLGLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAY--PG-TVVFVSHDrhfMDR 226
Cdd:COG4152 117 -LGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ---MEL 191
|
.
gi 1844953743 227 V 227
Cdd:COG4152 192 V 192
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-228 |
9.25e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.86 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGS--------------VERRLpldqw 70
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepreVRRRI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 71 GWMGQQTEADEAVftHAYveegcpEHYAAKRRLkeleaqmqdaaapcmeslladyqeaaeryMGLDGYHWETQVERKLLQ 150
Cdd:cd03265 76 GIVFQDLSVDDEL--TGW------ENLYIHARL-----------------------------YGVPGAERRERIDELLDF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 151 LGLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW-----LRAYPGTVVFVShdRHFM- 224
Cdd:cd03265 119 VGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA--HVWeyiekLKEEFGMTILLT--THYMe 193
|
250
....*....|
gi 1844953743 225 ------DRVA 228
Cdd:cd03265 194 eaeqlcDRVA 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-220 |
1.12e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRLPLDQWGWMGQQTEAD 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 -------EAVFTHAYVEEGCpehyaakrrlkeleaQMQ-DAAAPCMESLLAdyqeAAERYMG---LDGYHWETQVErkll 149
Cdd:PRK11701 83 rrrllrtEWGFVHQHPRDGL---------------RMQvSAGGNIGERLMA----VGARHYGdirATAGDWLERVE---- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 150 qLGLGReLWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVWLRAYPGTVVFVSHD 220
Cdd:PRK11701 140 -IDAAR-IDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-236 |
1.16e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTEADEA- 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT----LD-----GKPVEGPGAe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 ---VFTHayveEGCpehYAAKRRLKELEAQMQDAAAPCMEslladyQEAAERYM----GLDGYHwetqverkllqlglGR 155
Cdd:PRK11248 72 rgvVFQN----EGL---LPWRNVQDNVAFGLQLAGVEKMQ------RLEIAHQMlkkvGLEGAE--------------KR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 156 ELWdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWL-EVWLRAYPGT---VVFVSHDRHFMDRVATCL 231
Cdd:PRK11248 125 YIW-----QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMqTLLLKLWQETgkqVLLITHDIEEAVFMATEL 199
|
....*
gi 1844953743 232 VELTP 236
Cdd:PRK11248 200 VLLSP 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-238 |
1.29e-13 |
|
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: 71.37 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAG---------KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMG 74
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS---------FRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 75 QQteadeavfthayVEEGCPEHYAAKRRlkELEAQMQDA--AAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLG 152
Cdd:TIGR02769 73 QD------------LYQLDRKQRRAFRR--DVQLVFQDSpsAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 153 LGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVwLRAYPGTV-VFVSHD----RHF 223
Cdd:TIGR02769 139 LRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlqAVILELLRK-LQQAFGTAyLFITHDlrlvQSF 217
|
250
....*....|....*....
gi 1844953743 224 MDRVATC----LVELTPTG 238
Cdd:TIGR02769 218 CQRVAVMdkgqIVEECDVA 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
361-531 |
1.40e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV---RQHPQTSIGYFSQEL------EHLDDG 431
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlfeRQSIKKDLCTYQKQLcfvghrSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLLDSLLTLPAMTQTQARTILGCFLFS-GEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIE- 509
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVGITELCRLFSlEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIt 168
|
170 180
....*....|....*....|....
gi 1844953743 510 --QALLRYPGAMVIVSHDRFFIRK 531
Cdd:PRK13540 169 kiQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-237 |
1.61e-13 |
|
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: 70.29 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGS-VERRLPLDQWGWMGQQTEADEA- 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApDEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 -----VFTHAYVeegcpehyaakrrlkeLEAQMQD--AAAPcmesLLADYQEAAERymgldgyhwETQVERKLLQLGLGR 155
Cdd:cd03260 81 rrvgmVFQKPNP----------------FPGSIYDnvAYGL----RLHGIKLKEEL---------DERVEEALRKAALWD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 156 ELWDQPLG-QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLR--AYPGTVVFVSHDRHFMDRVAT--- 229
Cdd:cd03260 132 EVKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHNMQQAARVADrta 211
|
250
....*....|...
gi 1844953743 230 -----CLVELTPT 237
Cdd:cd03260 212 fllngRLVEFGPT 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
361-525 |
1.62e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.96 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLDD-------GVT 433
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR--------LNGRPLADWSPaelarrrAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 434 LLDSLLTLP-------AM-------TQTQARTIL-------GCFLFSGEEVRKrigdLSMGERCR------LAFLKLYFS 486
Cdd:PRK13548 82 PQHSSLSFPftveevvAMgraphglSRAEDDALVaaalaqvDLAHLAGRDYPQ----LSGGEQQRvqlarvLAQLWEPDG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1844953743 487 GANLLVLDEPTNYLDIDSRERIEQAL----LRYPGAMVIVSHD 525
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLArqlaHERGLAVIVVLHD 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
353-571 |
1.64e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.88 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------QHPQTSIGYFSQElE 426
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAERGVVFQN-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 427 HLDDGVTLLDSL---LTLPAMTQTQ----ARTILGCFLFSGEEVRkRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNY 499
Cdd:PRK11248 80 GLLPWRNVQDNVafgLQLAGVEKMQrleiAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 500 LDIDSRERIEQALLRY---PGAMV-IVSHDRFFIRKLATKLLWLS------AERSPIAFSGTYDEyAEASLASESSPEQL 569
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwqeTGKQVlLITHDIEEAVFMATELVLLSpgpgrvVERLPLNFARRFVA-GESSRSIKSDPQFI 237
|
..
gi 1844953743 570 AR 571
Cdd:PRK11248 238 AM 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-226 |
1.76e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 70.16 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEY--AGKPL--FEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQ-TE 78
Cdd:COG4181 8 IIELRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR---------LAGQDlFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 ADEavfthayveegcpEHYAAKRR---------------LKELEAQMqdaaapcMESLLADYQEAAERymgldgyhwetq 143
Cdd:COG4181 79 LDE-------------DARARLRArhvgfvfqsfqllptLTALENVM-------LPLELAGRRDARAR------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLGRELWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSH 219
Cdd:COG4181 127 ARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTH 205
|
....*..
gi 1844953743 220 DRHFMDR 226
Cdd:COG4181 206 DPALAAR 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-196 |
1.77e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVmkEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqTEAD 80
Cdd:PRK09536 2 PMIDVSDLSV--EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV---------------LVAG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVfthayveegcpEHYAAKrrlkelEAQMQDAAAPCMESLLADYQEAAERYMG-------LDGYHW--ETQVERKLLQL 151
Cdd:PRK09536 65 DDV-----------EALSAR------AASRRVASVPQDTSLSFEFDVRQVVEMGrtphrsrFDTWTEtdRAAVERAMERT 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 152 GLGReLWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK09536 128 GVAQ-FADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-232 |
2.00e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 72.06 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 22 QVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDQWGWmgQQTEADEAVFTH----AYV--EEGCPE 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR----LGGEVL--QDSARGIFLPPHrrriGYVfqEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 HYAAKRRLkeleaqmQDAAAPCmeslladyqEAAERYMGLDGYhwetqVERkllqLGLGrELWDQPLGQLSGGQKTRAQL 175
Cdd:COG4148 91 HLSVRGNL-------LYGRKRA---------PRAERRISFDEV-----VEL----LGIG-HLLDRRPATLSGGERQRVAI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 176 ARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLV 232
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHSLDEVARLADHVV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-234 |
2.10e-13 |
|
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: 72.07 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsverRLPLDQWGWMgqqtEADEAVFThayveegcPEHyaaKRR 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEG----EIVLNGRTLF----DSRKGIFL--------PPE---KRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LKELeaqMQDAaapcmeSLLADYQEAAERYMGL---DGYHWETQVERKLLQLGLGrELWDQPLGQLSGGQKTRAQLARLM 179
Cdd:TIGR02142 77 IGYV---FQEA------RLFPHLSVRGNLRYGMkraRPSERRISFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 180 VREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVEL 234
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDPRkyeiLPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-220 |
2.19e-13 |
|
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: 70.02 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAG-KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQW----GWM 73
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgediREQDPVELrrkiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 74 GQQTeadeAVFTHAYVEEGCPehyAAKRRLKELEAQMQDAAAPCMESLLADYQEAAERYmgldgyhwetqverkllqlgl 153
Cdd:cd03295 81 IQQI----GLFPHMTVEENIA---LVPKLLKWPKEKIRERADELLALVGLDPAEFADRY--------------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 154 grelwdqPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWL----RAYPGTVVFVSHD 220
Cdd:cd03295 133 -------P-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHD 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-228 |
3.30e-13 |
|
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: 69.32 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 21 EQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTEADEAvfthayveegcpehyAAK 100
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT----VD-----GFDVVKEPA---------------EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 101 RRLKELEAQMQdaaapcmeslLADYQEAAE------RYMGLDGYHWETQVERKLLQLGLgRELWDQPLGQLSGGQKTRAQ 174
Cdd:cd03266 78 RRLGFVSDSTG----------LYDRLTAREnleyfaGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 175 LARLMVREPQLLLLDEPTNHLD----AASLEWLEVwLRAYPGTVVFVSHDRHFMDRVA 228
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDvmatRALREFIRQ-LRALGKCILFSTHIMQEVERLC 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
3.43e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG-------TLELDKGSVERRLPLDQWGWM 73
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeqptagQIMLDGVDLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 74 GQQTEAdeaVFTHAYVEE----GCPEHYAAKRRLKELEAQMQDaaapcmeslLADYQEAAERymgldgyhwetqverkll 149
Cdd:PRK11607 96 MFQSYA---LFPHMTVEQniafGLKQDKLPKAEIASRVNEMLG---------LVHMQEFAKR------------------ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 150 qlglgrelwdQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA-----SLEWLEVwLRAYPGTVVFVSHDR 221
Cdd:PRK11607 146 ----------KP-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrmQLEVVDI-LERVGVTCVMVTHDQ 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-236 |
3.77e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTE---ADEAV-FTHayve 90
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT----LD-----GVPVTgpgADRGVvFQK---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 egcpehyaakrrlkeleaqmqDAAAPCMESLlaDYQEAAERYMGLDGYHWETQVERKLLQLGLGrELWDQPLGQLSGGQK 170
Cdd:COG4525 85 ---------------------DALLPWLNVL--DNVAFGLRLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 171 TRAQLARLMVREPQLLLLDEPTNHLDAASLE-----WLEVWLRAYPGtVVFVSHDRH---FMdrvATCLVELTP 236
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREqmqelLLDVWQRTGKG-VFLITHSVEealFL---ATRLVVMSP 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-227 |
3.92e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.11 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmgqqteadeavfthayveegcpeh 96
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT----LD---------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 97 yaakrrlkeleaqmqdaaapcmESLLADYQEAAERYMGL---DGYHWETQverklLQLGLGRelwdqplgQLSGGQKTRA 173
Cdd:cd03247 63 ----------------------GVPVSDLEKALSSLISVlnqRPYLFDTT-----LRNNLGR--------RFSGGERQRL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVWLRAYPG-TVVFVSHDR---HFMDRV 227
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHHLtgiEHMDKI 166
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
354-513 |
4.08e-13 |
|
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: 72.01 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---QHPQTS--------IGYF 421
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgVPVSSLdqdevrrrVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQElEHLDDgVTLLDSLL------TLPAMTQTQARTILGCFLFSGEE-VRKRIGD----LSMGERCRLAFLKLYFSGANL 490
Cdd:TIGR02868 415 AQD-AHLFD-TTVRENLRlarpdaTDEELWAALERVGLADWLRALPDgLDTVLGEggarLSGGERQRLALARALLADAPI 492
|
170 180
....*....|....*....|...
gi 1844953743 491 LVLDEPTNYLDIDSRERIEQALL 513
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLL 515
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-229 |
6.58e-13 |
|
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: 68.30 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAG--KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWMGQ---QTEA 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA----------YINGysiRTDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DeavftHAYVEEG-CPEHyaakrrlkeleaqmqDAAAP---CMESLladyqeaaeRYMG-LDGYHWET---QVERKLLQL 151
Cdd:cd03263 71 K-----AARQSLGyCPQF---------------DALFDeltVREHL---------RFYArLKGLPKSEikeEVELLLRVL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 152 GLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW---LRAYPG-TVVFVSHDRHFMDRV 227
Cdd:cd03263 122 GLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR--AIWdliLEVRKGrSIILTTHSMDEAEAL 198
|
..
gi 1844953743 228 AT 229
Cdd:cd03263 199 CD 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-525 |
6.91e-13 |
|
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: 68.93 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERElFAELSLSVDR-GDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHP--QTSIGYF-SQELEH-----LDDGV 432
Cdd:cd03236 9 RYGPNS-FKLHRLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwDEILDEFrGSELQNyftklLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 TLL---DSLLTLPAMTQTQARTILG-----------CFLFSGEEVRKR-IGDLSMGERCRLAFLKLYFSGANLLVLDEPT 497
Cdd:cd03236 88 KVIvkpQYVDLIPKAVKGKVGELLKkkdergkldelVDQLELRHVLDRnIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 498 NYLDIDSR---ERIEQALLRYPGAMVIVSHD 525
Cdd:cd03236 168 SYLDIKQRlnaARLIRELAEDDNYVLVVEHD 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-550 |
7.09e-13 |
|
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: 67.90 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELfaELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQH------------PQTSIGYF 421
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaappadrPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQELEHLD--DGVTL-LDSLLTLPAMTQTQARTILGCFLFSGEEVRkRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:cd03298 79 NNLFAHLTveQNVGLgLSPGLKLTAEDRQAIEVALARVGLAGLEKR-LPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 499 YLDIDSRERIEQALL---RYPGAMVI-VSHDRFFIRKLATKLLWLsaERSPIAFSG 550
Cdd:cd03298 158 ALDPALRAEMLDLVLdlhAETKMTVLmVTHQPEDAKRLAQRVVFL--DNGRIAAQG 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-238 |
7.70e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlPldqwgwmgqqtEADEAVF--THAYVEEGc 93
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--P-----------AGARVLFlpQRPYLPLG- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 pehyaakrRLKEL------EAQMQDAAapcmeslladYQEAAERyMGLDgyHWETQVERkllqlglgRELWDQplgQLSG 167
Cdd:COG4178 441 --------TLREAllypatAEAFSDAE----------LREALEA-VGLG--HLAERLDE--------EADWDQ---VLSL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRA-YPG-TVVFVSHdRHFMDRVATCLVELTPTG 238
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
373-540 |
8.53e-13 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 67.90 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 373 SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-------------------RQHpqtsIGYFSQELeHLDDGVT 433
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekelaafrRRH----IGFVFQSF-NLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 434 LLDSLLtLPAMTQT--------QARTILgcflfsgEEV------RKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNY 499
Cdd:cd03255 99 ALENVE-LPLLLAGvpkkerreRAEELL-------ERVglgdrlNHYPSELSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 500 LDIDSRERIEQALLR----YPGAMVIVSHDRFFIRkLATKLLWLS 540
Cdd:cd03255 171 LDSETGKEVMELLRElnkeAGTTIVVVTHDPELAE-YADRIIELR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
373-561 |
9.46e-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: 68.36 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 373 SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV---------------RQHpQTSIGYFSQELeHLDDGVTLLDS 437
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalRQL-RRQIGMIFQQF-NLIERLSVLEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 438 LLT--LPAMTQTqaRTILGcfLFSGEEVR----------------KRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNY 499
Cdd:cd03256 99 VLSgrLGRRSTW--RSLFG--LFPKEEKQralaalervglldkayQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 500 LDIDSRERIEQALLRYP---GAMVIVS-HDRFFIRKLATKLLWLSAERspIAFSGTYDEYAEASLA 561
Cdd:cd03256 175 LDPASSRQVMDLLKRINreeGITVIVSlHQVDLAREYADRIVGLKDGR--IVFDGPPAELTDEVLD 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
354-525 |
1.00e-12 |
|
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: 67.88 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYG----ERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------QHPQTSIGYFSQ 423
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 424 E---LEHLddgvTLLDSL---LTLPAMTQTQARTILGCFLfsgEEV------RKRIGDLSMGERCRLAFLKLYFSGANLL 491
Cdd:cd03293 81 QdalLPWL----TVLDNValgLELQGVPKAEARERAEELL---ELVglsgfeNAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1844953743 492 VLDEPTNYLDIDSRERIEQALLR----YPGAMVIVSHD 525
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
372-525 |
1.01e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---QHPqtsigyFSQELEHLDD-GV------------TLL 435
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVP------FKRRKEFARRiGVvfgqrsqlwwdlPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 436 DSLLTLPAM---TQTQARTILGCF--LFSGEE-----VRKrigdLSMGER--CRLAflklyfsgANLL------VLDEPT 497
Cdd:COG4586 115 DSFRLLKAIyriPDAEYKKRLDELveLLDLGElldtpVRQ----LSLGQRmrCELA--------AALLhrpkilFLDEPT 182
|
170 180 190
....*....|....*....|....*....|..
gi 1844953743 498 NYLDIDSRERIEQALLRY---PGAMVIV-SHD 525
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnreRGTTILLtSHD 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-198 |
1.14e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLfeQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWMGQQTEADEA- 82
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL----------TLNGQDHTTTPp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 -------------VFTHAYVEE--GCPEHYAAKrrlkeleaqmqdaaapcmeslLADYQEAaerymgldgyhwetQVERK 147
Cdd:PRK10771 69 srrpvsmlfqennLFSHLTVAQniGLGLNPGLK---------------------LNAAQRE--------------KLHAI 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 148 LLQLGLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA 198
Cdd:PRK10771 114 ARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-202 |
1.15e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRLpldqwgwmgqqteAD 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI--SL-------------CG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAYVeegcpehyaakrrlkeleAQMQDAAAPCMESLLADYQEAAE-----RYMGLDGYHWETQVErKLLQLGLGR 155
Cdd:PRK13537 69 EPVPSRARH------------------ARQRVGVVPQFDNLDPDFTVRENllvfgRYFGLSAAAARALVP-PLLEFAKLE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1844953743 156 ELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD--AASLEW 202
Cdd:PRK13537 130 NKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMW 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-234 |
1.30e-12 |
|
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: 67.13 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 25 LEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-------ERRLPLDQWGWMGQQteaDEAVFTHAYVEEGCPEHY 97
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvTAAPPADRPVSMLFQ---ENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 98 AAKRRLKELEAQMQDAAApcmeslladyqeaaeRYMGLDGyhwetqverKLLQLGlgrelwdqplGQLSGGQKTRAQLAR 177
Cdd:cd03298 96 SPGLKLTAEDRQAIEVAL---------------ARVGLAG---------LEKRLP----------GELSGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 178 LMVREPQLLLLDEPTNHLDAA---SLEWLEVWLRAYPG-TVVFVSHDRHFMDRVATCLVEL 234
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPAlraEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
349-525 |
1.30e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.19 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRY----GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------QHPQTSI 418
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 419 GYFSQElehlddgvtllDSLL---------TLPAMTQTQARtilgcflfsgEEVRKRIGD-----------------LSM 472
Cdd:COG1116 83 GVVFQE-----------PALLpwltvldnvALGLELRGVPK----------AERRERAREllelvglagfedayphqLSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 473 GERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLR----YPGAMVIVSHD 525
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwqeTGKTVLFVTHD 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
351-577 |
1.38e-12 |
|
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: 70.32 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 351 RSLVRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAA---GKVRQHPQ---------- 415
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRdllelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 416 -TSIGYFSQELEHLDDGVTLLDSL---LTLPAMTQTQART-ILGCFLFSGEEVRKR--IGDLSMGERCRLAFLKLYFSGA 488
Cdd:COG1123 82 gRRIGMVFQDPMTQLNPVTVGDQIaeaLENLGLSRAEARArVLELLEAVGLERRLDryPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 489 NLLVLDEPTNYLDIDSRERIEQALLR----YPGAMVIVSHDRFFIRKLATKLLWLSAERspIAFSGTYDEYAEASLASES 564
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRElqreRGTTVLLITHDLGVVAEIADRVVVMDDGR--IVEDGPPEEILAAPQALAA 239
|
250
....*....|...
gi 1844953743 565 SPEQLARANERRQ 577
Cdd:COG1123 240 VPRLGAARGRAAP 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
368-545 |
1.70e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 65.64 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 368 LFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLvGELQPAA-GKVRQHPQTSIGYFSQElehlddgvtlldslltlPAMTQ 446
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGsGRIGMPEGEDLLFLPQR-----------------PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 447 TQARTILgCFLFSGEevrkrigdLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYpGAMVI-VSHd 525
Cdd:cd03223 78 GTLREQL-IYPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL-GITVIsVGH- 146
|
170 180
....*....|....*....|
gi 1844953743 526 RFFIRKLATKLLWLSAERSP 545
Cdd:cd03223 147 RPSLWKFHDRVLDLDGEGGW 166
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
353-532 |
1.86e-12 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 66.99 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGEREL----FAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-------RQHPQTSIGY- 420
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVlfngqslSKLSSNERAKl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 421 ------FSQELEHLDDGVTLLDSL---LTLPAMTQTQARTILGCFLFS---GEEVRKRIGDLSMGERCRLAFLKLYFSGA 488
Cdd:TIGR02211 81 rnkklgFIYQFHHLLPDFTALENVampLLIGKKSVKEAKERAYEMLEKvglEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1844953743 489 NLLVLDEPTNYLDIDSRERIEQALLR----YPGAMVIVSHDRFFIRKL 532
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLElnreLNTSFLVVTHDLELAKKL 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-234 |
1.92e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWM-GQQTEadeavfthayveeg 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV----------WLdGEHIQ-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpeHYAAKRRLKELEAQMQDAAAP---CMESLLA----DYQEAAERYMGLDgyhwETQVERKLLQLGLgRELWDQPLGQL 165
Cdd:PRK10253 73 ---HYASKEVARRIGLLAQNATTPgdiTVQELVArgryPHQPLFTRWRKED----EEAVTKAMQATGI-THLADQSVDTL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 166 SGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLVEL 234
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHqidlLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
364-524 |
1.93e-12 |
|
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: 66.40 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGelqpaagkvrqHPQTSIgyfsqelehlDDGVTLLD--SLLTL 441
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-----------HPKYEV----------TEGEILFKgeDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 PamtqTQARTILGCFL-------FSGEEVRKRIGDL----SMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQ 510
Cdd:cd03217 70 P----PEERARLGIFLafqyppeIPGVKNADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170
....*....|....*..
gi 1844953743 511 AL--LRYPG-AMVIVSH 524
Cdd:cd03217 146 VInkLREEGkSVLIITH 162
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
354-554 |
1.95e-12 |
|
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: 67.25 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGEREL-FAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-------RQHPQTS----IGYF 421
Cdd:cd03254 3 IEFENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidiRDISRKSlrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQElEHLDDGvTLLDSlLTLPAMTQTQARTILGC----------FLFSG--EEVRKRIGDLSMGERCRLAFLKLYFSGAN 489
Cdd:cd03254 83 LQD-TFLFSG-TIMEN-IRLGRPNATDEEVIEAAkeagahdfimKLPNGydTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 490 LLVLDEPTNYLDIDSRERIEQAL--LRYPGAMVIVSHdRFFIRKLATKLLWLsaERSPIAFSGTYDE 554
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH-RLSTIKNADKILVL--DDGKIIEEGTHDE 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
355-571 |
2.16e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.09 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 355 RLERAAFRYGERELfaELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV----RQHPQTSIG-----YFSQE- 424
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngQDLTALPPAerpvsMLFQEn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 425 --LEHLD--DGVTL-LDSLLTLPAMTQTQARTILGCFLFSGEEVRKRiGDLSMGERCRLAFLKLYFSGANLLVLDEPTNY 499
Cdd:COG3840 81 nlFPHLTvaQNIGLgLRPGLKLTAEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 500 LDIDSRER----IEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERspIAFSGTYDEyaeasLASESSPEQLAR 571
Cdd:COG3840 160 LDPALRQEmldlVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR--IAADGPTAA-----LLDGEPPPALAA 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
370-526 |
2.21e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.66 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 370 AELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEHLDD--GVTLLDSLLtLPAMTQT 447
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRkiGVVFQDFRL-LPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 448 QARTI-LGCFLFSGEEVRKRIGD-----------------LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIE 509
Cdd:cd03292 97 ENVAFaLEVTGVPPREIRKRVPAalelvglshkhralpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180
....*....|....*....|
gi 1844953743 510 QAL--LRYPGAMVIVS-HDR 526
Cdd:cd03292 177 NLLkkINKAGTTVVVAtHAK 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-64 |
2.32e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 2.32e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERR 64
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-199 |
2.48e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELdKGS-----VE-RRLPLDQW----GWMGQqteadEAVFT 85
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSlkingIElRELDPESWrkhlSWVGQ-----NPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 86 HAYVEE----GCPEhyAAkrrlkelEAQMQDAAApcmeslLADYQEAAERymgldgyhwetqverklLQLGLGRELWDQP 161
Cdd:PRK11174 436 HGTLRDnvllGNPD--AS-------DEQLQQALE------NAWVSEFLPL-----------------LPQGLDTPIGDQA 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 1844953743 162 LGqLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:PRK11174 484 AG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-219 |
2.65e-12 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 69.68 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQW---------GWMGQQTEadeaVF 84
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV--RLdgaDLKQWdretfgkhiGYLPQDVE----LF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 thayveEGCpehyaakrrLKELEAQMQDAAAPcmESLLadyqEAAErymgLDGYHwetqveRKLLQLGLGrelWDQPLGQ 164
Cdd:TIGR01842 405 ------PGT---------VAENIARFGENADP--EKII----EAAK----LAGVH------ELILRLPDG---YDTVIGP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 165 ----LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA---ASLEWLEVWLRAYPGTVVFVSH 219
Cdd:TIGR01842 451 ggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEegeQALANAIKALKARGITVVVITH 512
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-429 |
2.70e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.27 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 24 ELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER------RLPLDQWgwmgQQTEADEAvfthayveegcpehy 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSqfshitRLSFEQL----QKLVSDEW--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 98 aaKRRLKELEAQMQDAAApcmeslladyQEAAEryMGLDGYHWETQVERKLLQLGLGReLWDQPLGQLSGGQKTRAQLAR 177
Cdd:PRK10938 84 --QRNNTDMLSPGEDDTG----------RTTAE--IIQDEVKDPARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 178 LMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHDRH----FMDRVATcLVELTPTgcrkyrggyteyt 250
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDeipdFVQFAGV-LADCTLA------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 251 rqkelelrtqeqlyrkqqllreqleesirtyrqwfHQGEKNAQMAEVPIqrgyfqgragahvsrmnAKMKELERLEGNRV 330
Cdd:PRK10938 215 -----------------------------------ETGEREEILQQALV-----------------AQLAHSEQLEGVQL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 331 EKPREAAHlKVKLSASDfasrSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGElQPAA--- 407
Cdd:PRK10938 243 PEPDEPSA-RHALPANE----PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGysn 316
|
410 420 430
....*....|....*....|....*....|...
gi 1844953743 408 -----GKVRQHPQT------SIGYFSQELeHLD 429
Cdd:PRK10938 317 dltlfGRRRGSGETiwdikkHIGYVSSSL-HLD 348
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-227 |
2.73e-12 |
|
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: 69.39 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQW---------GWMGQQTEadea 82
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV--RLdgaDLSQWdreelgrhiGYLPQDVE---- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 VF--THAyveegcpEHYAakrRLKELEAQMQDAAApcmesLLADyqeAAERYMGL-DGYhwETQVerkllqlglgrelwD 159
Cdd:COG4618 417 LFdgTIA-------ENIA---RFGDADPEKVVAAA-----KLAG---VHEMILRLpDGY--DTRI--------------G 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLE---VWLRAYPGTVVFVSHDRHFMDRV 227
Cdd:COG4618 463 EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAaaiRALKARGATVVVITHRPSLLAAV 533
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
316-514 |
2.92e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.32 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 316 NAKMKELERLEGNRVEKPREAAHLKVKLSASdfASRSLVRLERAAFR--YGERELFAELSLSVDRGDRLAVLGPNGSGKT 393
Cdd:PRK13536 4 RAVAEEAPRRLELSPIERKHQGISEAKASIP--GSMSTVAIDLAGVSksYGDKAVVNGLSFTVASGECFGLLGPNGAGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 394 TLLKLLVGELQPAAGKVR----QHP------QTSIGYFSQeLEHLDDGVTLLDSLLTLPAMTQTQARTI------LGCFL 457
Cdd:PRK13536 82 TIARMILGMTSPDAGKITvlgvPVPararlaRARIGVVPQ-FDNLDLEFTVRENLLVFGRYFGMSTREIeavipsLLEFA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 458 FSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSR----ERIEQALLR 514
Cdd:PRK13536 161 RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhliwERLRSLLAR 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
354-532 |
2.98e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.23 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLDD-- 430
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL--------VNGQDLSRLKRre 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 --------GVT-----LLDSL-----LTLPAMtqtqartILGcflFSGEEVRKRIGD-----------------LSMGER 475
Cdd:COG2884 74 ipylrrriGVVfqdfrLLPDRtvyenVALPLR-------VTG---KSRKEIRRRVREvldlvglsdkakalpheLSGGEQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 476 CRLAFlklyfsgA----N---LLVLDEPTNYLDIDSRERIEQALLRY--PGAMVIV-SHDRFFIRKL 532
Cdd:COG2884 144 QRVAI-------AralvNrpeLLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRM 203
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-196 |
3.11e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 18 PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDQwgwmGQQTEADEAVFThAYveegcpehy 97
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQ----IDG----KTATRGDRSRFM-AY--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 98 aakrrLKELEAQMQDAAApcMESLladyqeaaERYMGLDGYHWETQVERKLLQLGL-GRElwDQPLGQLSGGQKTRAQLA 176
Cdd:PRK13543 87 -----LGHLPGLKADLST--LENL--------HFLCGLHGRRAKQMPGSALAIVGLaGYE--DTLVRQLSAGQKKRLALA 149
|
170 180
....*....|....*....|
gi 1844953743 177 RLMVREPQLLLLDEPTNHLD 196
Cdd:PRK13543 150 RLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-220 |
3.40e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV---ERRL----PLDQWGWMGQQTEAde 81
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigEKRMndvpPAERGVGMVFQSYA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 aVFTHAYVEE----GCPEHYAAKRrlkELEAQMQDAAapcmeslladyqeaaerymgldgyhwetqverKLLQLGlgrEL 157
Cdd:PRK11000 86 -LYPHLSVAEnmsfGLKLAGAKKE---EINQRVNQVA--------------------------------EVLQLA---HL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 158 WDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAslewLEVWLRA--------YPGTVVFVSHD 220
Cdd:PRK11000 127 LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA----LRVQMRIeisrlhkrLGRTMIYVTHD 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-191 |
3.53e-12 |
|
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: 66.41 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWMGQQTeadeavF 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI----------LLDGQD------I 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAyveegcPEHYAAKRRLKELEaqmQDAAApcMESL-LADYQEAAERYMGLDGYHWETQVERKLLQLGLGReLWDQPLG 163
Cdd:cd03218 65 TKL------PMHKRARLGIGYLP---QEASI--FRKLtVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKAS 132
|
170 180
....*....|....*....|....*...
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEP 191
Cdd:cd03218 133 SLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
5-198 |
5.19e-12 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 65.65 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLfeQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLE-------LDKGSVERRLPLDQWGWMGQQt 77
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEpasgsikVNDQSHTGLAPYQRPVSMLFQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 eaDEAVFTHAYVEEGCPEHYAAKRRLKELEAQMQDAAApcmeslladyqeaaeRYMGLDGYhwetqverkllqlglgrel 157
Cdd:TIGR01277 78 --ENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAA---------------QQVGIADY------------------- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1844953743 158 WDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA 198
Cdd:TIGR01277 122 LDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-231 |
5.29e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGtleLDKGSV-ERRLpldqwgwMGQQTeadeavftHAYVEEGcpehyAAKR 101
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSSgEVSL-------VGQPL--------HQMDEEA-----RAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 102 RLKELEAQMQD-AAAPCMESLLADYQEAAERymGLDGYHWETQVERKLLQLGLGRELWDQPlGQLSGGQKTRAQLARLMV 180
Cdd:PRK10584 86 RAKHVGFVFQSfMLIPTLNALENVELPALLR--GESSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 181 REPQLLLLDEPTNHLDAASLEWLEVWL----RAYPGTVVFVSHDRHFMDRVATCL 231
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRL 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-220 |
5.30e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFE-----QVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqWGWMGQQTEA 79
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE-------WIFKDEKNKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEAVFTHAYVEEGCPEHYAAK-RRLKELEAQM----QDAAAPCME------------SLLADYQEAAERymgldgyhwet 142
Cdd:PRK13651 76 KTKEKEKVLEKLVIQKTRFKKiKKIKEIRRRVgvvfQFAEYQLFEqtiekdiifgpvSMGVSKEEAKKR----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 143 qvERKLLQL-GLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEVWLRAYPG--TVVFVS 218
Cdd:PRK13651 145 --AAKYIELvGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQgkTIILVT 222
|
..
gi 1844953743 219 HD 220
Cdd:PRK13651 223 HD 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-220 |
5.43e-12 |
|
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: 65.95 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 21 EQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlpldqwgwmGQQteadeavfthayVEEGCPEHYAAK 100
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE---------GKQ------------ITEPGPDRMVVF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 101 RRLKELE-AQMQDAAAPCMESLLADYQEAAERymgldgyhweTQVERKLLQLGLgRELWDQPLGQLSGGQKTRAQLARLM 179
Cdd:TIGR01184 61 QNYSLLPwLTVRENIALAVDRVLPDLSKSERR----------AIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARAL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844953743 180 VREPQLLLLDEPTNHLDAASL-----EWLEVWLRAYPgTVVFVSHD 220
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRgnlqeELMQIWEEHRV-TVLMVTHD 174
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
354-525 |
6.10e-12 |
|
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: 65.78 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERE-LFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--------QHP---QTSIGYF 421
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgedireQDPvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQE---LEHL--DDGVTLLDSLLTLP-AMTQTQARTILGCFLFSGEEVRKRI-GDLSMGERCRLAFLKLYFSGANLLVLD 494
Cdd:cd03295 81 IQQiglFPHMtvEENIALVPKLLKWPkEKIRERADELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1844953743 495 EPTNYLDIDSRERIEQALLRYPGAM----VIVSHD 525
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELgktiVFVTHD 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-197 |
6.72e-12 |
|
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: 65.37 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLElDKGSVERRLPLDqwgwmGQQTEADEAVFTHAYVEEGC---PE---- 95
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSGQILFN-----GQPRKPDQFQKCVAYVRQDDillPGltvr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 ---HYAAKRRLKELEAQMQDAAapcmeslladyqeaaerymgldgyhwETQVERkLLQLGLGReLWDQPLGQLSGGQKTR 172
Cdd:cd03234 100 etlTYTAILRLPRKSSDAIRKK--------------------------RVEDVL-LRDLALTR-IGGNLVKGISGGERRR 151
|
170 180
....*....|....*....|....*
gi 1844953743 173 AQLARLMVREPQLLLLDEPTNHLDA 197
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-226 |
6.86e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 65.12 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEY-AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlpldqwgwmGQQTEA--DE 81
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN---------GQDVSDlrGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVfthAYVEEGCPEHYAAKRRLKELEAQmqDAAAPCMESLLADYQEAAERYMGLdgyhwetqverkLLQLGLGRELWDQP 161
Cdd:cd03292 72 AI---PYLRRKIGVVFQDFRLLPDRNVY--ENVAFALEVTGVPPREIRKRVPAA------------LELVGLSHKHRALP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 162 lGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA-SLEWLEVW--LRAYPGTVVFVSHDRHFMDR 226
Cdd:cd03292 135 -AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDtTWEIMNLLkkINKAGTTVVVATHAKELVDT 201
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-196 |
7.16e-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: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 11 MKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrLPLDQWGWMGQQTEADEAVFTHAYVE 90
Cdd:cd03237 6 MKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE--IELDTVSYKPQYIKADYEGTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 91 EGCPEHYAAKrrlkeleaqmqdaaapcmeslladyqeaaerymgldgyHWETQVeRKLLQLglgRELWDQPLGQLSGGQK 170
Cdd:cd03237 84 SITKDFYTHP--------------------------------------YFKTEI-AKPLQI---EQILDREVPELSGGEL 121
|
170 180
....*....|....*....|....*.
gi 1844953743 171 TRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:cd03237 122 QRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-192 |
8.08e-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: 65.15 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQ---WGwMGQQTEaDEAVFTHAYVEE-- 91
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrdiTGLPPHErarAG-IGYVPE-GRRIFPELTVEEnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 92 --GCpehYAAKRRLKEleaqmqdaaapcmesllADYQEAAERYMGLdgyhwetqverkllqlglgRELWDQPLGQLSGGQ 169
Cdd:cd03224 97 llGA---YARRRAKRK-----------------ARLERVYELFPRL-------------------KERRKQLAGTLSGGE 137
|
170 180
....*....|....*....|....*
gi 1844953743 170 ktRAQLA--RLMVREPQLLLLDEPT 192
Cdd:cd03224 138 --QQMLAiaRALMSRPKLLLLDEPS 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-191 |
8.14e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.44 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQWGWMG---- 74
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgediTHLPMHKRARLGigyl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 75 -QqteadEA-VFTHAYVEEGCpehYAAkrrlkeLEAQMQDAAA--PCMESLLADyqeaaerymgldgyhwetqverkllq 150
Cdd:COG1137 84 pQ-----EAsIFRKLTVEDNI---LAV------LELRKLSKKEreERLEELLEE-------------------------- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1844953743 151 LGLGReLWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEP 191
Cdd:COG1137 124 FGITH-LRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-196 |
8.37e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.40 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTEADEA- 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT----VD-----GEDLTDSKKd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 ----------VF------THAYVEEGCpehyaakrrlkeLEAQMQdaaapcmeSLLADYQEAAERYMGLdgyhwetqver 146
Cdd:COG1126 72 inklrrkvgmVFqqfnlfPHLTVLENV------------TLAPIK--------VKKMSKAEAEERAMEL----------- 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1844953743 147 kLLQLGLGrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:COG1126 121 -LERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-196 |
1.12e-11 |
|
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: 67.50 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 26 EVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRL-----PldqwgwmgQ--QTEADEAVfthayveegcpehya 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLkisykP--------QyiSPDYDGTV--------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 99 akrrlkeleaqmqdaaapcmESLLadYQEAAERYmglDGYHWETQVERKllqLGLGReLWDQPLGQLSGGqktraQLARL 178
Cdd:COG1245 419 --------------------EEFL--RSANTDDF---GSSYYKTEIIKP---LGLEK-LLDKNVKDLSGG-----ELQRV 464
|
170 180
....*....|....*....|...
gi 1844953743 179 MV-----REPQLLLLDEPTNHLD 196
Cdd:COG1245 465 AIaaclsRDADLYLLDEPSAHLD 487
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
373-524 |
1.23e-11 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 63.22 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 373 SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigyfsqelehlddgvtlldslltlpamtqtqarti 452
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL----------------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 453 lgcflFSGEEV---------RKRIG---DLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQAL--LRYPG- 517
Cdd:cd03216 59 -----VDGKEVsfasprdarRAGIAmvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrLRAQGv 133
|
....*..
gi 1844953743 518 AMVIVSH 524
Cdd:cd03216 134 AVIFISH 140
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-226 |
1.45e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEAv 83
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL---------FERQSIKKDLC- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 fthAYVEEGCpehYAAKRRLKELEAQMQdaaapcmESLLADYQEAAERyMGLDgyhwetqverKLLQLGLGRELWDQPLG 163
Cdd:PRK13540 71 ---TYQKQLC---FVGHRSGINPYLTLR-------ENCLYDIHFSPGA-VGIT----------ELCRLFSLEHLIDYPCG 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWL---RAYPGTVVFVSHDRHFMDR 226
Cdd:PRK13540 127 LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIqehRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-202 |
1.58e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 2 TLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqTEADE 81
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---------------TVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVfthayveegcPEHYAAKRRLKELEAQMQ--DAAAPCMESLLAdyqeaAERYMGLDGYHWETqVERKLLQLGLGRELWD 159
Cdd:PRK13536 104 PV----------PARARLARARIGVVPQFDnlDLEFTVRENLLV-----FGRYFGMSTREIEA-VIPSLLEFARLESKAD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD--AASLEW 202
Cdd:PRK13536 168 ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIW 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-228 |
1.74e-11 |
|
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: 64.52 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGK----PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtLEL-DKGSVErrlpldqwgWMGQqte 78
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVL---------VDGT--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 adeAVFThayveegcpehyAAKRRLKELEAQM----------------QDAAAPcmesLLADYQEAAERymgldgyhwET 142
Cdd:cd03258 68 ---DLTL------------LSGKELRKARRRIgmifqhfnllssrtvfENVALP----LEIAGVPKAEI---------EE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 143 QVERKLLQLGLGRELWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVS 218
Cdd:cd03258 120 RVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLIT 198
|
250
....*....|....
gi 1844953743 219 HD----RHFMDRVA 228
Cdd:cd03258 199 HEmevvKRICDRVA 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-196 |
2.10e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 26 EVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRL-----PldqwgwmgQQTEADEAVfthayveegcpehyaak 100
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELkisykP--------QYIKPDYDG----------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 101 rRLKELEAQMQDAaapcmeslladyqeaaerymgLDGYHWETQVERKllqLGLGReLWDQPLGQLSGGQKTRAQLARLMV 180
Cdd:PRK13409 416 -TVEDLLRSITDD---------------------LGSSYYKSEIIKP---LQLER-LLDKNVKDLSGGELQRVAIAACLS 469
|
170
....*....|....*.
gi 1844953743 181 REPQLLLLDEPTNHLD 196
Cdd:PRK13409 470 RDADLYLLDEPSAHLD 485
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-232 |
2.34e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.96 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSverrLPLDqwgwmGQQTEADeavfthay 88
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD----LIVD-----GLKVNDP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 veegcpehyAAKRRLKELEAQM---QDAAAPCMESLladyqeaaERYM-------GLDGYHWETQVERKLLQLGLGRELW 158
Cdd:PRK09493 69 ---------KVDERLIRQEAGMvfqQFYLFPHLTAL--------ENVMfgplrvrGASKEEAEKQARELLAKVGLAERAH 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 159 DQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA-SLEWLEVwLR--AYPG-TVVFVSHDRHFMDRVATCLV 232
Cdd:PRK09493 132 HYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKV-MQdlAEEGmTMVIVTHEIGFAEKVASRLI 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
352-411 |
2.37e-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: 65.50 E-value: 2.37e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL 63
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-227 |
2.52e-11 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 62.45 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEadeavf 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------VDGKEVS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 thayveegcpehyaakrrlkeleaqmqdaaapcmeslLADYQEAaerymgldgyhwetqverklLQLGLGRelwdqpLGQ 164
Cdd:cd03216 66 -------------------------------------FASPRDA--------------------RRAGIAM------VYQ 82
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWL-EVW--LRAYPGTVVFVSH----DRHFMDRV 227
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLfKVIrrLRAQGVAVIFISHrldeVFEIADRV 152
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
362-496 |
2.81e-11 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 63.72 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------------QHPQTSIGYFSQElEHLD 429
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditklpmhKRARLGIGYLPQE-ASIF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 430 DGVTLLDSLLTLPAMT---QTQARTILGCFL--FSGEEVRKRIGD-LSMGERCRLAFLKLYFSGANLLVLDEP 496
Cdd:cd03218 88 RKLTVEENILAVLEIRglsKKEREEKLEELLeeFHITHLRKSKASsLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-192 |
2.94e-11 |
|
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: 63.85 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEavfTHAYVEEG---CPEHyaa 99
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR---------FDGEDITGLP---PHRIARLGigyVPEG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 100 kRRL-KELeaqmqdaaaPCMESLLAdyqeAAERYMGLDGYHWetQVER------KLlqlglgRELWDQPLGQLSGGQktR 172
Cdd:COG0410 87 -RRIfPSL---------TVEENLLL----GAYARRDRAEVRA--DLERvyelfpRL------KERRRQRAGTLSGGE--Q 142
|
170 180
....*....|....*....|..
gi 1844953743 173 AQLA--RLMVREPQLLLLDEPT 192
Cdd:COG0410 143 QMLAigRALMSRPKLLLLDEPS 164
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-219 |
3.05e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRLPLDQWGwmgqqteADEAV 83
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG-------REASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 FTHAYveegcpehyaakrrlkeleaqmqdaaapcmesLLADYQEAAERymgldgyhwetqverkLLQLGLGRE-LWDQPL 162
Cdd:COG2401 103 IDAIG--------------------------------RKGDFKDAVEL----------------LNAVGLSDAvLWLRRF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-----AASLEWLEVWLRAyPGTVVFVSH 219
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtakRVARNLQKLARRA-GITLVVATH 195
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-199 |
3.13e-11 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 63.86 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEY-AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV---------ERRLPLDQW--- 70
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditkLRGKKLRKLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 71 -GWMGQqteadeavfthayveegcpeHYAAKRRLKELEAQMQD--AAAPCMESLL-----ADYQEAAE--RYMGLDGYHw 140
Cdd:TIGR02315 81 iGMIFQ--------------------HYNLIERLTVLENVLHGrlGYKPTWRSLLgrfseEDKERALSalERVGLADKA- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 141 etqverkllqlglgrelwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:TIGR02315 140 ------------------YQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
362-554 |
3.27e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLK------------LLVGELQ---PAAgKVRQHPQTSIGYFSQelE 426
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKvndPKV-DERLIRQEAGMVFQQ--F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 427 HLDDGVTLLDSLLTLP--------AMTQTQARTILGCFLFSgEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:PRK09493 87 YLFPHLTALENVMFGPlrvrgaskEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 499 YLDIDSRE---RIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAERspIAFSGTYDE 554
Cdd:PRK09493 166 ALDPELRHevlKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR--IAEDGDPQV 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-196 |
3.65e-11 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 63.40 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEY-AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLD----QWGWMGQQT 77
Cdd:cd03253 5 NVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdiREVTLDslrrAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 eadeaVFTHAYVEegcpeHYAAKRRLKELEAQMQDAAapcmeslladyqEAA---ERYMGL-DGYhwETQV-ERKLlqlg 152
Cdd:cd03253 85 -----VLFNDTIG-----YNIRYGRPDATDEEVIEAA------------KAAqihDKIMRFpDGY--DTIVgERGL---- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 153 lgrelwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:cd03253 137 -----------KLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
379-537 |
3.73e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 63.08 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 379 GDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQT---------------SIGYFSQELE---HLDDGVTLLDSLLT 440
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQYAlfpHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 441 LPAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLR----YP 516
Cdd:cd03297 103 KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLN 182
|
170 180
....*....|....*....|.
gi 1844953743 517 GAMVIVSHDRFFIRKLATKLL 537
Cdd:cd03297 183 IPVIFVTHDLSEAEYLADRIV 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-524 |
3.77e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--QHP---------Q 415
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlnGQPiadyseaalR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 416 TSIGYFSQELeHLDDGvTLLDSLL------TLPAMTQTQARTILGCFLFSGEEVRKRIGD----LSMGERCRLAFLKLYF 485
Cdd:PRK11160 414 QAISVVSQRV-HLFSA-TLRDNLLlaapnaSDEALIEVLQQVGLEKLLEDDKGLNAWLGEggrqLSGGEQRRLGIARALL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1844953743 486 SGANLLVLDEPTNYLDIDSRERIEQALLRYPG--AMVIVSH 524
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITH 532
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-192 |
3.94e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 63.31 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEAvftH------- 86
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIR---------LDGEDITKLPP---Heraragi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 87 AYVEEGcpehyaakrrlKELEAQMQdaaapCMESLLadyqeaaeryMGLDGYhweTQVERKLLQLGLG-----RELWDQP 161
Cdd:TIGR03410 78 AYVPQG-----------REIFPRLT-----VEENLL----------TGLAAL---PRRSRKIPDEIYElfpvlKEMLGRR 128
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 162 LGQLSGGQKTRAQLARLMVREPQLLLLDEPT 192
Cdd:TIGR03410 129 GGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
354-512 |
4.39e-11 |
|
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: 63.02 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQhpqtsigyfsqelehldDG 431
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlrDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-----------------DG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTL----LDSLLTLPAMTQTQArtilgcFLFSG---------------EEVRK--------------------RIGD--- 469
Cdd:cd03251 64 HDVrdytLASLRRQIGLVSQDV------FLFNDtvaeniaygrpgatrEEVEEaaraanahefimelpegydtVIGErgv 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 470 -LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQAL 512
Cdd:cd03251 138 kLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
4.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAG-KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlpldqwgwmGQQteadea 82
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR---------GEP------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 vFTHAYVEEgcpehyaaKRRLKELEAQMQDAA--APCMESLLAdyqeAAERYMGLDGYHWETQVERKLLQLGLgRELWDQ 160
Cdd:PRK13652 68 -ITKENIRE--------VRKFVGLVFQNPDDQifSPTVEQDIA----FGPINLGLDEETVAHRVSSALHMLGL-EELRDR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 161 PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHD 220
Cdd:PRK13652 134 VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQ 197
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
363-507 |
4.54e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.25 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 363 YGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-------------------QHPQ-TSIGY-F 421
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaraasrrvaSVPQdTSLSFeF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 S--QELE-----HLD--DGVTLLDSLLTLPAMTQTQARTIlgcflfsgeeVRKRIGDLSMGERCRLAFLKLYFSGANLLV 492
Cdd:PRK09536 93 DvrQVVEmgrtpHRSrfDTWTETDRAAVERAMERTGVAQF----------ADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170
....*....|....*
gi 1844953743 493 LDEPTNYLDIDSRER 507
Cdd:PRK09536 163 LDEPTASLDINHQVR 177
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-199 |
5.05e-11 |
|
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: 63.02 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGK--PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLD----QWGWMGQQ 76
Cdd:cd03251 5 NVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvRDYTLAslrrQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 TeadeaVFTHAYVEEGcpehyAAKRRLKELEAQMQDAAApcmeslLAdyqEAAERYMGL-DGYHweTQV-ERKLlqlglg 154
Cdd:cd03251 85 V-----FLFNDTVAEN-----IAYGRPGATREEVEEAAR------AA---NAHEFIMELpEGYD--TVIgERGV------ 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 155 relwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03251 138 ---------KLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-199 |
5.15e-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: 62.18 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG--TLELDKGSV---ERRLPLDQW----GWMGQqteaDEAVFT 85
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlinGRPLDKRSFrkiiGYVPQ----DDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 86 HAYVEEGCpeHYAAKRRlkeleaqmqdaaapcmeslladyqeaaerymgldgyhwetqverkllqlglgrelwdqplgQL 165
Cdd:cd03213 96 TLTVRETL--MFAAKLR-------------------------------------------------------------GL 112
|
170 180 190
....*....|....*....|....*....|....
gi 1844953743 166 SGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-535 |
6.67e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 62.83 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLDD------GV------------ 432
Cdd:COG4674 28 DLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVL--------FGGTDLTGLDEheiarlGIgrkfqkptvfee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 -TLLDSLLtlpaMTQTQARTILGCFLF-SGEEVRKRI-----------------GDLSMGERCRLAFLKLYFSGANLLVL 493
Cdd:COG4674 100 lTVFENLE----LALKGDRGVFASLFArLTAEERDRIeevletigltdkadrlaGLLSHGQKQWLEIGMLLAQDPKLLLL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 494 DEPTNYLDIDSRERIEQALLRYPG--AMVIVSHDRFFIRKLATK 535
Cdd:COG4674 176 DEPVAGMTDAETERTAELLKSLAGkhSVVVVEHDMEFVRQIARK 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
7.83e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 26 EVNAGERIAIYGRNGIGKTTLLRLLAGTLEldkGSVERRL---PLDQW---------GWMGQQTEADEAVFTHAYVEEgc 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP---GSGSIQFagqPLEAWsaaelarhrAYLSQQQTPPFAMPVFQYLTL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 peHYAAKRRLKELEAQMQDAAApcmeslladyqeaaerymgldgyhwetqverkLLQLG--LGRelwdqPLGQLSGGQKT 171
Cdd:PRK03695 93 --HQPDKTRTEAVASALNEVAE--------------------------------ALGLDdkLGR-----SVNQLSGGEWQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 172 RAQLARLMVR-------EPQLLLLDEPTNHLDAASLEWLEVWLRAYP---GTVVFVSHD 220
Cdd:PRK03695 134 RVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
362-501 |
8.66e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGEL--QPAAGKVRQHPqtsigyfsqelEHLDDGVTLLDSLl 439
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD-----------NQFGREASLIDAI- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 440 tLPAMTQTQARTILG-CFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:COG2401 107 -GRKGDFKDAVELLNaVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-228 |
9.22e-11 |
|
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: 64.44 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAG------KPLfEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRLPlDQWGWMgqqt 77
Cdd:TIGR03269 279 IIKVRNVSKRYISvdrgvvKAV-DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVG-DEWVDM---- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 eadeavfthayVEEGCPEHYAAKRRLKELEaqmQDAAAPCMESLLADYQEAaeryMGLDgYHWETQVERKLLQLGL---- 153
Cdd:TIGR03269 353 -----------TKPGPDGRGRAKRYIGILH---QEYDLYPHRTVLDNLTEA----IGLE-LPDELARMKAVITLKMvgfd 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 154 ---GRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVWLRA---YPGTVVFVSHDRHFM-- 224
Cdd:TIGR03269 414 eekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITkVDVTHSILKAreeMEQTFIIVSHDMDFVld 493
|
....*.
gi 1844953743 225 --DRVA 228
Cdd:TIGR03269 494 vcDRAA 499
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
352-410 |
9.27e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 9.27e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 352 SLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
371-508 |
9.81e-11 |
|
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: 62.95 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSigyFSQELEHLDDGvTLLDSLLTLPAMTQTQAR 450
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS---FSSQFSWIMPG-TIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 451 TIL-GCFLFS-----GEEVRKRIGD----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERI 508
Cdd:cd03291 131 SVVkACQLEEditkfPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
354-554 |
9.87e-11 |
|
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: 62.12 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYG--ERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-----------RQHPQTSIGY 420
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 421 FSQELEHLDDgvTLLDSL-LTLPAMTQ---TQARTILGCFLF-------SGEEVRKRIGDLSMGERCRLAFLKLYFSGAN 489
Cdd:cd03252 81 VLQENVLFNR--SIRDNIaLADPGMSMervIEAAKLAGAHDFiselpegYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 490 LLVLDEPTNYLDIDSRERIEQALLRY-PGAMVIVSHDRFFIRKLATKLLWLsaERSPIAFSGTYDE 554
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIcAGRTVIIIAHRLSTVKNADRIIVM--EKGRIVEQGSHDE 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-222 |
1.06e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRLPLdQWGWMGQQTEAD 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-RIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVfthayveegcPEHYAAKRRLKeleaqmqdaaaPCMESllADYQEAAERymgldgyhwetqverklLQLGlgrELWDQ 160
Cdd:PRK09544 80 TTL----------PLTVNRFLRLR-----------PGTKK--EDILPALKR-----------------VQAG---HLIDA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 161 PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA----ASLEWLEVWLRAYPGTVVFVSHDRH 222
Cdd:PRK09544 117 PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvALYDLIDQLRRELDCAVLMVSHDLH 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
354-424 |
1.08e-10 |
|
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: 61.33 E-value: 1.08e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 354 VRLERAAFRYGERE-----LFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPqtSIGYFSQE 424
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQE 74
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
1.35e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEY-AGKPLFE---QVELEVNAGERIAIYGRNGIGKTTLLRLLAGtleLDKGSV-ERRLPldqwgwmGQ 75
Cdd:PRK10535 1 MTALLELKDIRRSYpSGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGC---LDKPTSgTYRVA-------GQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 76 QteadeavfthayVEEGCPEHYAAKRR------------LKELEAQmQDAAAPCMeslladyqeaaerYMGLDGYHWETQ 143
Cdd:PRK10535 71 D------------VATLDADALAQLRRehfgfifqryhlLSHLTAA-QNVEVPAV-------------YAGLERKQRLLR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLGRELWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW-----LRAYPGTVVFVS 218
Cdd:PRK10535 125 AQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE--EVMailhqLRDRGHTVIIVT 201
|
..
gi 1844953743 219 HD 220
Cdd:PRK10535 202 HD 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-234 |
1.36e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 12 KEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlplDQWGWMGQQTEADEAVFThayvee 91
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN---GQTINLVRDKDGQLKVAD------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 92 gcpehyaaKRRLKELEAQM----QDAAAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGRELWDQPLGQLSG 167
Cdd:PRK10619 84 --------KNQLRLLRTRLtmvfQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAASL-EWLEVWLR-AYPG-TVVFVSHDRHFMDRVATCLVEL 234
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQQlAEEGkTMVVVTHEMGFARHVSSHVIFL 225
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
232-335 |
1.39e-10 |
|
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: 57.97 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 232 VELTPTGCRKYRGGYTEYTRQKELELRTQEQLYRKQQLLREQLEESIRTYRQWfhqgEKNAQMAevpiqrgyfQGRagah 311
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAK----ASKAKQA---------QSR---- 63
|
90 100
....*....|....*....|....
gi 1844953743 312 vsrmnakMKELERLEgnRVEKPRE 335
Cdd:pfam12848 64 -------IKALEKME--RIEKPER 78
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
372-525 |
1.41e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 61.68 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRqhpqtsigYFSQELEHLD-DGVTLL---------DSLLTL 441
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR--------LAGQDLFALDeDARARLrarhvgfvfQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 PAMT-----------------QTQARTIL---GCflfsGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:COG4181 103 PTLTalenvmlplelagrrdaRARARALLervGL----GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
170 180
....*....|....*....|....*...
gi 1844953743 502 IDSRERIEQALL----RYPGAMVIVSHD 525
Cdd:COG4181 179 AATGEQIIDLLFelnrERGTTLVLVTHD 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-238 |
1.54e-10 |
|
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: 60.25 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlPldqwgwmgqqteADEAVFthaYVeegcP 94
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--P------------EGEDLL---FL----P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 95 EHyaakrrlkeleaqmqdaaaPcmeslladyqeaaerYMGLdgyhwetqverkllqlGLGREL----WDQplgQLSGGQK 170
Cdd:cd03223 71 QR-------------------P---------------YLPL----------------GTLREQliypWDD---VLSGGEQ 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 171 TRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHdRHFMDRVATCLVELTPTG 238
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-220 |
1.59e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLA-------GTLELDKGSV--------ERRLPLdq 69
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqsGTVFLGDKPIsmlssrqlARRLAL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 70 wgwMGQQTEADEAVFTHAYVEEGCPEHYAAKRRLKELEAQMQDAAapcMEslladyqeaaerymgldgyhwETQVErkll 149
Cdd:PRK11231 81 ---LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQA---ME---------------------QTRIN---- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 150 qlglgrELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD---AASLEWLEVWLRAYPGTVVFVSHD 220
Cdd:PRK11231 130 ------HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
372-523 |
1.66e-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: 61.23 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGK-------VRQHPQTS---IGYFSQElEHLDDGVTLLDSLL-- 439
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEPAEArrrLGFVSDS-TGLYDRLTARENLEyf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 440 ----TLPAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQAL--L 513
Cdd:cd03266 103 aglyGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIrqL 182
|
170
....*....|
gi 1844953743 514 RYPGAMVIVS 523
Cdd:cd03266 183 RALGKCILFS 192
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
372-554 |
1.82e-10 |
|
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: 61.59 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-----------------------QHPQTsigyFSQE--LE 426
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriarlgiartfQNPRL----FPELtvLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 427 ------HLDDGVTLLDSLLTLPAMTQT------QARTILGcFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLD 494
Cdd:COG0411 99 nvlvaaHARLGRGLLAALLRLPRARREereareRAEELLE-RVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 495 EPTNYLDIDSRERIEQALLRYPG----AMVIVSHDRFFIRKLATKLLWLSAERsPIAfSGTYDE 554
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRDergiTILLIEHDMDLVMGLADRIVVLDFGR-VIA-EGTPAE 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-220 |
1.90e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDKGSVERrLPldqwgwmGQQTEADEAVFTHAYVeegcpe 95
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptGGTILLRGQHIEG-LP-------GHQIARMGVVRTFQHV------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 hyaakRRLKE-------LEAQMQDAAAPCMESLLA--DY----QEAAERYMgldgyHWetqverkLLQLGLgRELWDQPL 162
Cdd:PRK11300 90 -----RLFREmtvienlLVAQHQQLKTGLFSGLLKtpAFrraeSEALDRAA-----TW-------LERVGL-LEHANRQA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPT---NHLDAASLEWLEVWLRAYPG-TVVFVSHD 220
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvTVLLIEHD 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-537 |
2.38e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLDQWGWMG 74
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 75 QQTEADEA-VFTHAYVEE----GCPEHYAAKRRLKELEAQMQ-----DAAApcmeSLLadyqEAAERYMgldgyhwetqV 144
Cdd:PRK15439 88 IYLVPQEPlLFPNLSVKEnilfGLPKRQASMQKMKQLLAALGcqldlDSSA----GSL----EVADRQI----------V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 145 ErkllqlglgrelwdqplgqlsggqktraqLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGT---VVFVSHDR 221
Cdd:PRK15439 150 E-----------------------------ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 222 HFMDRVATCLVELtptgcrkyRGGYTeytrqkelelrtqeqlyrkqqllreQLEESIRTYRqwfhqgekNAQM--AEVPI 299
Cdd:PRK15439 201 PEIRQLADRISVM--------RDGTI-------------------------ALSGKTADLS--------TDDIiqAITPA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 300 QRGyfqgragahvSRMNAKMKELERLEGNRVEKPREAAHLKV-KLSAsdfasrslvrleraafrygerELFAELSLSVDR 378
Cdd:PRK15439 240 ARE----------KSLSASQKLWLELPGNRRQQAAGAPVLTVeDLTG---------------------EGFRNISLEVRA 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 379 GDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV------------RQHPQTSIGYFSQELE----HLDDGVTLLDSLLT-- 440
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkeinalstAQRLARGLVYLPEDRQssglYLDAPLAWNVCALThn 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 441 -LPAMTQTQA--------RTILGcFLFSGEEvrKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQa 511
Cdd:PRK15439 369 rRGFWIKPARenavleryRRALN-IKFNHAE--QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQ- 444
|
570 580 590
....*....|....*....|....*....|
gi 1844953743 512 LLRYPG----AMVIVSHDRFFIRKLATKLL 537
Cdd:PRK15439 445 LIRSIAaqnvAVLFISSDLEEIEQMADRVL 474
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-237 |
2.40e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLagTLELDKGSVERrlpldqwgWMGQQTEADEAVF 84
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL--NRMNDKVSGYR--------YSGDVLLGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAYVEEgcpehyaAKRRLKELEAQMQDAAAPCMESLLADYQeaAERYMGLDGYHWETQVerKLLQLGL----GRELWDQ 160
Cdd:PRK14271 92 NYRDVLE-------FRRRVGMLFQRPNPFPMSIMDNVLAGVR--AHKLVPRKEFRGVAQA--RLTEVGLwdavKDRLSDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 161 PLgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVSHD----RHFMDRVATC---- 230
Cdd:PRK14271 161 PF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNlaqaARISDRAALFfdgr 239
|
....*..
gi 1844953743 231 LVELTPT 237
Cdd:PRK14271 240 LVEEGPT 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-219 |
2.80e-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: 60.56 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKP---LFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsverRLPLDqwgwmGQQTEAD 80
Cdd:cd03248 11 IVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG----QVLLD-----GKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAYVEEGCPEHYAAKRRLKE-LEAQMQDAAAPCMeslladyQEAAerymglDGYHWETQVErkLLQLGLGRELwD 159
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDnIAYGLQSCSFECV-------KEAA------QKAHAHSFIS--ELASGYDTEV-G 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVSH 219
Cdd:cd03248 146 EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
371-554 |
3.82e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSigyFSQELEHLDDGvTLLDSLLTLPAMTQTQAR 450
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS---FSPQTSWIMPG-TIKDNIIFGLSYDEYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 451 TIL-GCFL-----FSGEEVRKRIGD----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLrypgAMV 520
Cdd:TIGR01271 520 SVIkACQLeediaLFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL----CKL 595
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1844953743 521 IVSHDRFFIR------KLATKLLWLSAERSpiAFSGTYDE 554
Cdd:TIGR01271 596 MSNKTRILVTsklehlKKADKILLLHEGVC--YFYGTFSE 633
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-200 |
4.12e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIkAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsverRLPLDQwgwmgqqtEAD 80
Cdd:PRK10895 1 MATLT-AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAG----NIIIDD--------EDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAYVEEGC---PEHYAAKRRLKELEAQMqdAAAPCMESLLAD-YQEAAERYMglDGYHWEtqverkllqlglgrE 156
Cdd:PRK10895 68 SLLPLHARARRGIgylPQEASIFRRLSVYDNLM--AVLQIRDDLSAEqREDRANELM--EEFHIE--------------H 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 157 LWDQpLGQ-LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASL 200
Cdd:PRK10895 130 LRDS-MGQsLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-232 |
4.32e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTEADEAVFTHAYVEEGCPEH 96
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL----LD-----GVPLVQYDHHYLHRQVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 97 YAAKRRLKELEAQMQDAAApcMESLLADYQEA-AERYMGLDGYHWETQVERKLlqlglgrelwdqplGQLSGGQKTRAQL 175
Cdd:TIGR00958 565 VLFSGSVRENIAYGLTDTP--DEEIMAAAKAAnAHDFIMEFPNGYDTEVGEKG--------------SQLSGGQKQRIAI 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 176 ARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLV 232
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILV 685
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
354-525 |
4.69e-10 |
|
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: 59.89 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLL-----VGELQPAAGKVRqhpqtsigYFSQELEHL 428
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVL--------LDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 DDGVTLLDS----LLTLPAMTQT----------QARTILGCFLFSG--EEVRKRIG------------DLSMGERCRLAF 480
Cdd:cd03260 73 DVDVLELRRrvgmVFQKPNPFPGsiydnvayglRLHGIKLKEELDErvEEALRKAAlwdevkdrlhalGLSGGQQQRLCL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844953743 481 LKLYFSGANLLVLDEPTNYLDIDSRERIEQAL--LRYPGAMVIVSHD 525
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIaeLKKEYTIVIVTHN 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-228 |
5.41e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYA-GKPL----FEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqTEA 79
Cdd:PRK13641 3 IKFENVDYIYSpGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---------------TIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEavftHAYVEEGcpeHYAAKRRLKELEAQMQDAAAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLGRELWD 159
Cdd:PRK13641 68 GY----HITPETG---NKNLKKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLIS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVWL--RAYPGTVVFVSHDrhfMDRVA 228
Cdd:PRK13641 141 KSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKdyQKAGHTVILVTHN---MDDVA 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
144-266 |
5.47e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLGRELWDQ---PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVS 218
Cdd:PRK14246 130 VEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVS 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1844953743 219 HDRHFMDRVATCLVELtptgcrkYRGGYTEYTRQKELELRTQEQLYRK 266
Cdd:PRK14246 210 HNPQQVARVADYVAFL-------YNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-221 |
6.05e-10 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 60.97 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 35 IYGRNGIGKTTLLRLLAGTLELDKGSV--------ERRLPLDQWGWMGQqteaDEAVFTHAYVEEGCPehYAAKRRlKEL 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSImldgedvtNVPPHLRHINMVFQ----SYALFPHMTVEENVA--FGLKMR-KVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 107 EAQMqdaAAPCMESL-LADYQEAAERYmgldgyhwetqverkllqlglgrelwdqpLGQLSGGQKTRAQLARLMVREPQL 185
Cdd:TIGR01187 74 RAEI---KPRVLEALrLVQLEEFADRK-----------------------------PHQLSGGQQQRVALARALVFKPKI 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1844953743 186 LLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHDR 221
Cdd:TIGR01187 122 LLLDEPLSALDKKLRDQMQLELKTIQEqlgiTFVFVTHDQ 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
373-497 |
8.74e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 373 SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV----RQHPQTS--------IGYFSQeleHlddgvtlldslLT 440
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgKPVRIRSprdaialgIGMVHQ---H-----------FM 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 441 L-PAMTQTQ----ARTILGCFLFSGEEVRKRI-----------------GDLSMGERCRLAFLKLYFSGANLLVLDEPT 497
Cdd:COG3845 91 LvPNLTVAEnivlGLEPTKGGRLDRKAARARIrelserygldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
363-554 |
8.97e-10 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 58.98 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 363 YGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQ--TS----------IGYFSQElEHLDD 430
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdiTGlppheraragIGYVPEG-RRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GVTLLDSLLtlpamtqtqartiLGCFLFSGEEVRKRI------------------GDLSMGERCRLAFLKLYFSGANLLV 492
Cdd:cd03224 89 ELTVEENLL-------------LGAYARRRAKRKARLervyelfprlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 493 LDEPTNYLDIDSRERIEQALLRYPG---AMVIVSHDRFFIRKLATKLLWLsaERSPIAFSGTYDE 554
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVL--ERGRVVLEGTAAE 218
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
362-496 |
9.48e-10 |
|
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: 59.21 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------------QHPQTSIGYFSQElEHLD 429
Cdd:TIGR04406 10 SYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILidgqdithlpmhERARLGIGYLPQE-ASIF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 430 DGVTLLDSLL----TLPAMTQTQARTILGCFL--FSGEEVRK-RIGDLSMGERCRLAFLKLYFSGANLLVLDEP 496
Cdd:TIGR04406 89 RKLTVEENIMavleIRKDLDRAEREERLEALLeeFQISHLRDnKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
350-410 |
1.05e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.62 E-value: 1.05e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 350 SRSLVRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI 66
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-220 |
1.06e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGK-PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG-------TLELDKGSVERRLPLDQWGWMGQQ 76
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWIGGRVVNELEPADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 teaDEAVFTHAYVEEGCPehYAAK-RRLK--ELEAQMQDAAapcmeslladyqeaaerymgldgyhwetqverKLLQLGl 153
Cdd:PRK11650 84 ---NYALYPHMSVRENMA--YGLKiRGMPkaEIEERVAEAA--------------------------------RILELE- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 154 grELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAslewLEVWLRA--------YPGTVVFVSHD 220
Cdd:PRK11650 126 --PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK----LRVQMRLeiqrlhrrLKTTSLYVTHD 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-237 |
1.14e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.13 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQteadeavFTHAyveegcpehyaAKRR 102
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL---------FDGQD-------ITGL-----------SGRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LKEL--EAQM--QDAAA---PCM-------ESL----LADYQEAAERymgldgyhwetqVERKLLQLGLGRELWDQPLGQ 164
Cdd:COG4608 90 LRPLrrRMQMvfQDPYAslnPRMtvgdiiaEPLrihgLASKAERRER------------VAELLELVGLRPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVwLRAYPG-TVVFVSHD----RHFMDRVATC----L 231
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLED-LQDELGlTYLFISHDlsvvRHISDRVAVMylgkI 236
|
....*.
gi 1844953743 232 VELTPT 237
Cdd:COG4608 237 VEIAPR 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-199 |
1.15e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 59.09 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 18 PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDkGSVERRLPLDQW----GWMGQqteadEAVFTH 86
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLD-GVDIRDLNLRWLrsqiGLVSQ-----EPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 87 AYVEEGCpehyaakrRLKELEAQMQDAAAPCMESLLADYqeaaerYMGL-DGYhwETQV-ERKllqlglgrelwdqplGQ 164
Cdd:cd03249 91 GTIAENI--------RYGKPDATDEEVEEAAKKANIHDF------IMSLpDGY--DTLVgERG---------------SQ 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
372-525 |
1.26e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGeLQPAAGKVR-------QHPQTSI----GYFSQELE-------------H 427
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQfagqpleAWSAAELarhrAYLSQQQTppfampvfqyltlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 428 LDDGVTLLDSLLTLPAMTQtqartilgcFLFSGEEVRKRIGDLSMGE--RCRLA--FLKLYFSG---ANLLVLDEPTNYL 500
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAE---------ALGLDDKLGRSVNQLSGGEwqRVRLAavVLQVWPDInpaGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*...
gi 1844953743 501 DIDSR---ERIEQALLRYPGAMVIVSHD 525
Cdd:PRK03695 165 DVAQQaalDRLLSELCQQGIAVVMSSHD 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
362-525 |
1.47e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGER--ELFaelSL-SVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHP--QTSIGYFS----QE-LEHLDDG 431
Cdd:PRK13409 82 RYGVNgfKLY---GLpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEVLKRFRgtelQNyFKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 ----------VTLLDSLL---TLPAMTQTQARTILgcflfsgEEVRKR----------IGDLSMGERCRLAFLKLYFSGA 488
Cdd:PRK13409 159 eikvvhkpqyVDLIPKVFkgkVRELLKKVDERGKL-------DEVVERlglenildrdISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 489 NLLVLDEPTNYLDIdsRERIEQALL-------RYpgaMVIVSHD 525
Cdd:PRK13409 232 DFYFFDEPTSYLDI--RQRLNVARLirelaegKY---VLVVEHD 270
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
386-532 |
1.52e-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: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 386 GPNGSGKTTLLKLLV----GELqPAAGKVRQHP------QTSIGYFSQELEHLDDG-------VTLLDSLLTLPamtQTQ 448
Cdd:cd03240 29 GQNGAGKTTIIEALKyaltGEL-PPNSKGGAHDpklireGEVRAQVKLAFENANGKkytitrsLAILENVIFCH---QGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 449 ARTILgcflfsgEEVRKRigdLSMGERC------RLAFLKLYFSGANLLVLDEPTNYLDidsRERIEQALLR-------- 514
Cdd:cd03240 105 SNWPL-------LDMRGR---CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEiieerksq 171
|
170
....*....|....*...
gi 1844953743 515 YPGAMVIVSHDRFFIRKL 532
Cdd:cd03240 172 KNFQLIVITHDEELVDAA 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
350-536 |
1.73e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 350 SRSLVRLERAAFRYGERELFAEL----SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQT--------- 416
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTDVlhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 417 ------SIGYFSQELEHLDDGVTLLDSLLTL------PAMTQTQARTILGCFlfsGEEVRK--RIGDLSMGERCRLAFLK 482
Cdd:PRK11629 82 aelrnqKLGFIYQFHHLLPDFTALENVAMPLligkkkPAEINSRALEMLAAV---GLEHRAnhRPSELSGGERQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 483 LYFSGANLLVLDEPTNYLDIDSRERIEQAL----LRYPGAMVIVSHDRFFIRKLATKL 536
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLgelnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-199 |
2.25e-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: 60.12 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEY--AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsverRLPLDqwgwmgqqteadeavfth 86
Cdd:TIGR02203 335 NVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG----QILLD------------------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 87 ayveeGCP-EHYaakrRLKELEAQM----QDAAapcmesLLADYQEAAERYMGLDGYHwETQVERKL-----------LQ 150
Cdd:TIGR02203 393 -----GHDlADY----TLASLRRQValvsQDVV------LFNDTIANNIAYGRTEQAD-RAEIERALaaayaqdfvdkLP 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 151 LGLgrelwDQPLGQ----LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:TIGR02203 457 LGL-----DTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
350-526 |
2.35e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 350 SRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV---------------RQhp 414
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistlkpeiyRQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 415 QTSigYFSQELEHLDDgvTLLDSLLtLPAMTQTQA------RTILGCFLFSGEEVRKRIGDLSMGERCRLAFLK-LYFSg 487
Cdd:PRK10247 82 QVS--YCAQTPTLFGD--TVYDNLI-FPWQIRNQQpdpaifLDDLERFALPDTILTKNIAELSGGEKQRISLIRnLQFM- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1844953743 488 ANLLVLDEPTNYLDIDSRERIEQALLRYPG----AMVIVSHDR 526
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-228 |
2.52e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQ-----VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDQWGWMGQQTEA 79
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKkaldnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII----IDGVDITDKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 DEA------VFTHayveegcPEHyaakrRLKElEAQMQDAA-APcmeslladyqeaaeRYMGLDGYHWETQVERKLLQLG 152
Cdd:PRK13637 79 SDIrkkvglVFQY-------PEY-----QLFE-ETIEKDIAfGP--------------INLGLSEEEIENRVKRAMNIVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 153 LGRE-LWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDrhfMDRV 227
Cdd:PRK13637 132 LDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeiLNKIKELHKEYNMTIILVSHS---MEDV 208
|
.
gi 1844953743 228 A 228
Cdd:PRK13637 209 A 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-228 |
2.70e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDKGSVERRLPLDQwgwmgQQT 77
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGDITIDTARSLSQ-----QKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 EADEA------------VFTHAYVEEGCPEHYAAkrrlkeLEAQMQDAAAPCMESLLADyqeaaeryMGLDGYhwETQVE 145
Cdd:PRK11264 79 LIRQLrqhvgfvfqnfnLFPHRTVLENIIEGPVI------VKGEPKEEATARARELLAK--------VGLAGK--ETSYP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 146 RKLlqlglgrelwdqplgqlSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHDRH 222
Cdd:PRK11264 143 RRL-----------------SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIVTHEMS 205
|
....*.
gi 1844953743 223 FMDRVA 228
Cdd:PRK11264 206 FARDVA 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-196 |
2.70e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNvmKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLEL--------DKGSVERRL 65
Cdd:COG4161 1 MSIQLKNIN--CFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIaghqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 66 PLDQ-WGWMGQQTEadeaVFTHAYVEEGCPEhyAAKRRLKELEAQMQDAAAPCMESL-LADYqeaAERYmgldgyhwetq 143
Cdd:COG4161 79 LLRQkVGMVFQQYN----LWPHLTVMENLIE--APCKVLGLSKEQAREKAMKLLARLrLTDK---ADRF----------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 144 verkllqlglgrelwdqPLgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:COG4161 139 -----------------PL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
351-411 |
3.66e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 3.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 351 RSLVRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATYAlkDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT 65
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
362-525 |
4.21e-09 |
|
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: 59.41 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERElFAELSLSVDR-GDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTS--IGYFS----QE-LEHLDDG-- 431
Cdd:COG1245 82 RYGENG-FRLYGLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDevLKRFRgtelQDyFKKLANGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 --------VTLLDSLLTLPA---MTQTQARTILgcflfsgEEVRKR----------IGDLSMGERCRLA----FLKlyfs 486
Cdd:COG1245 161 kvahkpqyVDLIPKVFKGTVrelLEKVDERGKL-------DELAEKlglenildrdISELSGGELQRVAiaaaLLR---- 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 487 GANLLVLDEPTNYLDIdsRERIEQA-----LLRYPGAMVIVSHD 525
Cdd:COG1245 230 DADFYFFDEPSSYLDI--YQRLNVArlireLAEEGKYVLVVEHD 271
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-228 |
4.32e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.83 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEqVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqTEADEAVFTHAYVEEGC 93
Cdd:PRK13649 18 FEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---------------RVDDTLITSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 PEHYAAKRRLKELEAQMQDaaapcmESLLADYQEAAERYmGLDGYHWETQVERKLLQLGLGRELWDQPLGQLSGGQKTRA 173
Cdd:PRK13649 82 QIRKKVGLVFQFPESQLFE------ETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLD-AASLEWLEVWLRAYPG--TVVFVShdrHFMDRVA 228
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDpKGRKELMTLFKKLHQSgmTIVLVT---HLMDDVA 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-220 |
5.25e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWM-GQQTEAdeavFTHAYVeegcpe 95
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI----------LFdGENIPA----MSRSRL------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 hYAAKRRLKELeaqMQDAAAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLgRELWDQPLGQLSGGQKTRAQL 175
Cdd:PRK11831 80 -YTVRKRMSML---FQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1844953743 176 ARLMVREPQLLLLDEPTNHLDAASLEWLeVWL-----RAYPGTVVFVSHD 220
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVL-VKLiselnSALGVTCVVVSHD 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
362-526 |
5.64e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 58.23 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---------QHPQTS-IGYFSQE---LEHL 428
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnLPPRERrVGFVFQHyalFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 ddgvtlldslltlpamtqTQARTI---LGCFLFSGEEVRKRIGD-----------------LSMGERCRLAFLKLYFSGA 488
Cdd:COG1118 91 ------------------TVAENIafgLRVRPPSKAEIRARVEEllelvqlegladrypsqLSGGQRQRVALARALAVEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 489 NLLVLDEPTNYLDIDSRERIEQALLR----YPGAMVIVSHDR 526
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRlhdeLGGTTVFVTHDQ 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-196 |
7.14e-09 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 56.46 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYA-GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKG----------SVERRLPLDQWGWM 73
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 74 GQqteaDEAVFTHAYVEegcpehyaaKRRLKELEAQMQDAAAPCMESLLADYQEAAErymglDGYhwETQV-ERKllqlg 152
Cdd:cd03254 83 LQ----DTFLFSGTIME---------NIRLGRPNATDEEVIEAAKEAGAHDFIMKLP-----NGY--DTVLgENG----- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 153 lgrelwdqplGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:cd03254 138 ----------GNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-220 |
7.64e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV---------ERRLPLDQWGW-MGQQT--------------- 77
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpfkRRKEFARRIGVvFGQRSqlwwdlpaidsfrll 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 ----EADEAVFthayveegcpehyaaKRRLKELeaqmqdaaapcmeslladyqeaaerymgldgyhwetqveRKLLQLGl 153
Cdd:COG4586 121 kaiyRIPDAEY---------------KKRLDEL---------------------------------------VELLDLG- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 154 grELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAY----PGTVVFVSHD 220
Cdd:COG4586 146 --ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrerGTTILLTSHD 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
354-411 |
8.26e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.78 E-value: 8.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL 61
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
9.04e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.17 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYA-GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqqteadea 82
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 vfthayveEGCPEHYAAKRRLKELEAQMQDAAAPCMESLLAD-YQEAAERYMGLDGYHWETQ--VERKLLQLGLGrELWD 159
Cdd:PRK13636 66 --------DGKPIDYSRKGLMKLRESVGMVFQDPDNQLFSASvYQDVSFGAVNLKLPEDEVRkrVDNALKRTGIE-HLKD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASL-EWLEVWLRAYPG---TVVFVSHD 220
Cdd:PRK13636 137 KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVsEIMKLLVEMQKElglTIIIATHD 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-227 |
1.04e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQ-TEADEAvfthayveegcpehyaaKR 101
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA---------WLGKDlLGMKDD-----------------EW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 102 RLKELEAQM--QDAAA---PCM-------ESLLADYQEaaerymgLDGYHWETQVERKLLQLGLGRELWDQPLGQLSGGQ 169
Cdd:PRK15079 94 RAVRSDIQMifQDPLAslnPRMtigeiiaEPLRTYHPK-------LSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 170 KTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVWLRAYPGTVVFVSHD----RHFMDRV 227
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHDlavvKHISDRV 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-233 |
1.06e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 18 PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerRL---PLDQWgwmgqqteaDEAVFTHA--YVEEg 92
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI--LLngqPIADY---------SEAALRQAisVVSQ- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpehyaakrRLKELEAQMQDaaapcmESLLADYQEAAERYMGLdgyhwETQVE-RKLLQLGLGRELWdqpLG----QLSG 167
Cdd:PRK11160 422 ---------RVHLFSATLRD------NLLLAAPNASDEALIEV-----LQQVGlEKLLEDDKGLNAW---LGeggrQLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVWLRAYPG-TVVFVSHDRHF---MDRVatCLVE 233
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGleqFDRI--CVMD 547
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
365-523 |
1.11e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 365 ERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAA---------GKVRQHPQTSIGYFSQE---LEHLDDGV 432
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftgtilannRKPTKQILKRTGFVTQDdilYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 TLL-DSLLTLPAMTQTQARTILGCFLFSGEEVRK----RIGD-----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDI 502
Cdd:PLN03211 160 TLVfCSLLRLPKSLTKQEKILVAESVISELGLTKcentIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180
....*....|....*....|...
gi 1844953743 503 DSRERIEQAL--LRYPGAMVIVS 523
Cdd:PLN03211 240 TAAYRLVLTLgsLAQKGKTIVTS 262
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
349-502 |
1.23e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQT-----------S 417
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 418 IGYFSQELEHLdDGVTLLDslltLPAMTQTQARTILGCFlfsGEEVRKRIGD-----------------LSMGERCRLAF 480
Cdd:PRK10575 87 VAYLPQQLPAA-EGMTVRE----LVAIGRYPWHGALGRF---GAADREKVEEaislvglkplahrlvdsLSGGERQRAWI 158
|
170 180
....*....|....*....|..
gi 1844953743 481 LKLYFSGANLLVLDEPTNYLDI 502
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDI 180
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
372-512 |
1.31e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.93 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELqPAAGKV---------------RQHpqtsIGYFSQE--LEH--LDDGV 432
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielreldpeswRKH----LSWVGQNpqLPHgtLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 433 TLLDSLLTLPAMTQTQARTILGCFLFSGE-----EVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRER 507
Cdd:PRK11174 444 LLGNPDASDEQLQQALENAWVSEFLPLLPqgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
....*
gi 1844953743 508 IEQAL 512
Cdd:PRK11174 524 VMQAL 528
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-220 |
1.35e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.56 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEY--AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwMGQQTEADE 81
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT----------VGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVfthayveegcpehYAAKRRL---------KELEAQMQDAAAPCMESLLADYQEAAERymgldgyhwetqVERKLLQLG 152
Cdd:PRK13635 75 TV-------------WDVRRQVgmvfqnpdnQFVGATVQDDVAFGLENIGVPREEMVER------------VDQALRQVG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 153 LGRELWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEV--WLRAYPG-TVVFVSHD 220
Cdd:PRK13635 130 MEDFLNREP-HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDpRGRREVLETvrQLKEQKGiTVLSITHD 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
313-524 |
1.39e-08 |
|
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: 57.84 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 313 SRMNAKMKELERLEGNRVEKPREAAhlkvKLSASDFASRSLVRLERAAFRYGER---------------ELFAELSLSVD 377
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEE----IESGREGGRNSNLVPGRGIVEYQDNgikfeniplvtpngdVLIESLSFEVP 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 378 RGDRLAVLGPNGSGKTTLLKLLvGELQPAAGKVRQHP-QTSIGYFSQE----LEHLDDGVTLLDSLL----------TLP 442
Cdd:TIGR00954 477 SGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPaKGKLFYVPQRpymtLGTLRDQIIYPDSSEdmkrrglsdkDLE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 443 AMTQ-TQARTIL---GCFlfsgEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGA 518
Cdd:TIGR00954 556 QILDnVQLTHILereGGW----SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGIT 631
|
....*.
gi 1844953743 519 MVIVSH 524
Cdd:TIGR00954 632 LFSVSH 637
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-196 |
1.46e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 56.24 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlpldqwgwmgqqteadeavfthayveeGCPEHYAAKRR 102
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK---------------------------GEPIKYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LKELEA-----QMQDAA--APCMESLLAdyqeAAERYMGLDGYHWETQVERKLLQLGL-GRElwDQPLGQLSGGQKTRAQ 174
Cdd:PRK13639 74 LEVRKTvgivfQNPDDQlfAPTVEEDVA----FGPLNLGLSKEEVEKRVKEALKAVGMeGFE--NKPPHHLSGGQKKRVA 147
|
170 180
....*....|....*....|..
gi 1844953743 175 LARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLD 169
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
363-535 |
1.46e-08 |
|
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: 55.80 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 363 YGERELFaELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQH--------PQT-SIGYFSQE---LEHLDD 430
Cdd:cd03299 10 WKEFKLK-NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKrDISYVPQNyalFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GVTLLDSLLTLPAMTQTQARTILGC--FLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERI 508
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 509 EQAL---LRYPGAMVI-VSHDRFFIRKLATK 535
Cdd:cd03299 169 REELkkiRKEFGVTVLhVTHDFEEAWALADK 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-227 |
1.47e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.15 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYA-GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-ERRLPLDQWGWMGQQTEADE 81
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVFTHayveegcPEHYAAKRRLKEleaqmQDAAAPcmESLLADYQEAAERymgldgyhwetqVERKLLQLGLGRELWDQP 161
Cdd:PRK13644 81 IVFQN-------PETQFVGRTVEE-----DLAFGP--ENLCLPPIEIRKR------------VDRALAEIGLEKYRHRSP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 162 lGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVwLRAYPGTVVFVSH---DRHFMDRV 227
Cdd:PRK13644 135 -KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgiavLERIKK-LHEKGKTIVYITHnleELHDADRI 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
362-539 |
1.69e-08 |
|
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: 55.23 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAG-----------------KVRQHpqtsIGYFSQE 424
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglkltddkkninELRQK----VGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 425 ---LEHLD--DGVTLldSLLTLPAMTQTQARTIlgcflfsGEEVRKRIG----------DLSMGERCRLAFLKLYFSGAN 489
Cdd:cd03262 85 fnlFPHLTvlENITL--APIKVKGMSKAEAEER-------ALELLEKVGladkadaypaQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 490 LLVLDEPTNYLD---IDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWL 539
Cdd:cd03262 156 VMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-196 |
1.94e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNvmKEY-AGKPLFEqVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLEL---------DKGSVER 63
Cdd:PRK11124 1 MSIQLNGIN--CFYgAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIagnhfdfskTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 64 RLPLDQWGWMGQQTEadeaVFTHAYVEEGCPEhyaakrrlkeleaqmqdaaAPCMESLLADyQEAAERYMGLdgyhwetq 143
Cdd:PRK11124 78 RELRRNVGMVFQQYN----LWPHLTVQQNLIE-------------------APCRVLGLSK-DQALARAEKL-------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 144 VERklLQLGLGRELWdqPLgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK11124 126 LER--LRLKPYADRF--PL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
362-539 |
2.18e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLV------------------------GELQPAAGKVRQHPQTS 417
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpsegsivvngqtinlvrdkdGQLKVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 418 IGYFSQELeHLDDGVTLLDSLLTLP----AMTQTQARTILGCFL----FSGEEVRKRIGDLSMGERCRLAFLKLYFSGAN 489
Cdd:PRK10619 94 LTMVFQHF-NLWSHMTVLENVMEAPiqvlGLSKQEARERAVKYLakvgIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 490 LLVLDEPTNYLD---IDSRERIEQALLRYPGAMVIVSHDRFFIRKLATKLLWL 539
Cdd:PRK10619 173 VLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
362-537 |
2.48e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQ--------------------TSIGYF 421
Cdd:PRK11701 15 LYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalseaerrrllrTEWGFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQeleHLDDGVTLLDS--------LLTLPAMTQTQARTILGCFLFSGEEVRKRIGDL----SMGERCRLAFLKLYFSGAN 489
Cdd:PRK11701 95 HQ---HPRDGLRMQVSaggnigerLMAVGARHYGDIRATAGDWLERVEIDAARIDDLpttfSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 490 LLVLDEPTNYLDIDSRERI---EQALLRYPG-AMVIVSHDRFFIRKLATKLL 537
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLldlLRGLVRELGlAVVIVTHDLAVARLLAHRLL 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
353-501 |
2.56e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYgeRELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR----QHPQTS-----IGYFSQ 423
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqDHTTTPpsrrpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 424 E---LEHLDDGVTL---LDSLLTLPAMTQTQARTILGcfLFSGEEVRKRI-GDLSMGERCRLAFLKLYFSGANLLVLDEP 496
Cdd:PRK10771 79 EnnlFSHLTVAQNIglgLNPGLKLNAAQREKLHAIAR--QMGIEDLLARLpGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
....*
gi 1844953743 497 TNYLD 501
Cdd:PRK10771 157 FSALD 161
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
353-554 |
2.67e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEHlDDG 431
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR-NIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLLDSLLTlpamtqtqARTI-----LGCFLFSGEEVRK--------------------RIGD----LSMGERCRLAFLK 482
Cdd:PRK13657 413 VVFQDAGLF--------NRSIednirVGRPDATDEEMRAaaeraqahdfierkpdgydtVVGErgrqLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 483 LYFSGANLLVLDEPTNYLDIDSRERIEQAL--LRYPGAMVIVSHDRFFIRKlATKLLWLSAERspIAFSGTYDE 554
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALdeLMKGRTTFIIAHRLSTVRN-ADRILVFDNGR--VVESGSFDE 555
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-220 |
2.91e-08 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 55.34 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 22 QVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqqteadeavfthayveEGCPEHYAAKR 101
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI---------------------------DGQDIAAMSRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 102 RLKELEAQ---M--QD-AAAPCMESLladyqEAAERYMGLDGYHWETQVERKLLQLGL-GRELW-DQPLGQLSGGQKTRA 173
Cdd:cd03294 95 ELRELRRKkisMvfQSfALLPHRTVL-----ENVAFGLEVQGVPRAEREERAAEALELvGLEGWeHKYPDELSGGMQQRV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLDA-ASLEWLEVWLR---AYPGTVVFVSHD 220
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPlIRREMQDELLRlqaELQKTIVFITHD 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-197 |
3.44e-08 |
|
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: 54.01 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 12 KEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRLPL---DQWGWMGQQTEADEAVFTHAY 88
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayvSQEPWIQNGTIRENILFGKPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 VEEgcpehyaakrRLKE-LEAqmqdaaapCmeSLLADYQEaaerYMGLDgyhwETQV-ERkllqlGLGrelwdqplgqLS 166
Cdd:cd03250 93 DEE----------RYEKvIKA--------C--ALEPDLEI----LPDGD----LTEIgEK-----GIN----------LS 129
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 167 GGQKTRAQLARLMVREPQLLLLDEPTNHLDA 197
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
362-411 |
3.57e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 54.60 E-value: 3.57e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 362 RYGERE-LFaELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:COG0410 12 GYGGIHvLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR 61
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
362-496 |
3.65e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.65 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--QHPQTS----------IGYFSQE---LE 426
Cdd:COG1137 12 SYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldGEDITHlpmhkrarlgIGYLPQEasiFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 427 HLddgvTLLDSLL----TLPaMTQTQARTILGCFL--FSGEEVRKRIGD-LSMGERCR------LAflklyfSGANLLVL 493
Cdd:COG1137 92 KL----TVEDNILavleLRK-LSKKEREERLEELLeeFGITHLRKSKAYsLSGGERRRveiaraLA------TNPKFILL 160
|
...
gi 1844953743 494 DEP 496
Cdd:COG1137 161 DEP 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
353-532 |
3.65e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV----RQHP--------QTSIGY 420
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinnINYNkldhklaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 421 FSQELEHLDDgVTLLDSLLT--LPamtqtqARTILGCFLFSGEEVRKR-----------------IGDLSMGERCRLAFL 481
Cdd:PRK09700 85 IYQELSVIDE-LTVLENLYIgrHL------TKKVCGVNIIDWREMRVRaammllrvglkvdldekVANLSISHKQMLEIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 482 KLYFSGANLLVLDEPTNYL---DIDSRERIEQALLRYPGAMVIVSHDRFFIRKL 532
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRI 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
372-501 |
3.72e-08 |
|
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: 56.88 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVrqHPQTSIGYFSQELEHLDDgvTLLDSLLTLPAMTQTQART 451
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--HMKGSVAYVPQQAWIQND--SLRENILFGKALNEKYYQQ 732
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 452 IL-GCFLFSGEEV-----RKRIGD----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:TIGR00957 733 VLeACALLPDLEIlpsgdRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-359 |
3.85e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV--ERRLP-LDQWGWMGQQTEADEAVFthaYVEEGc 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaERSIAyVPQQAWIMNATVRGNILF---FDEED- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 pehyaakrrlkelEAQMQDAAAPCmeslladyqeaaerymgldgyhwetQVERKLLQLGLGRELWDQPLG-QLSGGQKTR 172
Cdd:PTZ00243 749 -------------AARLADAVRVS-------------------------QLEADLAQLGGGLETEIGEKGvNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 173 AQLARLMVREPQLLLLDEPTNHLDAASLEWL--EVWLRAYPG-TVVFVSHDRHFMDRvATCLVELTpTGCRKYRGGYTEY 249
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVveECFLGALAGkTRVLATHQVHVVPR-ADYVVALG-DGRVEFSGSSADF 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 250 trqkelelrtqeqlyrkqqlLREQLEESIRtyrqwfhqgeknAQMAEVPIQRGyfqGRAGAHVSRMNAKMKELERLEGNr 329
Cdd:PTZ00243 869 --------------------MRTSLYATLA------------AELKENKDSKE---GDADAEVAEVDAAPGGAVDHEPP- 912
|
330 340 350
....*....|....*....|....*....|
gi 1844953743 330 VEKPREAAHLKVKLSASDFASRSLVRLERA 359
Cdd:PTZ00243 913 VAKQEGNAEGGDGAALDAAAGRLMTREEKA 942
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-192 |
3.85e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.50 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE-RRLPLDQWgwmgqQTE- 78
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfDGKDITDW-----QTAk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 -ADEAVfthAYVEEGcpehyaakRRLKeleAQMQDAAAPCMESLLAD---YQEAAERYMGLDGYHWETQVERKllqlglg 154
Cdd:PRK11614 77 iMREAV---AIVPEG--------RRVF---SRMTVEENLAMGGFFAErdqFQERIKWVYELFPRLHERRIQRA------- 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 1844953743 155 relwdqplGQLSGGQKTRAQLARLMVREPQLLLLDEPT 192
Cdd:PRK11614 136 --------GTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
372-525 |
4.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.08 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTsIGYFSQELEHLDDGVTLL----DSLLTLPAMTQT 447
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-IKYDKKSLLEVRKTVGIVfqnpDDQLFAPTVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 448 QARTILGCFLfSGEEVRKRIGD-----------------LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQ 510
Cdd:PRK13639 100 VAFGPLNLGL-SKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK 178
|
170
....*....|....*...
gi 1844953743 511 AL--LRYPGAMVIVS-HD 525
Cdd:PRK13639 179 LLydLNKEGITIIIStHD 196
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
354-536 |
5.75e-08 |
|
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: 52.96 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSlSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVrQHPQTSIGYFSQELehlddgvt 433
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-EWDGITPVYKPQYI-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 434 lldslltlpamtqtqartilgcflfsgeevrkrigDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALL 513
Cdd:cd03222 71 -----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180
....*....|....*....|....*..
gi 1844953743 514 RY----PGAMVIVSHDRFFIRKLATKL 536
Cdd:cd03222 116 RLseegKKTALVVEHDLAVLDYLSDRI 142
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
362-523 |
5.77e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 54.73 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR-------QHPQTSIGYFSQElehldDG--- 431
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYLPEE-----RGlyp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 -VTLLDSLL---TLPAMTQTQARTILGcFLFS----GEEVRKRIGDLSMGERCRLAFLklyfsGA-----NLLVLDEPTN 498
Cdd:COG4152 85 kMKVGEQLVylaRLKGLSKAEAKRRAD-EWLErlglGDRANKKVEELSKGNQQKVQLI-----AAllhdpELLILDEPFS 158
|
170 180
....*....|....*....|....*..
gi 1844953743 499 YLDIDSRERIEQAL--LRYPGAMVIVS 523
Cdd:COG4152 159 GLDPVNVELLKDVIreLAAKGTTVIFS 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
354-411 |
6.80e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 53.41 E-value: 6.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY 58
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-199 |
8.48e-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: 54.09 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER--RLPL-DQWGWMGQQTEADEAVFTHAYVEeg 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHsgRISFsSQFSWIMPGTIKENIIFGVSYDE-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpehYAAKRRLKELEaqmqdaaapcMESLLADYQEAAERYMGLDGYhwetqverkllqlglgrelwdqplgQLSGGQKTR 172
Cdd:cd03291 127 ----YRYKSVVKACQ----------LEEDITKFPEKDNTVLGEGGI-------------------------TLSGGQRAR 167
|
170 180
....*....|....*....|....*..
gi 1844953743 173 AQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-199 |
9.06e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKgSVERRLPLdqWGWMGQQTEAD 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-SAGSHIEL--LGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAYVEEGCP-EHYAAKRRLKELEAQMQDA--AAPCMESLLAdyqeaaerymgldgyhWETQVERKLLQLGLGR-- 155
Cdd:PRK09984 78 ARDIRKSRANTGYIfQQFNLVNRLSVLENVLIGAlgSTPFWRTCFS----------------WFTREQKQRALQALTRvg 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844953743 156 --ELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:PRK09984 142 mvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
357-523 |
1.06e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 357 ERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV------------RQHPQTSIGYFSQE 424
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 425 ------LEHLDDGVTLLDSLLTLPAmTQTQARTILGCFLFSGEEVRKRIGD-LSMGERCRLAFLKLYFSGANLLVLDEPT 497
Cdd:PRK10895 87 asifrrLSVYDNLMAVLQIRDDLSA-EQREDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190
....*....|....*....|....*....|
gi 1844953743 498 NYLD----IDSRERIEQalLRYPGAMVIVS 523
Cdd:PRK10895 166 AGVDpisvIDIKRIIEH--LRDSGLGVLIT 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
371-526 |
1.07e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKvrqhpqtsIGYFSQELEHLDDGV----TLLDSLLTLPAMTQ 446
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQ--------IMLDGVDLSHVPPYQrpinMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 447 TQARTI-LGCFLFSGEEVRKRIGD-----------------LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERI 508
Cdd:PRK11607 109 EQNIAFgLKQDKLPKAEIASRVNEmlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180
....*....|....*....|..
gi 1844953743 509 E----QALLRYPGAMVIVSHDR 526
Cdd:PRK11607 189 QlevvDILERVGVTCVMVTHDQ 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-238 |
1.10e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.79 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqteadeaVFTHAYVEEGCP 94
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------------------LFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 95 EHYaakRRLKELEAQmqdaaAPCM------ESLLADYQEaaeRYMGLDgyhwETQVERKLLQLGLGRELWDQPLGQLSGG 168
Cdd:PRK10247 77 EIY---RQQVSYCAQ-----TPTLfgdtvyDNLIFPWQI---RNQQPD----PAIFLDDLERFALPDTILTKNIAELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 169 QKTRAQLARLMVREPQLLLLDEPTNHLDAASL----EWLEVWLRAYPGTVVFVSHDRhfmDRVATC--LVELTPTG 238
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDK---DEINHAdkVITLQPHA 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
354-410 |
1.31e-07 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 53.01 E-value: 1.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI 57
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-219 |
1.32e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 54.75 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE-RRLPLDQWgwmgqqteadeavfthayveegcp 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlNGFSLKDI------------------------ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 95 EHYAAKRRLKELEAQMQDAAAPCMESLLADYQEAAERYMGLDGYHW-ETQVERKLLQLGLGRELWDQPlGQLSGGQKTRA 173
Cdd:TIGR01193 542 DRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIaEIKDDIENMPLGYQTELSEEG-SSISGGQKQRI 620
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844953743 174 QLARLMVREPQLLLLDEPTNHLDA-ASLEWLEVWLRAYPGTVVFVSH 219
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTiTEKKIVNNLLNLQDKTIIFVAH 667
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-220 |
1.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwmgqqteadeaVFTHAYVEEGCpehyaakrr 102
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVK--------------------VMGREVNAENE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 lKELEAQM----QDAAAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLgRELWDQPLGQLSGGQKTRAQLARL 178
Cdd:PRK13647 75 -KWVRSKVglvfQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844953743 179 MVREPQLLLLDEPTNHLDAAS----LEWLEVwLRAYPGTVVFVSHD 220
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGqetlMEILDR-LHNQGKTVIVATHD 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
354-543 |
1.58e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRY--GERELfAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQ-----HPQT------SIGY 420
Cdd:PRK13647 5 IEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmgrevNAENekwvrsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 421 FSQElehLDDGV---TLLDSLLTLPAMtqtqartiLGcflFSGEEVRKRIGD-----------------LSMGERCRLAF 480
Cdd:PRK13647 84 VFQD---PDDQVfssTVWDDVAFGPVN--------MG---LDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 481 LKLYFSGANLLVLDEPTNYLDIDSRERIEQAL--LRYPGAMVIVS-HDRFFIRKLATKLLWLSAER 543
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdrLHNQGKTVIVAtHDVDLAAEWADQVIVLKEGR 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
312-411 |
1.62e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.03 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 312 VSRMNAKMKELERLEGNRVEKPREAAHLKVKLSASDFASrslVRLERAAFRY---GERELFA--ELSLSVDRGDRLAVLG 386
Cdd:COG4615 289 LSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQT---LELRGVTYRYpgeDGDEGFTlgPIDLTIRRGELVFIVG 365
|
90 100
....*....|....*....|....*
gi 1844953743 387 PNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEIL 390
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-228 |
1.67e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELD-----KGSVErrlpldqwgWMGQQTea 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVE---------FFNQNI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 80 deavfthayveegcpehYAAKRRLKELEAQMQDAAAPCMESLLADYQEAAeryMGLDGYHWETQVE-RKLLQLGL-GREL 157
Cdd:PRK14258 77 -----------------YERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVA---YGVKIVGWRPKLEiDDIVESALkDADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 158 WDQPLGQ-------LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLE-----VWLRAyPGTVVFVSHDRHFMD 225
Cdd:PRK14258 137 WDEIKHKihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVEsliqsLRLRS-ELTMVIVSHNLHQVS 215
|
...
gi 1844953743 226 RVA 228
Cdd:PRK14258 216 RLS 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-227 |
1.73e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERRlpldqwgwmgqQTEAD 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-----------NINYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EavFTHAYVEE-GCPEHYAAKRRLKELEAQmqdaaapcmESLLADyQEAAERYMGLDGYHWETQVERK---LLQLGLGRE 156
Cdd:PRK09700 71 K--LDHKLAAQlGIGIIYQELSVIDELTVL---------ENLYIG-RHLTKKVCGVNIIDWREMRVRAammLLRVGLKVD 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 157 LwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEV---WLRAYPGTVVFVSHD----RHFMDRV 227
Cdd:PRK09700 139 L-DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLimnQLRKEGTAIVYISHKlaeiRRICDRY 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-200 |
1.73e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 52.76 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG--TLELDKGSVErrlpLDqwgwmGQQ-TEADeavfthayVEEg 92
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIL----LD-----GEDiLELS--------PDE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpehyaakRRLKELEAQMQDaaaPC------MESLLadyQEA--AERYMGLDGYHWETQVERKLLQLGLGRELWDQPLGQ 164
Cdd:COG0396 74 --------RARAGIFLAFQY---PVeipgvsVSNFL---RTAlnARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNE 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 1844953743 165 -LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASL 200
Cdd:COG0396 140 gFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDAL 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-228 |
1.76e-07 |
|
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: 53.52 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLE---LDKGSVErrlpldqwgWMGQQ-TEADEAvfthayveegcpehya 98
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEIL---------FDGEDlLKLSEK---------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 99 AKRRLKELEAQM--QDAAA---PCM--ESLLAdyqEAAERYMGLDGYHWETQVERKLLQLGL---GRELWDQPlGQLSGG 168
Cdd:COG0444 79 ELRKIRGREIQMifQDPMTslnPVMtvGDQIA---EPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYP-HELSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 169 QKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVwLRAYPG-TVVFVSHD----RHFMDRVA 228
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKD-LQRELGlAILFITHDlgvvAEIADRVA 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-198 |
1.94e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLeldKGSVERRlpldqwgwmGQQTEADEAVfthayveEGCPEHYAAKRR 102
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPR---------GARVTGDVTL-------NGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LKELEAQMQDAAAPCME------SLLADYQEAaeRYMGLDGYHwETQVERKLLQLGLGRELWDQPLGQLSGGQKTRAQLA 176
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAfsareiVLLGRYPHA--RRAGALTHR-DGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 177 RLM---------VREPQLLLLDEPTNHLDAA 198
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLA 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
378-529 |
2.08e-07 |
|
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: 50.83 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 378 RGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVrqhpqtsigyfsqelehlddgvtLLDSLLTLPAMTQTQARTILGCFL 457
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------IYIDGEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 458 FSGEEVRKRIgdlsmgercRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSHDRFFI 529
Cdd:smart00382 58 KASGSGELRL---------RLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-266 |
2.14e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLEL-DKGSVERRLPLDqwgwmGQQteadeaV 83
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELyPEARVSGEVYLD-----GQD------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 FTHAYVEegcpehyaaKRRLKELEAQMQD-----------AAAPCMESLLADYQEAAERY-MGLDGYHWETQVERKLlql 151
Cdd:PRK14247 73 FKMDVIE---------LRRRVQMVFQIPNpipnlsifenvALGLKLNRLVKSKKELQERVrWALEKAQLWDEVKDRL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 152 glgrelwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD---AASLEWLEVWLRAyPGTVVFVSHDRHFMDRVA 228
Cdd:PRK14247 141 -------DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpenTAKIESLFLELKK-DMTIVLVTHFPQQAARIS 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 1844953743 229 TCLVELtptgcrkYRGGYTEYTRQKELELRTQEQLYRK 266
Cdd:PRK14247 213 DYVAFL-------YKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-233 |
2.23e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 52.43 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 25 LEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgWMGQQ--TEADEA---------------VFTHA 87
Cdd:COG4674 31 LYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV----------LFGGTdlTGLDEHeiarlgigrkfqkptVFEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 88 YVEEGCPEHYAAKRRLkeleaqmqdaaapcMESLLAdyqeaaerymGLDGYHWEtQVERKLLQLGLGRELwDQPLGQLSG 167
Cdd:COG4674 101 TVFENLELALKGDRGV--------------FASLFA----------RLTAEERD-RIEEVLETIGLTDKA-DRLAGLLSH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 168 GQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG--TVVFVSHDRHFMDRVA---TCLVE 233
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHDMEFVRQIArkvTVLHQ 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
372-525 |
2.33e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.15 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGeLQPAAGKV-------RQHPQTSI----GYFSQELEHLddGVTLLDSLLT 440
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIllngrplSDWSAAELarhrAYLSQQQSPP--FAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 441 L----PAMTQTQARTI--------LGCFLfsgeevRKRIGDLSMGE--RCRLA--FLKLYfSGAN----LLVLDEPTNYL 500
Cdd:COG4138 92 LhqpaGASSEAVEQLLaqlaealgLEDKL------SRPLTQLSGGEwqRVRLAavLLQVW-PTINpegqLLLLDEPMNSL 164
|
170 180 190
....*....|....*....|....*....|...
gi 1844953743 501 DIdsrerIEQA----LLRY----PGAMVIVSHD 525
Cdd:COG4138 165 DV-----AQQAaldrLLRElcqqGITVVMSSHD 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-199 |
3.00e-07 |
|
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: 51.72 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV---ERRLPLDQWGWMGQQTeadeavfthAYVEEg 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdGHDLALADPAWLRRQV---------GVVLQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpEHYAAKRRLKELEAqMQDAAAPcMESLLadyqEAAErymgLDGYHwetqveRKLLQLGLGrelWDQPLGQ----LSGG 168
Cdd:cd03252 84 --ENVLFNRSIRDNIA-LADPGMS-MERVI----EAAK----LAGAH------DFISELPEG---YDTIVGEqgagLSGG 142
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 169 QKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALDYES 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
353-516 |
3.01e-07 |
|
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: 51.70 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGER---ELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV--RQHP---------QTSI 418
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVllDGKPisqyehkylHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 419 GYFSQE----LEHLDDGVTLldSLLTLPAMTQTQARTILGCFLFSGE-------EVRKRIGDLSMGERCRLAFLKLYFSG 487
Cdd:cd03248 91 SLVGQEpvlfARSLQDNIAY--GLQSCSFECVKEAAQKAHAHSFISElasgydtEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180
....*....|....*....|....*....
gi 1844953743 488 ANLLVLDEPTNYLDIDSRERIEQALLRYP 516
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWP 197
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-228 |
3.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.43 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEY---AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV----ERRLPLDQWG-- 71
Cdd:PRK13650 1 MSNIIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgDLLTEENVWDir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 72 -WMGQQTEADEAVFTHAYVEegcpehyaakrrlkeleaqmqDAAAPCMESLLADYQEAAERymgldgyhwetqVERKLLQ 150
Cdd:PRK13650 81 hKIGMVFQNPDNQFVGATVE---------------------DDVAFGLENKGIPHEEMKER------------VNEALEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 151 LGLgRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRA----YPGTVVFVSHDrhfMDR 226
Cdd:PRK13650 128 VGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD---LDE 203
|
..
gi 1844953743 227 VA 228
Cdd:PRK13650 204 VA 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
373-524 |
3.16e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 373 SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--------QHPQTS----IGYFSQEL---EHLDdgVT---L 434
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfRSPRDAqaagIAIIHQELnlvPNLS--VAeniF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 435 LDSLLTLP------AMTQtQARTIL---GCflfsGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSR 505
Cdd:COG1129 102 LGREPRRGglidwrAMRR-RARELLarlGL----DIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREV 176
|
170 180
....*....|....*....|....
gi 1844953743 506 ER----IEQalLRYPG-AMVIVSH 524
Cdd:COG1129 177 ERlfriIRR--LKAQGvAIIYISH 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
351-514 |
3.19e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 351 RSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLK----LLVGELQPA----------------AGKV 410
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGshiellgrtvqregrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 411 RQhPQTSIGYFSQELeHLDDGVTLLDSLLT----------------LPAMTQT--QARTILGCFLFSgeevRKRIGDLSM 472
Cdd:PRK09984 82 RK-SRANTGYIFQQF-NLVNRLSVLENVLIgalgstpfwrtcfswfTREQKQRalQALTRVGMVHFA----HQRVSTLSG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 473 GERCRLAFLKLYFSGANLLVLDEPTNYLDIDSrERIEQALLR 514
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPES-ARIVMDTLR 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-228 |
3.20e-07 |
|
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: 53.15 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTL----LRLLA--GTLELDkgsverrlpldqwgwmgqqteadeavfthayveeGCPEH 96
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLglalLRLIPseGEIRFD----------------------------------GQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 97 YAAKRRLKELEAQM----QDAAA---PCM-------ESLLADYQE--AAERymgldgyhwETQVERKLLQLGLGRELWDQ 160
Cdd:COG4172 351 GLSRRALRPLRRRMqvvfQDPFGslsPRMtvgqiiaEGLRVHGPGlsAAER---------RARVAEALEEVGLDPAARHR 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 161 PLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVWLRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLFISHDlavvRALAHRVM 497
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-287 |
3.24e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgwmgqqteADEAVFTHayveegcpehyaaKRR 102
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT----------------VDDITITH-------------KTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LKELEAQMQDAAA----PcmESLLadYQEAAERYM-------GLDGYHWETQVERKLLQLGLGRELWDQPLGQLSGGQKT 171
Cdd:PRK13646 77 DKYIRPVRKRIGMvfqfP--ESQL--FEDTVEREIifgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 172 RAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYP----GTVVFVSHDrhfMDRVA------------TCLVELT 235
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD---MNEVAryadevivmkegSIVSQTS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 236 PtgcrKYRGGYTEYTRQKELEL----RTQEQLYRKQQLLREQL----EESIRTYRQWFHQ 287
Cdd:PRK13646 230 P----KELFKDKKKLADWHIGLpeivQLQYDFEQKYQTKLKDIalteEEFVSLYKEWQHE 285
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-568 |
3.28e-07 |
|
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: 53.27 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVG--ELQPAAGKVRQH-----------PQTSIGY 420
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyveRPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 421 -----------FSQELEHLDDGV----------------------TLLDSLLTLPAMTQTQARTILGCFLFSGEEVR--K 465
Cdd:TIGR03269 81 pcpvcggtlepEEVDFWNLSDKLrrrirkriaimlqrtfalygddTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQlsH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 466 RIG----DLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLR----YPGAMVIVSHDRFFIRKLATKLL 537
Cdd:TIGR03269 161 RIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|.
gi 1844953743 538 WLsaERSPIAFSGTYDEYAEASLASESSPEQ 568
Cdd:TIGR03269 241 WL--ENGEIKEEGTPDEVVAVFMEGVSEVEK 269
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
354-539 |
3.38e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLL-------VGEL-----------QPAAGKVRQHPQ 415
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLniagnhfdfskTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 416 TSIGYFSQelEHLDDGVTLLDSLLTLP--------AMTQTQARTILGcflfsgeevRKRIGD--------LSMGERCRLA 479
Cdd:PRK11124 83 NVGMVFQQ--YNLWPHLTVQQNLIEAPcrvlglskDQALARAEKLLE---------RLRLKPyadrfplhLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 480 FLKLYFSGANLLVLDEPTNYLDIDSRERIEQAL--LRYPG-AMVIVSHDRFFIRKLATKLLWL 539
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIreLAETGiTQVIVTHEVEVARKTASRVVYM 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-524 |
3.77e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 370 AELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIgyFSQELEHLDDGVTLLDSLLTL-PAMT--- 445
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAALAAGVAIIYQELHLvPEMTvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 446 -------------------QTQARTILGCFlfsGEEV--RKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLdiDS 504
Cdd:PRK11288 99 nlylgqlphkggivnrrllNYEAREQLEHL---GVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL--SA 173
|
170 180
....*....|....*....|....*.
gi 1844953743 505 RErIEQ-----ALLRYPGAMVI-VSH 524
Cdd:PRK11288 174 RE-IEQlfrviRELRAEGRVILyVSH 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-197 |
3.96e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtLE--------LDKGSVERRLPldqwgwmgQQTE-- 78
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG-LEkptegqifIDGEDVTHRSI--------QQRDic 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 ---ADEAVFTHAYVEEGCpeHYAAK---RRLKELEAQMQDAAApcmeslLADYQEAAERYmgldgyhwetqverkllqlg 152
Cdd:PRK11432 82 mvfQSYALFPHMSLGENV--GYGLKmlgVPKEERKQRVKEALE------LVDLAGFEDRY-------------------- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 153 lgrelwdqpLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA 197
Cdd:PRK11432 134 ---------VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
372-501 |
4.20e-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: 51.12 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAA---GKV--------RQHPQTSIGYFSQeLEHLDDGVTLLDSL-- 438
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqprkPDQFQKCVAYVRQ-DDILLPGLTVRETLty 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 439 ---LTLPAMTQTQARTILGCFLFSGEEVRKRIGD-----LSMGERCRLAFlklyfsGANL------LVLDEPTNYLD 501
Cdd:cd03234 105 taiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSI------AVQLlwdpkvLILDEPTSGLD 175
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
360-533 |
4.29e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 360 AFRYG--ERELFAELSLSVDRGDRLAVLGPNGSGKT-TLLKLLvgELQPAAGKVrqHPQTSIGYFSQELEHLDDGvTL-- 434
Cdd:PRK15134 14 AFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVV--YPSGDIRFHGESLLHASEQ-TLrg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 435 ----------------LDSLLTLP-----------AMTQTQART-ILGCFLFSG-EEVRKRIGD----LSMGERCRLAFL 481
Cdd:PRK15134 89 vrgnkiamifqepmvsLNPLHTLEkqlyevlslhrGMRREAARGeILNCLDRVGiRQAAKRLTDyphqLSGGERQRVMIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 482 KLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPG----AMVIVSHDRFFIRKLA 533
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLA 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-220 |
4.64e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.55 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 14 YAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQqteadeavfthayveegc 93
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVL---------WQGK------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 94 PEHYAaKRRLKELEAQM----QDAAAPCMESLLADYQEAAERYMGLDgyhwETQVERKL---LQLGLGRELWDQPLGQLS 166
Cdd:PRK13638 64 PLDYS-KRGLLALRQQVatvfQDPEQQIFYTDIDSDIAFSLRNLGVP----EAEITRRVdeaLTLVDAQHFRHQPIQCLS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 167 GGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPGT---VVFVSHD 220
Cdd:PRK13638 139 HGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHD 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-227 |
5.17e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTEADEAvfthayveegcpehyAAKRR 102
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI---------FNGQPMSKLSS---------------AAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 103 LK--ELEAQMQdaaapcMESLLADYQEAAERYMGL-DGYHWETQVERKLLQL----GLGRELWDQPlGQLSGGQKTRAQL 175
Cdd:PRK11629 84 LRnqKLGFIYQ------FHHLLPDFTALENVAMPLlIGKKKPAEINSRALEMlaavGLEHRANHRP-SELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 176 ARLMVREPQLLLLDEPTNHLD---AASLEWLEVWLRAYPGTV-VFVSHDRHFMDRV 227
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHDLQLAKRM 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
364-501 |
5.23e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 50.24 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAA--GKVR-----QHPQT---SIGYFSQELEHLDdgvt 433
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLingrpLDKRSfrkIIGYVPQDDILHP---- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 434 lldslltlpamTQTQARTilgcFLFSGEevrkrIGDLSMGERCRLAF-LKLyFSGANLLVLDEPTNYLD 501
Cdd:cd03213 96 -----------TLTVRET----LMFAAK-----LRGLSGGERKRVSIaLEL-VSNPSLLFLDEPTSGLD 143
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
349-502 |
7.22e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.14 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 349 ASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEHL 428
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 ddgVTLLDSLLTLPAMTQTQARTILGCF----LFS-------------------GEEVRKRIGDLSMGERCRLAFLKLYF 485
Cdd:PRK10253 83 ---IGLLAQNATTPGDITVQELVARGRYphqpLFTrwrkedeeavtkamqatgiTHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170
....*....|....*..
gi 1844953743 486 SGANLLVLDEPTNYLDI 502
Cdd:PRK10253 160 QETAIMLLDEPTTWLDI 176
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
383-523 |
7.52e-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: 52.71 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 383 AVLGPNGSGKTTLLKLLVGELQPAAGKVR---QHPQTSIGYFSQEL----EH--LDDGVTLLDSLL---TLPAMTQTQAR 450
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLvggKDIETNLDAVRQSLgmcpQHniLFHHLTVAEHILfyaQLKGRSWEEAQ 1039
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 451 TILGCFLFSGEEVRKR---IGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRY-PGAMVIVS 523
Cdd:TIGR01257 1040 LEMEAMLEDTGLHHKRneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYrSGRTIIMS 1116
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-204 |
7.54e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 7.54e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1844953743 161 PLGQ-LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLE 204
Cdd:PTZ00265 1354 PYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
364-523 |
8.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.96 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV--RQHPQTsigyfSQELEHLDDGVTLL----DS 437
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPIT-----KENIREVRKFVGLVfqnpDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 438 LLTLPAMTQTQA---------------RTILGCFLFSGEEVRKRI-GDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:PRK13652 90 QIFSPTVEQDIAfgpinlgldeetvahRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180
....*....|....*....|....*
gi 1844953743 502 IDSRERIEQALLRYP---GAMVIVS 523
Cdd:PRK13652 170 PQGVKELIDFLNDLPetyGMTVIFS 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-234 |
8.44e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDKgsverrLPLDQWgwmgqqteade 81
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsEGEILLDA------QPLESW----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 avfthayveegcpEHYAAKRRLKELEAQMQDAAAPCMESLLADYQEAAERYMGLDGYHWETQVERKLLQLGLgrelwdQP 161
Cdd:PRK10575 79 -------------SSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGL------KP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 162 LGQ-----LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHDRHFMDRVATCLV 232
Cdd:PRK10575 140 LAHrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHqvdvLALVHRLSQERGLTVIAVLHDINMAARYCDYLV 219
|
..
gi 1844953743 233 EL 234
Cdd:PRK10575 220 AL 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
372-582 |
1.06e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQH--------P----QTSIGYFSQElEHLDDGVTLLDS-L 438
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcarltPakahQLGIYLVPQE-PLLFPNLSVKENiL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 439 LTLPAMTQTQAR-----TILGCFLfsgeEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERI---EQ 510
Cdd:PRK15439 109 FGLPKRQASMQKmkqllAALGCQL----DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLfsrIR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 511 ALLRYPGAMVIVSHDRFFIRKLATkllWLSAERS-PIAFSGTYDEYAEASLASESSPEQLA-RANERRQLELTL 582
Cdd:PRK15439 185 ELLAQGVGIVFISHKLPEIRQLAD---RISVMRDgTIALSGKTADLSTDDIIQAITPAAREkSLSASQKLWLEL 255
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
363-415 |
1.14e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 1.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 363 YGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQ 415
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT 64
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-525 |
1.32e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-----------------RQHPQTSIGYFSQ 423
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgllalRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 424 ELEHLDDGVTLLDSLLTLPAMTQTQARTILGCF-LFSGEEVRKR-IGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLD 501
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALtLVDAQHFRHQpIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180
....*....|....*....|....*..
gi 1844953743 502 IDSRERIEQALLRYPGA---MVIVSHD 525
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQgnhVIISSHD 195
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
353-525 |
1.38e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGE-RELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQtSIGYFSQELEHLDDG 431
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLL----DSLLTLPAMTQTQARTILGCFLfSGEEVRKRIGD-----------------LSMGERCRLAFLKLYFSGANL 490
Cdd:PRK13636 84 VGMVfqdpDNQLFSASVYQDVSFGAVNLKL-PEDEVRKRVDNalkrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1844953743 491 LVLDEPTNYLDIDSRERIEQALLRYPGAM----VIVSHD 525
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELgltiIIATHD 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
353-524 |
1.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGERELFA-----ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---------------Q 412
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 413 HPQTSIGYFSQELEHLDDGVTLLDSLLTLP---AMTQTQARTILGCFL----FSGEEVRKRIGDLSMGERCRLAFLKLYF 485
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVAFGPqnfGIPKEKAEKIAAEKLemvgLADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 486 SGANLLVLDEPTNYLDIDSR---ERIEQALLRYPGAMVIVSH 524
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
160-239 |
1.51e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.14 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 160 QPLGQLSGGQKTRAQLA-RLMVREP-----QLLLLDEPTNHLDAASLEW-LEVWLRAYPGTVVF----VSHDRHFMDRVA 228
Cdd:cd03240 111 DMRGRCSGGEKVLASLIiRLALAETfgsncGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFqlivITHDEELVDAAD 190
|
90
....*....|..
gi 1844953743 229 T-CLVELTPTGC 239
Cdd:cd03240 191 HiYRVEKDGRQK 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-219 |
1.54e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG----------TLeldkgsverrlpldqwgwM 73
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlTL------------------F 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 74 GQQTEADEAVF---TH-AYVEEgcpehyaakrrlkeleaqmqdaaapcmeSLLADYQ-EAAERYMGLDGYHWETQV---- 144
Cdd:PRK10938 322 GRRRGSGETIWdikKHiGYVSS----------------------------SLHLDYRvSTSVRNVILSGFFDSIGIyqav 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 145 ---ERKLLQ-----LGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPG 212
Cdd:PRK10938 374 sdrQQKLAQqwldiLGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNrqlvRRFVDVLISEGET 453
|
....*..
gi 1844953743 213 TVVFVSH 219
Cdd:PRK10938 454 QLLFVSH 460
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
144-237 |
1.79e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.65 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLgrelWD-------QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD---AASLEWLEVWLRA-Ypg 212
Cdd:COG1117 131 VEESLRKAAL----WDevkdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEELILELKKdY-- 204
|
90 100 110
....*....|....*....|....*....|....*.
gi 1844953743 213 TVVFVSHDrhfM-------DRVA----TCLVELTPT 237
Cdd:COG1117 205 TIVIVTHN---MqqaarvsDYTAffylGELVEFGPT 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
135-222 |
1.88e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 135 LDGYHWETQVERKLLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVWLRAY 210
Cdd:PRK15134 396 LSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKH 475
|
90
....*....|..
gi 1844953743 211 PGTVVFVSHDRH 222
Cdd:PRK15134 476 QLAYLFISHDLH 487
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
371-543 |
2.23e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSIGYFSQELEHLDDGVTLLDSLLTLPAMTQTQAR 450
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 451 TILGCFL-FS--GEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRYPGA---MVIVSH 524
Cdd:PRK13546 122 AMTPKIIeFSelGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSH 201
|
170
....*....|....*....
gi 1844953743 525 DRFFIRKLATKLLWLSAER 543
Cdd:PRK13546 202 NLGQVRQFCTKIAWIEGGK 220
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-201 |
2.44e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 3 LLIKAMNVMKEyaGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGT--LELDKGSVERR----LPLDqwgwmgQQ 76
Cdd:PRK09580 2 LSIKDLHVSVE--DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKgkdlLELS------PE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 TEADEAVF-THAYVEE--GCPEHYAAKRRLKELEAQMQdaaapcmeslladyQEAaerymgLDGYHWETQVERKLLQLGL 153
Cdd:PRK09580 74 DRAGEGIFmAFQYPVEipGVSNQFFLQTALNAVRSYRG--------------QEP------LDRFDFQDLMEEKIALLKM 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1844953743 154 GRELWDQPLGQ-LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLE 201
Cdd:PRK09580 134 PEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALK 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
366-560 |
2.61e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 366 RELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVrqHPQTSIGYFSQELEHLDdgVTLLDSLLTL-PAM 444
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--WAERSIAYVPQQAWIMN--ATVRGNILFFdEED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 445 TQTQARTILGCFLFS-----GEEVRKRIGD----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQALLRy 515
Cdd:PTZ00243 749 AARLADAVRVSQLEAdlaqlGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFL- 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1844953743 516 pGAM-----VIVSHdRFFIRKLATKLLWLSAERspIAFSGTYDEYAEASL 560
Cdd:PTZ00243 828 -GALagktrVLATH-QVHVVPRADYVVALGDGR--VEFSGSSADFMRTSL 873
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-226 |
2.86e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEY-AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGtleldkgsVERrlPLDQWGWMG----QQTE 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IER--PSAGKIWFSghdiTRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 79 ADEAVFTHAYVEEGCPEHYAAKRRlkeleAQMQDAAAPCMESlladyqeaaerymGLDGYHWETQVERKLLQLGLGRELW 158
Cdd:PRK10908 71 NREVPFLRRQIGMIFQDHHLLMDR-----TVYDNVAIPLIIA-------------GASGDDIRRRVSAALDKVGLLDKAK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 159 DQPLgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLevwLRAYPG------TVVFVSHDRHFMDR 226
Cdd:PRK10908 133 NFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI---LRLFEEfnrvgvTVLMATHDIGLISR 202
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
144-251 |
3.13e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLGRELWDQpLGQ----LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASL----EWLEVWLRAYpgTVV 215
Cdd:PRK14243 128 VERSLRQAALWDEVKDK-LKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTlrieELMHELKEQY--TII 204
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844953743 216 FVSHDRHFMDRVA--TCL--VELTPTGCRKyrGGYTEYTR 251
Cdd:PRK14243 205 IVTHNMQQAARVSdmTAFfnVELTEGGGRY--GYLVEFDR 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
356-525 |
3.41e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 356 LERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR------QHPQTSIGYFSQELEHLd 429
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplAEAREDTRLMFQDARLL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 430 DGVTLLDSL-LTLPAMTQTQARTILgcflfsgEEV--RKRIGD----LSMGERCRLAFLKLYFSGANLLVLDEPTNYLD- 501
Cdd:PRK11247 94 PWKKVIDNVgLGLKGQWRDAALQAL-------AAVglADRANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
|
170 180
....*....|....*....|....*..
gi 1844953743 502 ---IDSRERIEQALLRYPGAMVIVSHD 525
Cdd:PRK11247 167 ltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
365-411 |
3.45e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.93 E-value: 3.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1844953743 365 ERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
354-512 |
3.91e-06 |
|
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: 48.30 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGER---ELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV---------------RQHpq 415
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrwlRSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 416 tsIGYFSQElEHLDDGvTLLDSL-LTLPAMTQTQArtilgcflfsgEEVRK-----------------RIGD----LSMG 473
Cdd:cd03249 79 --IGLVSQE-PVLFDG-TIAENIrYGKPDATDEEV-----------EEAAKkanihdfimslpdgydtLVGErgsqLSGG 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1844953743 474 ERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQAL 512
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
144-199 |
3.99e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 3.99e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLGRE----LWDQPLGqLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:PRK14239 125 VEKSLKGASIWDEvkdrLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPIS 183
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-196 |
4.14e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.31 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGtLEL-DKGSVErrlpLDqwgwmGQQ-TEADEA-----------VFTHAY- 88
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERpTSGSVL----VD-----GVDlTALSERelraarrkigmIFQHFNl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 -----VEEgcpehyaakrrlkeleaqmqDAAAPcMEslLADYqEAAERymgldgyhwETQVErKLLQL-GLGRELWDQPl 162
Cdd:COG1135 94 lssrtVAE--------------------NVALP-LE--IAGV-PKAEI---------RKRVA-ELLELvGLSDKADAYP- 138
|
170 180 190
....*....|....*....|....*....|....
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
146-228 |
4.17e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 146 RKLLQL-GLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDA-ASLEWLEVWLRAYPG---TVVFVSHD 220
Cdd:PRK13634 126 REMIELvGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPkGRKEMMEMFYKLHKEkglTTVLVTHS 205
|
....*...
gi 1844953743 221 rhfMDRVA 228
Cdd:PRK13634 206 ---MEDAA 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-497 |
4.46e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 351 RSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGkvrqhpqtSIGYFSQELEHLDD 430
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSG--------RIVFDGKDITDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 431 GVTLLDSLLTLPAMTQTQARTI------LGCFLFSGEEVRKRI------------------GDLSMGERCRLAFLKLYFS 486
Cdd:PRK11614 75 AKIMREAVAIVPEGRRVFSRMTveenlaMGGFFAERDQFQERIkwvyelfprlherriqraGTMSGGEQQMLAIGRALMS 154
|
170
....*....|.
gi 1844953743 487 GANLLVLDEPT 497
Cdd:PRK11614 155 QPRLLLLDEPS 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
372-524 |
5.11e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.14 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVG--ELQPAAGKVR-----------------------QHPqtsigyfsQELE 426
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILldgedilelspderaragiflafQYP--------VEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 427 hlddGVTLLDSLLTlpAMTQtQARTILGCFLFSgEEVRKRIGDLSMGErcrlAFLKLY----FSG--------------- 487
Cdd:COG0396 91 ----GVSVSNFLRT--ALNA-RRGEELSAREFL-KLLKEKMKELGLDE----DFLDRYvnegFSGgekkrneilqmllle 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 488 ANLLVLDEPTNYLDIDS----RERIEQalLRYPG-AMVIVSH 524
Cdd:COG0396 159 PKLAILDETDSGLDIDAlrivAEGVNK--LRSPDrGILIITH 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-196 |
5.32e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVER--RLPLD-QWGWMGQQTEADEAVFTHAYVEeg 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHsgRISFSpQTSWIMPGTIKDNIIFGLSYDE-- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpehYAAKRRLKELEaqmqdaaapcMESLLADYQEAAERYMGLDGYhwetqverkllqlglgrelwdqplgQLSGGQKTR 172
Cdd:TIGR01271 516 ----YRYTSVIKACQ----------LEEDIALFPEKDKTVLGEGGI-------------------------TLSGGQRAR 556
|
170 180
....*....|....*....|....
gi 1844953743 173 AQLARLMVREPQLLLLDEPTNHLD 196
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-525 |
5.39e-06 |
|
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: 48.10 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV--------RQHPQT-SIGYFSQE 424
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQErNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 425 ---LEHLddgvTLLDSL---------LTLPAMTQTQART--ILGCFLFSGEEVRKRiGDLSMGERCRLAFLKLYFSGANL 490
Cdd:cd03296 83 yalFRHM----TVFDNVafglrvkprSERPPEAEIRAKVheLLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1844953743 491 LVLDEPTNYLDIDSRERIEQALLRYPGAM----VIVSHD 525
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHD 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-196 |
6.05e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAG--KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE-----------RRL------ 65
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenlKEIrkkigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 66 ----PLDQwgWMGQQTEADEAvFThayveegcpehyaakrrlkeLEAQMQDAAApcMESLLADYQEAAerymGLDGYhwe 141
Cdd:PRK13632 88 ifqnPDNQ--FIGATVEDDIA-FG--------------------LENKKVPPKK--MKDIIDDLAKKV----GMEDY--- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 142 tqverkllqlgLGRElwdqPLgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK13632 136 -----------LDKE----PQ-NLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
148-236 |
6.77e-06 |
|
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: 46.93 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQ--LLLLDEPTNHLDAASLE-WLEVW--LRAYPGTVVFVSHDRH 222
Cdd:cd03238 71 LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINqLLEVIkgLIDLGNTVILIEHNLD 150
|
90
....*....|....
gi 1844953743 223 FMDRvATCLVELTP 236
Cdd:cd03238 151 VLSS-ADWIIDFGP 163
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
157-237 |
8.31e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 157 LWDQPlGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD---AASLEWLEVWLRAyPGTVVFVSHDRHFMDRVATC--- 230
Cdd:PRK14267 143 LNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYvaf 220
|
90
....*....|..
gi 1844953743 231 -----LVELTPT 237
Cdd:PRK14267 221 lylgkLIEVGPT 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-228 |
8.43e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAG------KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV----------ERR 64
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 65 LPLDQWGWMGQQTEADEAVFThaYVEEgcpehyaakrrlkeleaqmqDAA-APcmESLLADYQEAAERymgldgyhwetq 143
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVAT--IVEE--------------------DVAfGP--ENLGIPPEEIRER------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 144 VERKLLQLGLgRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSh 219
Cdd:PRK13633 125 VDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGrrevVNTIKELNKKYGITIILIT- 202
|
....*....
gi 1844953743 220 drHFMDRVA 228
Cdd:PRK13633 203 --HYMEEAV 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-225 |
8.67e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.48 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQqtead 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL----LD-----GE----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 EAVFTHAyveegcpehyaakrrlkeLEAQM-------QdaaapcmESLLADYQEAAE---------RYMGLDgyhWETQV 144
Cdd:COG1129 67 PVRFRSP------------------RDAQAagiaiihQ-------ELNLVPNLSVAEniflgreprRGGLID---WRAMR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 145 ER--KLL-QLGLGRELwDQPLGQLSGGQKtraQL---ARLMVREPQLLLLDEPTNHLDAASLEWL-EVW--LRAYPGTVV 215
Cdd:COG1129 119 RRarELLaRLGLDIDP-DTPVGDLSVAQQ---QLveiARALSRDARVLILDEPTASLTEREVERLfRIIrrLKAQGVAII 194
|
250
....*....|
gi 1844953743 216 FVShdrHFMD 225
Cdd:COG1129 195 YIS---HRLD 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
352-546 |
8.78e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKvRQHPQTSIGYFSQE-LEHL-- 428
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLSFEqLQKLvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 ----DDGVTLL-----DSLLTLPAMTQTQARTILGCFLFS-----GEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLD 494
Cdd:PRK10938 81 dewqRNNTDMLspgedDTGRTTAEIIQDEVKDPARCEQLAqqfgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 495 EPTNYLDIDSRERIEQALLRYPG---AMVIVShDRF-----FIRK---LATKLLWLSAERSPI 546
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQsgiTLVLVL-NRFdeipdFVQFagvLADCTLAETGEREEI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
164-228 |
1.11e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVwLRAYPGT-VVFVSHD----RHFMDRVA 228
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKD-LQRELGMaLLLITHDlgvvRRFADRVA 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-199 |
1.14e-05 |
|
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: 46.72 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTeadeavfthayveegcpe 95
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL----ID-----GVDI------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 hyaAKRRLKELEAQM----QDaaaPCMESlladyqeAAERYmGLD--GYHWETQVERKLLQLGLgRELWDQPLGQL---- 165
Cdd:cd03244 69 ---SKIGLHDLRSRIsiipQD---PVLFS-------GTIRS-NLDpfGEYSDEELWQALERVGL-KEFVESLPGGLdtvv 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 166 -------SGGQKtraQL---ARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03244 134 eeggenlSVGQR---QLlclARALLRKSKILVLDEATASVDPET 174
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-227 |
1.24e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYA-GKPLFEQ---------VELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDkgsver 63
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvKRGLFKPerlvkaldgVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYYQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 64 rlpldqwgwmGQQ-TEADEA-----------VFTHAYveegcpehyAAKRRLKELEAQMQdaaapcmESLLADYQ-EAAE 130
Cdd:PRK11308 76 ----------GQDlLKADPEaqkllrqkiqiVFQNPY---------GSLNPRKKVGQILE-------EPLLINTSlSAAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 131 RymgldgyhwETQVERKLLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWL--- 203
Cdd:PRK11308 130 R---------REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNLMmdl 200
|
250 260 270
....*....|....*....|....*....|
gi 1844953743 204 --EVWLrAYpgtvVFVSHD----RHFMDRV 227
Cdd:PRK11308 201 qqELGL-SY----VFISHDlsvvEHIADEV 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
342-410 |
1.25e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 47.63 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 342 KLSASDFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
353-525 |
1.29e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.29 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRYGE-RELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHpQTSIGYFSQElehldDG 431
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS-GIDTGDFSKL-----QG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 432 VTLLDSLLTLPAMTQTQARTILGCFLFSGE-------EVRKRIG-----------------DLSMGERCRLAFLKLYFSG 487
Cdd:PRK13644 75 IRKLVGIVFQNPETQFVGRTVEEDLAFGPEnlclppiEIRKRVDralaeiglekyrhrspkTLSGGQGQCVALAGILTME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 488 ANLLVLDEPTNYLDIDS----RERIEQaLLRYPGAMVIVSHD 525
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSgiavLERIKK-LHEKGKTIVYITHN 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
159-192 |
1.58e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 1.58e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1844953743 159 DQPLGQLSGG--QKtrAQLARLMVREPQLLLLDEPT 192
Cdd:COG1129 389 EQPVGNLSGGnqQK--VVLAKWLATDPKVLILDEPT 422
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-196 |
1.58e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.80 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 25 LEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGS-------VERRLPLDQWGWMGQQTEADEA--VFTHAYVEEGCPE 95
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqpTRQALQKNLVAYVPQSEEVDWSfpVLVEDVVMMGRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 HYAAKRRLKELEAQMQDAAApcmeslladyqeaaERYMGLDGYHwetqverkllqlglgrelwdQPLGQLSGGQKTRAQL 175
Cdd:PRK15056 108 HMGWLRRAKKRDRQIVTAAL--------------ARVDMVEFRH--------------------RQIGELSGGQKKRVFL 153
|
170 180
....*....|....*....|.
gi 1844953743 176 ARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVD 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-219 |
1.62e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 4 LIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTleldkgsverrLPLDQWG----WMGQQ--- 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-----------YPHGTWDgeiyWSGSPlka 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 77 -----TEADEAVFTHayveegcpehyaakrrlKELeaqmqdaaapcmeSLLADYQEAAERYMG----LDGY--HWETQVE 145
Cdd:TIGR02633 70 snirdTERAGIVIIH-----------------QEL-------------TLVPELSVAENIFLGneitLPGGrmAYNAMYL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 146 R--KLL-QLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLR---AYPGTVVFVSH 219
Cdd:TIGR02633 120 RakNLLrELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRdlkAHGVACVYISH 199
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
163-196 |
1.79e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 46.72 E-value: 1.79e-05
10 20 30
....*....|....*....|....*....|....
gi 1844953743 163 GQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:COG4598 153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-246 |
2.16e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLGLGRelwdqPLGQLSGGQKTRAQLARLM---VREPQLLLLDEPTNHLDAASLEWL-EVWLR-AYPG-TVVFVSHDR 221
Cdd:PRK00635 798 LDYLPLGR-----PLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALiYVLQSlTHQGhTVVIIEHNM 872
|
90 100
....*....|....*....|....*
gi 1844953743 222 HFMdRVATCLVELTPTGCRKyrGGY 246
Cdd:PRK00635 873 HVV-KVADYVLELGPEGGNL--GGY 894
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
353-543 |
2.21e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.02 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 353 LVRLERAAFRY-GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV------------RQHP--QTS 417
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknREVPflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 418 IGYFSQElEHLDDGVTLLDSlLTLPAMtqtqartILGCflfSGEEVRKRIG-----------------DLSMGERCRLAF 480
Cdd:PRK10908 81 IGMIFQD-HHLLMDRTVYDN-VAIPLI-------IAGA---SGDDIRRRVSaaldkvglldkaknfpiQLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 481 LKLYFSGANLLVLDEPTNYLDIDSRE---RIEQALLRYPGAMVIVSHDRFFIRKLATKLLWLSAER 543
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-199 |
2.53e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 47.35 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELD-KGSVERRLPldqwgwmGQQTEADEAVFTHAYVEEG--- 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVLLN-------GMPIDAKEMRAISAYVQQDdlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 CP-----EH--YAAKRRLKELEAQMQDAAApcmeslladyqeaaerymgldgyhwetqVERKLLQLGLgRELWDQPLGQ- 164
Cdd:TIGR00955 111 IPtltvrEHlmFQAHLRMPRRVTKKEKRER----------------------------VDEVLQALGL-RKCANTRIGVp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1844953743 165 -----LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:TIGR00955 162 grvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-227 |
3.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.15 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFE-----QVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsverrlpldqwgwmgQQTEADEAV 83
Cdd:PRK13645 11 NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG---------------QTIVGDYAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 fthayveegcPehyAAKRRLKELEAQMQDAAAPCMESLLADYQEAAER-------YMGLDGYHWETQVERKLLQLGLGRE 156
Cdd:PRK13645 76 ----------P---ANLKKIKEVKRLRKEIGLVFQFPEYQLFQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPED 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 157 LWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLE-WLEVWLR---AYPGTVVFVSHDrhfMDRV 227
Cdd:PRK13645 143 YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlnkEYKKRIIMVTHN---MDQV 214
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-220 |
3.14e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 33 IAIYGRNGIGKTTLLRLLAGTLELDKGSvERRLPLDQWGWMGQQTEAdEAVFTHAyveegcPEHYAAKRRLKELEAQMQD 112
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSEEASV-ELEFEHG------GKRYRIERRQGEFAEFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 113 AAAPCMESL-----LADYQEAAERYMGLdgyhwETQVERKLLQLGLGRELWDQ---------PLGQLSGGQKTRAQLARL 178
Cdd:COG0419 98 KPSERKEALkrllgLEIYEELKERLKEL-----EEALESALEELAELQKLKQEilaqlsgldPIETLSGGERLRLALADL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 179 MVrepqlLLLDepTNHLDAASLEWLEVWLRAypgtVVFVSHD 220
Cdd:COG0419 173 LS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
371-588 |
3.16e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.98 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR---QH--PQTSigyfSQELEHLDDGVTLldsLLTLPAmT 445
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHitPETG----NKNLKKLRKKVSL---VFQFPE-A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 446 QTQARTILG-------CFLFSGEEVR-------KRIG-----------DLSMGERCRLAFLKLYFSGANLLVLDEPTNYL 500
Cdd:PRK13641 97 QLFENTVLKdvefgpkNFGFSEDEAKekalkwlKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 501 DIDSRERIEQALLRYPGA---MVIVSHDRFFIRKLATKLLWLSAER-----SPIA-FSGTydEYAEASLASESSPEQLAR 571
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKlikhaSPKEiFSDK--EWLKKHYLDEPATSRFAS 254
|
250 260
....*....|....*....|..
gi 1844953743 572 ANERRQLE-----LTLAQLMSE 588
Cdd:PRK13641 255 KLEKGGFKfsempLTIDELVDG 276
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-198 |
3.35e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.88 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGK-PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDK---GSVERRLPLDQWGWMGQqt 77
Cdd:PRK13657 339 DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGtdiRTVTRASLRRNIAVVFQ-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 eadEAVFTHAYVEE----GCPEHYAAkrrlkELEAQMQDAAApcmesllADYQEAAErymglDGYhwETQV-ERkllqlg 152
Cdd:PRK13657 417 ---DAGLFNRSIEDnirvGRPDATDE-----EMRAAAERAQA-------HDFIERKP-----DGY--DTVVgER------ 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844953743 153 lGRelwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAA 198
Cdd:PRK13657 469 -GR--------QLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-219 |
3.59e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 23 VELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQT------EADEA-------------V 83
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIL---------IDGKPVrirsprDAIALgigmvhqhfmlvpN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 84 FThayVEE----GCPEHYAAKRRLKELEAQMqdaaapcmeslladyQEAAERYmGLDgyhwetqVErkllqlglgrelWD 159
Cdd:COG3845 95 LT---VAEnivlGLEPTKGGRLDRKAARARI---------------RELSERY-GLD-------VD------------PD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 160 QPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHL---DAASLewLEV--WLRAYPGTVVFVSH 219
Cdd:COG3845 137 AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADEL--FEIlrRLAAEGKSIIFITH 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
164-203 |
3.62e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 3.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASlEWL 203
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYL 617
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-201 |
3.72e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG--TLELDKGSVErrlpLDqwgwmGQQTeadeavfTHAYVEEg 92
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL----FK-----GEDI-------TDLPPEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 cpehyaakRRLKELEAQMQDAAApcMESL-LADYQeaaeRYMGlDGyhwetqverkllqlglgrelwdqplgqLSGGQKT 171
Cdd:cd03217 74 --------RARLGIFLAFQYPPE--IPGVkNADFL----RYVN-EG---------------------------FSGGEKK 111
|
170 180 190
....*....|....*....|....*....|
gi 1844953743 172 RAQLARLMVREPQLLLLDEPTNHLDAASLE 201
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
372-539 |
3.81e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.51 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLL------------VGELQPAAGK-----------VRQHpqtsIGYFSQELeHL 428
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARslsqqkglirqLRQH----VGFVFQNF-NL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 429 DDGVTLLDSLLTLPAMTQTQ--------ARTILGCFLFSGEEVR--KRigdLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEpkeeatarARELLAKVGLAGKETSypRR---LSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844953743 499 YLDIDSRERIE---QALLRYPGAMVIVSHDRFFIRKLATKLLWL 539
Cdd:PRK11264 174 ALDPELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-199 |
4.08e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 30 GERIAIYGRNGIGKTTLLRLLAGTLE--------LDKGSVERRLPLDQWGWMGQqteaDEAVFTHAYVEEGCPehYAAKR 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnnftgtiLANNRKPTKQILKRTGFVTQ----DDILYPHLTVRETLV--FCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 102 RL-KELEAQMQDAAApcmESLLADyqeaaeryMGLdgyhweTQVERKLLQLGLGRelwdqplgQLSGGQKTRAQLARLMV 180
Cdd:PLN03211 168 RLpKSLTKQEKILVA---ESVISE--------LGL------TKCENTIIGNSFIR--------GISGGERKRVSIAHEML 222
|
170
....*....|....*....
gi 1844953743 181 REPQLLLLDEPTNHLDAAS 199
Cdd:PLN03211 223 INPSLLILDEPTSGLDATA 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-61 |
4.58e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 4.58e-05
10 20 30
....*....|....*....|....*....|..
gi 1844953743 30 GERIAIYGRNGIGKTTLLRLLAGTLELDKGSV 61
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
148-227 |
4.58e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.00 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEVWL--RAYPGTVVFVSHDrhfM 224
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpKGEHEMMQLILdaKANNKTVFVITHT---M 236
|
...
gi 1844953743 225 DRV 227
Cdd:PRK13631 237 EHV 239
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-246 |
4.71e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 141 ETQVERK---LLQLGLGRELWDQPLGQLSGGQKTRAQLAR-LMVRE--PQLLLLDEPTNHL---DAASLewLEVW--LRA 209
Cdd:TIGR00630 803 VPSISRKlqtLCDVGLGYIRLGQPATTLSGGEAQRIKLAKeLSKRStgRTLYILDEPTTGLhfdDIKKL--LEVLqrLVD 880
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844953743 210 YPGTVVFVSHDRHFMdRVATCLVELTPTGcrKYRGGY 246
Cdd:TIGR00630 881 KGNTVVVIEHNLDVI-KTADYIIDLGPEG--GDGGGT 914
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
364-524 |
5.36e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 364 GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGelQPA----AGKV--------------RQHpqtsIGYF---- 421
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDIlfkgesildlepeeRAH----LGIFlafq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 -----------------------SQELEHLD--DGVTLLDSLLTLPAMTQTqartilgcFL-------FSGeevrkrigd 469
Cdd:CHL00131 92 ypieipgvsnadflrlaynskrkFQGLPELDplEFLEIINEKLKLVGMDPS--------FLsrnvnegFSG--------- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 470 lsmGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQA---LLRYPGAMVIVSH 524
Cdd:CHL00131 155 ---GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGinkLMTSENSIILITH 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-199 |
5.38e-05 |
|
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: 44.71 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGK--PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDqwgwmGQQTeadea 82
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE----ID-----GIDI----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 83 vfthayveegcpehyaAKRRLKELEAQM----QDaaaPCMeslladyqeaaerYMG-----LDGYHWETQVE-RKLLQLG 152
Cdd:cd03369 73 ----------------STIPLEDLRSSLtiipQD---PTL-------------FSGtirsnLDPFDEYSDEEiYGALRVS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844953743 153 LGRElwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:cd03369 121 EGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
362-410 |
6.24e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.48 E-value: 6.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1844953743 362 RYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI 63
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
159-196 |
9.22e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.20 E-value: 9.22e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1844953743 159 DQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-228 |
9.79e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 43.57 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVERrlpldqwgwmgqqteadeavfthayveEGCPE 95
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL---------------------------DGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 96 HyaakrrlkeleaqmqdaaapcmeslLADYQEAAERYMGLdgyhwetqV--ERKLLQLGLGRELWDQ-PLGQ-LSGG--Q 169
Cdd:cd03215 65 T-------------------------RRSPRDAIRAGIAY--------VpeDRKREGLVLDLSVAENiALSSlLSGGnqQ 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 170 KtrAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW-----LRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:cd03215 112 K--VVLARWLARDPRVLILDEPTRGVDVGAKA--EIYrlireLADAGKAVLLISSEldelLGLCDRIL 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
372-500 |
1.13e-04 |
|
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: 45.20 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVG----------------ELQpaAGKVRQHPQTSIGYFSQELE--------- 426
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLK--ASNIRDTERAGIVIIHQELTlvpelsvae 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 427 --HLDDGVTLLDSLLTLPAMTQtQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYL 500
Cdd:TIGR02633 98 niFLGNEITLPGGRMAYNAMYL-RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-219 |
1.28e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVerrlpldqwgwmgqqteadeavfthay 88
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI--------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 89 veegcpehyaakrRLKELEAQMQDAAApcmeSLLAD----YQE--------AAERYM--------GLdgYHWETQVERKL 148
Cdd:PRK11288 62 -------------LIDGQEMRFASTTA----ALAAGvaiiYQElhlvpemtVAENLYlgqlphkgGI--VNRRLLNYEAR 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 149 LQL-GLGREL-WDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLE---VWLRAYPGTVVFVSH 219
Cdd:PRK11288 123 EQLeHLGVDIdPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFrviRELRAEGRVILYVSH 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
371-410 |
1.36e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.31 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV 67
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
159-196 |
1.39e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.39e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1844953743 159 DQPLGQLSGGQKTRAQLAR-LMVRePQLLLLDEPTNHLD 196
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARgLMTR-PKVLILDEPTRGVD 427
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
159-196 |
1.50e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.50e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1844953743 159 DQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
371-543 |
1.53e-04 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 43.72 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR--------------QHPQTSIGYFSQelehlddGVTLLD 436
Cdd:cd03258 23 DVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKARRRIGMIFQ-------HFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 437 SlltlpamtqtqaRTILGCFLF-------SGEEVRKRI-----------------GDLSMGERCRLAFLKLYFSGANLLV 492
Cdd:cd03258 96 S------------RTVFENVALpleiagvPKAEIEERVlellelvgledkadaypAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 493 LDEPTNYLDIDSRERIeQALLRYPGA-----MVIVSHDRFFIRKLATKLLWLSAER 543
Cdd:cd03258 164 CDEATSALDPETTQSI-LALLRDINRelgltIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-199 |
1.62e-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: 44.81 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 15 AGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE------RRLPLD----QWGWMGQQT------- 77
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgqdiRDVTQAslraAIGIVPQDTvlfndti 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 78 ---------EAdeavfTHAYVEEgcpehyAAKRrlkeleAQMQD--AAAPcmeslladyqeaaerymglDGYhwETQV-E 145
Cdd:COG5265 449 ayniaygrpDA-----SEEEVEA------AARA------AQIHDfiESLP-------------------DGY--DTRVgE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 146 RkllqlGLgrelwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:COG5265 491 R-----GL----------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
354-411 |
1.89e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 1.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERElFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:PRK10522 323 LELRNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
143-246 |
1.92e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 143 QVERK---LLQLGLGRELWDQPLGQLSGGQKTRAQLARLMVRE---PQLLLLDEPTNHL---DAASLewLEVWLR-AYPG 212
Cdd:cd03271 145 KIARKlqtLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKL--LEVLQRlVDKG 222
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844953743 213 -TVVFVSHDrhfMDRVATC--LVELTPTGCRkyRGGY 246
Cdd:cd03271 223 nTVVVIEHN---LDVIKCAdwIIDLGPEGGD--GGGQ 254
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-225 |
2.14e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 9 NVMK--EYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV-----ERRLPLDQWGWMGQQTEADE 81
Cdd:TIGR01257 933 NLVKifEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkDIETNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 82 AVFTHAYVEEGCPEHYAAKRRLKElEAQMQdaaapcMESLLADyqeaaerymglDGYHWETQVERKllqlglgrelwdqp 161
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWE-EAQLE------MEAMLED-----------TGLHHKRNEEAQ-------------- 1060
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 162 lgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEwlEVW---LRAYPGTVVFVShdRHFMD 225
Cdd:TIGR01257 1061 --DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR--SIWdllLKYRSGRTIIMS--THHMD 1121
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
371-537 |
2.15e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.52 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 371 ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQH-------------------------------PQTSIG 419
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklnraqrkafrrdiqmvfqdsisavnPRKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 420 YFSQE-LEHLddgvTLLDslltlPAMTQTQARTILGCFLFSGEEVRKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTN 498
Cdd:PRK10419 110 EIIREpLRHL----LSLD-----KAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844953743 499 YLD-------IDSRERIEQallRYPGAMVIVSHDRFFIRKLATKLL 537
Cdd:PRK10419 181 NLDlvlqagvIRLLKKLQQ---QFGTACLFITHDLRLVERFCQRVM 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-221 |
2.26e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 3 LLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTL----LRLLA--GTLELDkGSVERRLPLDQW----GW 72
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSteGEIQID-GVSWNSVTLQTWrkafGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 73 MGQQTeadeAVFTHAYveegcpehyaakRRLKELEAQMQDaaapcmESLLADYQEAAERYMgldgyhwETQVERKL-LQL 151
Cdd:TIGR01271 1297 IPQKV----FIFSGTF------------RKNLDPYEQWSD------EEIWKVAEEVGLKSV-------IEQFPDKLdFVL 1347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 152 GLGRELwdqplgqLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLR-AYPGTVVFVSHDR 221
Cdd:TIGR01271 1348 VDGGYV-------LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
354-411 |
2.32e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.47 E-value: 2.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 354 VRLERAAFRYGERELFAELSL-----SVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT 65
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
361-508 |
2.54e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 361 FRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGK--VRQHPQT--SIGYFSQELEHL-DDGVTLL 435
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEllIDDHPLHfgDYSYRSQRIRMIfQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 436 D------SLLTLPAMTQTQartilgcflFSGEEVRKRIGD------------------LSMGERCRLAFLKLYFSGANLL 491
Cdd:PRK15112 101 NprqrisQILDFPLRLNTD---------LEPEQREKQIIEtlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPKVI 171
|
170
....*....|....*..
gi 1844953743 492 VLDEPTNYLDIDSRERI 508
Cdd:PRK15112 172 IADEALASLDMSMRSQL 188
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-219 |
2.62e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.94 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 16 GKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGsvERRL---PLdqwgwmgqqteadeAVFTHAYVEEG 92
Cdd:PRK10790 353 DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG--EIRLdgrPL--------------SSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 93 CpehyaakrrlkeleAQMQDAAAPCMESLLADYQeaaeryMGLDGYhwETQVERKL--LQLG-LGRELWD---QPLGQ-- 164
Cdd:PRK10790 417 V--------------AMVQQDPVVLADTFLANVT------LGRDIS--EEQVWQALetVQLAeLARSLPDglyTPLGEqg 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 165 --LSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAY--PGTVVFVSH 219
Cdd:PRK10790 475 nnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-220 |
3.23e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.86 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSvERRLPLDQWGwMGQQTEAD--EAV----------F 84
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP-NSKITVDGIT-LTAKTVWDirEKVgivfqnpdnqF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 THAYVEEGCP---EHYAAKRrlkeleAQMQDAAAPCMESL-LADYQEAAERYmgldgyhwetqverkllqlglgrelwdq 160
Cdd:PRK13640 98 VGATVGDDVAfglENRAVPR------PEMIKIVRDVLADVgMLDYIDSEPAN---------------------------- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844953743 161 plgqLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAASLEWLEVWLRAYPG----TVVFVSHD 220
Cdd:PRK13640 144 ----LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
350-417 |
3.41e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.82 E-value: 3.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 350 SRSLVRLERAAFRYGERELFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV--RQHPQTS 417
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfyNNQAITD 75
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-218 |
3.67e-04 |
|
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: 42.25 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 12 KEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLElDKGSVERRLpldqwgwmgqqteadeavfthayvee 91
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE-GNVSVEGDI-------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 92 gcpeHYAAKrrlkeleaqmqdaaapcmesllaDYQEAAERYMGLDGY------HWETQVERKLLQLGLgRELWDQPLGQL 165
Cdd:cd03233 68 ----HYNGI-----------------------PYKEFAEKYPGEIIYvseedvHFPTLTVRETLDFAL-RCKGNEFVRGI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844953743 166 SGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS-LEWLEVwLRAYP---GTVVFVS 218
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTaLEILKC-IRTMAdvlKTTTFVS 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-199 |
3.77e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.47 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 5 IKAMNVMKEYAGK--PLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV--------ERRLP--LDQWGW 72
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghdlrDYTLAslRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 73 MGQQ------TEADEAVfthayveegcpehYAAKRRL--KELEAQMQDAAApcmesllADYQEAAERymGLDGYHWETQV 144
Cdd:PRK11176 422 VSQNvhlfndTIANNIA-------------YARTEQYsrEQIEEAARMAYA-------MDFINKMDN--GLDTVIGENGV 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 145 erkllqlglgrelwdqplgQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS 199
Cdd:PRK11176 480 -------------------LLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
366-525 |
3.89e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 366 RELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELqpaAGKVRQHPQTSIGYFSQELEHLD--DGVTLLDSLLTLPA 443
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVTGDVTLNGEPLAaiDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 444 MTQT----QARTI--LGCF---LFSGEE--------------------VRKRIGDLSMGERCRLAFLKLY---------F 485
Cdd:PRK13547 91 AAQPafafSAREIvlLGRYphaRRAGALthrdgeiawqalalagatalVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844953743 486 SGANLLVLDEPTNYLDIDSRERIEQALLRYP-----GAMVIVsHD 525
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnlGVLAIV-HD 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
164-228 |
4.07e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.87 E-value: 4.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLDAAS----LEWLEVWLRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsiLELLKDINRELGLTIVLITHEmdvvKRICDRVA 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-244 |
4.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 148 LLQLGLGRELWDQPLGQLSGGQKTRAQLARLMV---REPQLLLLDEPTNHLDAASLEWLEVWLRAYPG---TVVFVSHDR 221
Cdd:PRK00635 1683 LIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSlghSVIYIDHDP 1762
|
90 100
....*....|....*....|...
gi 1844953743 222 HFMdRVATCLVELTPtGCRKYRG 244
Cdd:PRK00635 1763 ALL-KQADYLIEMGP-GSGKTGG 1783
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-220 |
4.38e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 25 LEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpLDQwgwmgqqteADEAVFTHAYVEEGCPEHYAAKRRLK 104
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL----IDG---------VDIAKISDAELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 105 ELEAQMQ--DAAAPCMEslLADYQEAAERYMGLDGyhwetqverkLLQLGLGRELWDQPlGQLSGGQKTRAQLARLMVRE 182
Cdd:PRK10070 116 ALMPHMTvlDNTAFGME--LAGINAEERREKALDA----------LRQVGLENYAHSYP-DELSGGMRQRVGLARALAIN 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1844953743 183 PQLLLLDEPTNHLDAASLEWLE---VWLRA-YPGTVVFVSHD 220
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQdelVKLQAkHQRTIVFISHD 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
349-411 |
5.11e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.28 E-value: 5.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 349 ASRSLVRLERAAFRYGEreLFA--ELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGG--LLAvnNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL 63
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
351-524 |
5.77e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.79 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 351 RSLVRLERAAFRYGER---ELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV-----------RQHPQT 416
Cdd:TIGR00958 476 EGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 417 SIGYFSQELEHLDDGVT--LLDSLLTLPAMTQTQARTILGCFLFSGE-------EVRKRIGDLSMGERCRLAFLKLYFSG 487
Cdd:TIGR00958 556 QVALVGQEPVLFSGSVRenIAYGLTDTPDEEIMAAAKAANAHDFIMEfpngydtEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190
....*....|....*....|....*....|....*..
gi 1844953743 488 ANLLVLDEPTNYLDIDSRERIEQALLRYPGAMVIVSH 524
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
362-541 |
6.25e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 42.40 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 362 RYGERELFAELSLSvDRGdRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQT---------------SIGYFSQE-- 424
Cdd:COG4148 10 RRGGFTLDVDFTLP-GRG-VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQEar 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 425 -LEHLDDGVTLLDSLltlpAMTQTQARTIlgcflfSGEEV----------RKRIGDLSMGERCRLAFLKLYFSGANLLVL 493
Cdd:COG4148 88 lFPHLSVRGNLLYGR----KRAPRAERRI------SFDEVvellgighllDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 494 DEPTNYLDIDSRERIEQALLRYPGA----MVIVSHDRFFIRKLATKLLWLSA 541
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDEldipILYVSHSLDEVARLADHVVLLEQ 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
372-536 |
6.80e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.08 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQT----------SIGYFSQeLEHLDDGVTLLDSLLTL 441
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnisdvhqNMGYCPQ-FDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 442 PAMTQTQARTI----------LGCFLFSGeevrKRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIEQ- 510
Cdd:TIGR01257 2037 ARLRGVPAEEIekvanwsiqsLGLSLYAD----RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNt 2112
|
170 180
....*....|....*....|....*...
gi 1844953743 511 --ALLRYPGAMVIVSHDRFFIRKLATKL 536
Cdd:TIGR01257 2113 ivSIIREGRAVVLTSHSMEECEALCTRL 2140
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
457-525 |
7.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 457 LFSGEEVRkrIGDLSMGERC------RLAfLKLYFSGA-NLLVLDEPTNYLDIDSRER----IEQALLRYPgAMVIVSHD 525
Cdd:PRK03918 778 VYQGKERP--LTFLSGGERIalglafRLA-LSLYLAGNiPLLILDEPTPFLDEERRRKlvdiMERYLRKIP-QVIIVSHD 853
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
354-510 |
7.06e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 41.24 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGER--ELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVRQHPQ--TSIGyfsqeLEHLD 429
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdiSTIP-----LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 430 DGVTLLDSLLTLPAMTqtqARTILGCF-LFSGEEVRK--RIG----DLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDI 502
Cdd:cd03369 82 SSLTIIPQDPTLFSGT---IRSNLDPFdEYSDEEIYGalRVSegglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
....*...
gi 1844953743 503 DSRERIEQ 510
Cdd:cd03369 159 ATDALIQK 166
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
369-418 |
1.24e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1844953743 369 FAELSLSVDRGDRLAVL-GPNGSGKTTLLKLLVGELQPAAGKVRQHPQTSI 418
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALSGLLSRLDDVKFRKL 64
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-510 |
1.81e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVErrlpldqwgWMGQQTead 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL---------YLGKEV--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 81 eavfthayveegcpeHYAAKRrlkeleaQMQDAAAPCME---SLLADYQEAAERYMG------LDGYHWETQVER--KLL 149
Cdd:PRK10762 69 ---------------TFNGPK-------SSQEAGIGIIHqelNLIPQLTIAENIFLGrefvnrFGRIDWKKMYAEadKLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 150 Q-LGLGRELwDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHL---DAASLEWLEVWLRAYPGTVVFVSHdrhfmd 225
Cdd:PRK10762 127 ArLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISH------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 226 rvatclveltptgcrkyrggyteytRQKEL-ELRTQEQLYRKQQLLREQLEESIrtyrqwfhqgeKNAQMAEVPIQRgyf 304
Cdd:PRK10762 200 -------------------------RLKEIfEICDDVTVFRDGQFIAEREVADL-----------TEDSLIEMMVGR--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 305 qgragahvsrmnakmkeleRLEGN--RVEKPREAAHLKVK-LSASDfasrslVRleraafrygerelfaELSLSVDRGDR 381
Cdd:PRK10762 241 -------------------KLEDQypRLDKAPGEVRLKVDnLSGPG------VN---------------DVSFTLRKGEI 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 382 LAVLGPNGSGKTTLLKLLVGELQPAAGKVR--------QHPQ----TSIGYFSQELEHldDGVTLLDSL---LTLPAMTQ 446
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPRTSGYVTldghevvtRSPQdglaNGIVYISEDRKR--DGLVLGMSVkenMSLTALRY 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 447 TQARtilGCFLFSGEEVR-----------------KRIGDLSMGERCRLAFLKLYFSGANLLVLDEPTNYLDIDSRERIE 509
Cdd:PRK10762 359 FSRA---GGSLKHADEQQavsdfirlfniktpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
.
gi 1844953743 510 Q 510
Cdd:PRK10762 436 Q 436
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-62 |
1.89e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1844953743 26 EVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSVE 62
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE 57
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-52 |
2.10e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1844953743 17 KPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG 52
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
352-508 |
2.11e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.55 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 352 SLVRLERAAFRY--GERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAgkvrqHPQTSI----------- 418
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKItvdgitltakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 419 --------GYFSQELEHLDDGVTLLDSL---LTLPAMTQTQARTILgcflfsgEEVRKRIG----------DLSMGERCR 477
Cdd:PRK13640 79 vwdirekvGIVFQNPDNQFVGATVGDDVafgLENRAVPRPEMIKIV-------RDVLADVGmldyidsepaNLSGGQKQR 151
|
170 180 190
....*....|....*....|....*....|.
gi 1844953743 478 LAFLKLYFSGANLLVLDEPTNYLDIDSRERI 508
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-61 |
2.52e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 2.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 9 NVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAGTLELDKGSV 61
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
354-411 |
3.19e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 39.68 E-value: 3.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKVR 411
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
164-228 |
3.45e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 3.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844953743 164 QLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD----AASLEWLEVWLRAYPGTVVFVSHD----RHFMDRVA 228
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNlsivRKLADRVA 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-52 |
3.47e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 1 MTLLIKAMNVMKEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLLAG 52
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
354-523 |
4.12e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 354 VRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV------------RQHPQTSIGYF 421
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmadarhRRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 422 SQEL-----------EHLDdgvtlldslltlpamtqtqartilgcF---LF--SGEEVRKRIGDL--SMGercrLA-FL- 481
Cdd:NF033858 82 PQGLgknlyptlsvfENLD--------------------------FfgrLFgqDAAERRRRIDELlrATG----LApFAd 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844953743 482 ----KLyfSGA---------------NLLVLDEPTNYLDIDSR----ERIEQALLRYPGAMVIVS 523
Cdd:NF033858 132 rpagKL--SGGmkqklglccalihdpDLLILDEPTTGVDPLSRrqfwELIDRIRAERPGMSVLVA 194
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
32-60 |
5.04e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.46 E-value: 5.04e-03
10 20 30
....*....|....*....|....*....|.
gi 1844953743 32 RIAIYGRNGIGKTTLLRLLAGTLELD--KGS 60
Cdd:pfam13479 4 KILIYGPSGIGKTTFAKTLPKPLFLDteKGS 34
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
165-196 |
5.23e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.47 E-value: 5.23e-03
10 20 30
....*....|....*....|....*....|..
gi 1844953743 165 LSGGQKTRAQLARLMVREPQLLLLDEPTNHLD 196
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
373-410 |
6.91e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 38.91 E-value: 6.91e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1844953743 373 SLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
372-410 |
7.79e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 7.79e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1844953743 372 LSLSVDRGDRLAVLGPNGSGKTTLLKLLVGELQPAAGKV 410
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
344-399 |
8.43e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.48 E-value: 8.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1844953743 344 SASDFASRSLVRLERAAFRYGERELFAELSLSVDRGDRLAVLGPNGSGKTTLLKLL 399
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
159-220 |
8.66e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 38.85 E-value: 8.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844953743 159 DQPLGQLSGG--QKtrAQLARLMVREPQLLLLDEPTNHLDAASLEWleVW-----LRAYPGTVVFVSHD 220
Cdd:COG3845 397 DTPARSLSGGnqQK--VILARELSRDPKLLIAAQPTRGLDVGAIEF--IHqrlleLRDAGAAVLLISED 461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-220 |
8.89e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.12 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 12 KEYAGKPLFEQVELEVNAGERIAIYGRNGIGKTTLLRLL-------AGTLELDKGSVERRLPLDQwgwmgqqteadeavf 84
Cdd:PRK11288 261 DGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLygatrrtAGQVYLDGKPIDIRSPRDA--------------- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844953743 85 thayVEEG---CPEhyaaKRRlkeleaqmQDAAAPCmesllADYQE----AAERY-----MGLDGyHWETQ-VERKLLQL 151
Cdd:PRK11288 326 ----IRAGimlCPE----DRK--------AEGIIPV-----HSVADniniSARRHhlragCLINN-RWEAEnADRFIRSL 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844953743 152 GLGRELWDQPLGQLSGGQKTRAQLARLMVREPQLLLLDEPTNHLD-AASLEWLEVW--LRAYPGTVVFVSHD 220
Cdd:PRK11288 384 NIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvGAKHEIYNVIyeLAAQGVAVLFVSSD 455
|
|
| |
