|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-526 |
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: 658.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 10 VENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEELTVLE 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 90 ACFHHGNSTVELIKEYERCMETDGHPGLDG-----ILARMDHEKAWEYEQKAKQILSQLKI--RDFNQQVKSLSGGQLKR 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLerlaeLQEEFEALGGWEAEARAEEILSGLGFpeEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNYSYYLEK 242
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 243 REERIEAKTVEIERANNLYRTELEWMRRM-PQARGHK-ARYREDAFYELEKVAKQRfNNDNVKLDVK-ASYIGSKIFEAD 319
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFrAKARKAKqAQSRIKALEKLEREEPPR-RDKTVEIRFPpPERLGKKVLELE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 320 HLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGLQFDEQMKVIDV 399
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 400 VQDIAEvielgNGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEY 479
Cdd:COG0488 400 LRDGAP-----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2524717128 480 LRNFKGCVIVVSHDRYFMDKVVDHLLVFNGqGDIRDFPGNYTRYRDW 526
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFED-GGVREYPGGYDDYLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-527 |
5.50e-137 |
|
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: 411.25 E-value: 5.50e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEEL 85
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEACFHHGNSTVELIKEYERCMETDGHPG--LDGILARM-------DHEKAWEYEQKAKQILSQLKIRDFNQQVKSLS 156
Cdd:TIGR03719 84 TVRENVEEGVAEIKDALDRFNEISAKYAEPDadFDKLAAEQaelqeiiDAADAWDLDSQLEIAMDALRCPPWDADVTKLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNY 236
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 237 SYYLEKREER--IEAKTvEIERANNLYRtELEWMRRMPQARGHKARYREDAFYELEKVAKQRFNNDNVKLDVKASYIGSK 314
Cdd:TIGR03719 244 SSWLEQKQKRleQEEKE-ESARQKTLKR-ELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGDK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQ--DGLqfDE 392
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrDAL--DP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 QMKVIDVVQDIAEVIELGNgKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT 472
Cdd:TIGR03719 400 NKTVWEEISGGLDIIKLGK-REIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 473 LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQGDIRDFPGNYTRYRDWK 527
Cdd:TIGR03719 479 LRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDK 533
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-527 |
5.39e-127 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 385.63 E-value: 5.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFG-DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEEL 85
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEACFHHGNSTVELIKEYERCMETDGHPG--LDGILARM-------DHEKAWEYEQKAKQILSQLKIRDFNQQVKSLS 156
Cdd:PRK11819 86 TVRENVEEGVAEVKAALDRFNEIYAAYAEPDadFDALAAEQgelqeiiDAADAWDLDSQLEIAMDALRCPPWDAKVTKLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNY 236
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 237 SYYLEKREER--IEAKTvEIERANNLYRtELEWMRRMPQARGHKARYREDAFYELEKVAKQRfnndnvKLDVKASYI--- 311
Cdd:PRK11819 246 SSWLEQKAKRlaQEEKQ-EAARQKALKR-ELEWVRQSPKARQAKSKARLARYEELLSEEYQK------RNETNEIFIppg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 312 ---GSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQ--D 386
Cdd:PRK11819 318 prlGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQsrD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 GLqfDEQMKVIDVVQDIAEVIELGNgKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:PRK11819 398 AL--DPNKTVWEEISGGLDIIKVGN-REIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTN 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 467 DLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQGDIRDFPGNYTRYRDWK 527
Cdd:PRK11819 475 DLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDK 535
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-623 |
2.15e-117 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 363.50 E-value: 2.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEEL 85
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVL----EACFHHGnstvELIKEYE---RCMETDGhpgLDGILARM-------DHEKAWEYEQKAKQILSQLKIrDFNQQ 151
Cdd:PRK11147 82 TVYdfvaEGIEEQA----EYLKRYHdisHLVETDP---SEKNLNELaklqeqlDHHNLWQLENRINEVLAQLGL-DPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQ 231
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 232 YKGNYSYYLEKREE--RIEA-KTVEIERanNLYRTELeWMRRMPQARGHKARYREDAFYELEKVAKQRFN-NDNVKLDV- 306
Cdd:PRK11147 234 YPGNYDQYLLEKEEalRVEElQNAEFDR--KLAQEEV-WIRQGIKARRTRNEGRVRALKALRRERSERREvMGTAKMQVe 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 307 KASYIGSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQD 386
Cdd:PRK11147 311 EASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 GLQFDEQMKVIDVVQDIAEVIELgNGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:PRK11147 391 RAELDPEKTVMDNLAEGKQEVMV-NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 467 DLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQGDIRDFPGNYTRYRDwKDAKAAQEREKEKEAAKAQE 546
Cdd:PRK11147 470 DLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQ-QQAQYLALKQPAVKKKEEAA 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 547 EKTAKVRLNEKRRMSFKEKREFEQLEQDIAALEAEKQSIEEALCSGALSVDELTEKSKRLPELADL---IDEKTMRWLEL 623
Cdd:PRK11147 549 APKAETVKRSSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAeqeLEVAFERWEEL 628
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-523 |
5.19e-76 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 252.12 E-value: 5.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 12 NLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEELTVLEAC 91
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 92 FHHGNSTVELIKEYER------CMETDG-HPG-LDGILARMDHEKAweyEQKAKQILSQLKIrDFNQQVKSLS----GGQ 159
Cdd:PRK15064 86 IMGHTELWEVKQERDRiyalpeMSEEDGmKVAdLEVKFAEMDGYTA---EARAGELLLGVGI-PEEQHYGLMSevapGWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 160 LkRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNYSYY 239
Cdd:PRK15064 162 L-RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 240 LE---KREERIEA----KTVEIErannlyrtEL-EWMRRMpQARGHKARyredafyELEKVAKQRfnnDNVKLD-VKAS- 309
Cdd:PRK15064 241 MTaatQARERLLAdnakKKAQIA--------ELqSFVSRF-SANASKAK-------QATSRAKQI---DKIKLEeVKPSs 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 310 ----YI----GSKIF----EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGET 377
Cdd:PRK15064 302 rqnpFIrfeqDKKLHrnalEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 378 VRFGYYSQD-GLQFDEQMKVIDVvqdIAEVIELGNGKRLTASqFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNP 456
Cdd:PRK15064 382 ANIGYYAQDhAYDFENDLTLFDW---MSQWRQEGDDEQAVRG-TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 457 NFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQGdIRDFPGNYTRY 523
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-625 |
6.81e-76 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 254.71 E-value: 6.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 18 GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQD-PQYP-----------EEL 85
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQEtPALPqpaleyvidgdREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEACFHHGNStvelikeyercmETDGHpGLDGILARMDHEKAWEYEQKAKQILSQLKIRD--FNQQVKSLSGGQLKRV 163
Cdd:PRK10636 92 RQLEAQLHDANE------------RNDGH-AIATIHGKLDAIDAWTIRSRAASLLHGLGFSNeqLERPVSDFSGGWRMRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 164 ALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNYSYYLEKR 243
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 244 EERIEAKtveieraNNLYRTELEWMR---------RMPQARGHKARYREDAFYELEKVAKQRFNNDNVKLDVKASYIGSK 314
Cdd:PRK10636 239 ATRLAQQ-------QAMYESQQERVAhlqsyidrfRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGLQF---D 391
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFlraD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 392 EQmkvidVVQDIAEVIELGNGKRLtaSQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV 471
Cdd:PRK10636 392 ES-----PLQHLARLAPQELEQKL--RDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 472 TLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHL-LVFNGQgdIRDFPGNYTRYRDW-----KDAKAAQEREKEKEAAKAQ 545
Cdd:PRK10636 465 MRQALTEALIDFEGALVVVSHDRHLLRSTTDDLyLVHDGK--VEPFDGDLEDYQQWlsdvqKQENQTDEAPKENNANSAQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 546 EEKTAKVRLNEKRRMSFKEKREFEQLEQDIAALEAEKQSIEEALCSGAL----SVDELTEKSKRLPELADLIDEKTMRWL 621
Cdd:PRK10636 543 ARKDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELydqsRKAELTACLQQQASAKSGLEECEMAWL 622
|
....
gi 2524717128 622 ELSE 625
Cdd:PRK10636 623 EAQE 626
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-242 |
6.08e-61 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 211.46 E-value: 6.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQY-PEEL 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEElDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEacfhhgnstvELikeyercmeTDGHPGLDgilarmdhekaweyEQKAKQILSQLKIR--DFNQQVKSLSGGQLKRV 163
Cdd:COG0488 395 TVLD----------EL---------RDGAPGGT--------------EQEVRGYLGRFLFSgdDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 164 ALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNYSYYLEK 242
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
318-547 |
2.27e-56 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 199.14 E-value: 2.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 318 ADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDgLQFDEQMKVI 397
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 DVV-QDIAEVIEL---------------GNGKRLT-----------------ASQFLQHFLFTPETQHSYVYKLSGGERR 444
Cdd:COG0488 80 DTVlDGDAELRALeaeleeleaklaepdEDLERLAelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 445 RLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLL-VFNGQgdIRDFPGNYTRY 523
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILeLDRGK--LTLYPGNYSAY 237
|
250 260
....*....|....*....|....
gi 2524717128 524 RDWKDAKAAQErekEKEAAKAQEE 547
Cdd:COG0488 238 LEQRAERLEQE---AAAYAKQQKK 258
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-228 |
4.41e-53 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 178.41 E-value: 4.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQdpqypeeltv 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 88 leacfhhgnstvelikeyercmetdghpgldgilarmdhekaweyeqkakqilsqlkirdfnqqvksLSGGQLKRVALAN 167
Cdd:cd03221 71 -------------------------------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 168 TLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRR 228
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-522 |
3.93e-51 |
|
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: 184.72 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF--GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG---KEGYDSGTISFR-RDI-------- 70
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDgRDLlelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 --RVGYLEQDPqypeeLTVLeacfhhgnstvelikeyerCMETDGHPGLDGILAR-MDHEKAWEyeqKAKQILSQLKIRD 147
Cdd:COG1123 82 grRIGMVFQDP-----MTQL-------------------NPVTVGDQIAEALENLgLSRAEARA---RVLELLEAVGLER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 F-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:COG1123 135 RlDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 223 EIDNRRIyqykgnysyylekreerIEAKTVEIERANnlyRTELEWMRRMPQARGHKARYREDafyelekvakqrfnndnv 302
Cdd:COG1123 215 VMDDGRI-----------------VEDGPPEEILAA---PQALAAVPRLGAARGRAAPAAAA------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 303 kldvkasyiGSKIFEADHLYKSF-----GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GE 376
Cdd:COG1123 257 ---------AEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGK 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 TV-------------RFGYYSQD-GLQFDEQMKVIDVVQDIAEVIELGNGKRLT--ASQFLQHFLFTPETQHSYVYKLSG 440
Cdd:COG1123 328 DLtklsrrslrelrrRVQMVFQDpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRerVAELLERVGLPPDLADRYPHELSG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 441 GERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNG-----QG 511
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDgriveDG 487
|
570
....*....|....*
gi 2524717128 512 DIRDFPGN----YTR 522
Cdd:COG1123 488 PTEEVFANpqhpYTR 502
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
317-511 |
8.12e-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: 169.55 E-value: 8.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQdglqfdeqmkv 396
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 397 idvvqdiaevielgngkrltasqflqhflftpetqhsyvykLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVL 476
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 2524717128 477 EEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQG 511
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-524 |
1.01e-45 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 172.74 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLL---------------NILSGKE---GYDSGTIS--FR 67
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamhaidgipkncQILHVEQevvGDDTTALQcvLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RDI-RVGYLEQDPQYPEELTVLEACFHHGNSTVELIKEYERCMETDGhpgLDGILARMDHEKAWEYEQKAKQILSQLKIR 146
Cdd:PLN03073 258 TDIeRTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQR---LEEIYKRLELIDAYTAEARAASILAGLSFT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DFNQ--QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEI 224
Cdd:PLN03073 335 PEMQvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 225 DNRRIYQYKGNYSYYLEKREERIEAKTVEIErANNLYRTELEWM---RRMPQARGHKARYREDAFYELEKVaKQRFNNDN 301
Cdd:PLN03073 415 HGQKLVTYKGDYDTFERTREEQLKNQQKAFE-SNERSRSHMQAFidkFRYNAKRASLVQSRIKALDRLGHV-DAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 302 VKL-----DVKASyiGSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGE 376
Cdd:PLN03073 493 YKFefptpDDRPG--PPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 TVRFGYYSQ---DGLQFDEQmKVIDVVQDIAEVIElgngKRLTASqfLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLM 453
Cdd:PLN03073 571 KVRMAVFSQhhvDGLDLSSN-PLLYMMRCFPGVPE----QKLRAH--LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 454 RNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNgQGDIRDFPGNYTRYR 524
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHDYK 713
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
1.27e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAvNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------RRDIRVGY 74
Cdd:COG1121 1 MMM-MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQ----DPQYPeeLTVLEacfhhgnsTVElikeyercMETDGHPGLDGILARMDHEKAWEyeqkakqILSQLKIRDF-N 149
Cdd:COG1121 80 VPQraevDWDFP--ITVRD--------VVL--------MGRYGRRGLFRRPSRADREAVDE-------ALERVGLEDLaD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:COG1121 135 RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLLNR 214
|
....
gi 2524717128 227 RRIY 230
Cdd:COG1121 215 GLVA 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-230 |
6.04e-43 |
|
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: 154.82 E-value: 6.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDI--RVGYL 75
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEacfhhgnsTVELikeyercmetdG---HPGLDGILARMDHEKAWEyeqkakqILSQLKIRDF-NQQ 151
Cdd:COG1120 81 PQEPPAPFGLTVRE--------LVAL-----------GrypHLGLFGRPSAEDREAVEE-------ALERTGLEHLaDRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDryfLD---RVCSEIIEI 224
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLVLL 211
|
....*.
gi 2524717128 225 DNRRIY 230
Cdd:COG1120 212 KDGRIV 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-229 |
3.24e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.75 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDIR--VGYLEQ 77
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEELTVLEacfhhgnsTVELIkeyercmetdghpgldgilARMDHEKAWEYEQKAKQILSQLKIRDF-NQQVKSLS 156
Cdd:COG1131 81 EPALYPDLTVRE--------NLRFF-------------------ARLYGLPRKEARERIDELLELFGLTDAaDRKVGTLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:COG1131 134 GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRElaaEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-254 |
4.01e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 143.84 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS------------FRRDIrvGYL 75
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepreARRQI--GVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLeacfhhgnstvELIKEYERcmetdghpgldgiLARMDHEkawEYEQKAKQILSQLKIRDF-NQQVKS 154
Cdd:COG4555 80 PDERGLYDRLTVR-----------ENIRYFAE-------------LYGLFDE---ELKKRIEELIELLGLEEFlDRRVGE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVCSEIIEIDNRRIyQ 231
Cdd:COG4555 133 LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlkkEGKTVLFSSHIMQEVEALCDRVVILHKGKV-V 211
|
250 260
....*....|....*....|....
gi 2524717128 232 YKGNYSYYLEKR-EERIEAKTVEI 254
Cdd:COG4555 212 AQGSLDELREEIgEENLEDAFVAL 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-256 |
1.55e-38 |
|
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: 149.70 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPqypEE 84
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR---DA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 LTvleacfhhGNSTV-ELIkeyercmeTDGHpgldgilarmDHEKAWEYEQKAKQILSQLKIRDFNQQ--VKSLSGGQLK 161
Cdd:TIGR03719 397 LD--------PNKTVwEEI--------SGGL----------DIIKLGKREIPSRAYVGRFNFKGSDQQkkVGQLSGGERN 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 162 RVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII--EIDNRrIYQYKGNYSYY 239
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILafEGDSH-VEWFEGNFSEY 529
|
250
....*....|....*..
gi 2524717128 240 LEKREERIEAKTVEIER 256
Cdd:TIGR03719 530 EEDKKRRLGEDADQPHR 546
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-228 |
5.88e-38 |
|
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: 139.54 E-value: 5.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI---------RVGYLEQ 77
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgEPIrdaredyrrRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEELTVLEA-CFHHgnstvelikeyercmetdghpGLDGilARMDHEKAWEyeqkakqILSQLKIRDF-NQQVKSL 155
Cdd:COG4133 83 ADGLKPELTVRENlRFWA---------------------ALYG--LRADREAIDE-------ALEAVGLAGLaDLPVRQL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVcsEIIEIDNRR 228
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhlaRGGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-231 |
2.38e-37 |
|
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: 138.05 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------RRDIRVGYLEQ----D 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQrrsiD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPeeLTVLEacfhhgnsTVelikeyerCMETDGHPGLDGILARmdhekawEYEQKAKQILSQLKIRDF-NQQVKSLSG 157
Cdd:cd03235 81 RDFP--ISVRD--------VV--------LMGLYGHKGLFRRLSK-------ADKAKVDEALERVGLSELaDRQIGELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQ 231
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-229 |
8.98e-37 |
|
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: 136.85 E-value: 8.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI----------------SFR 67
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RDiRVGYLEQDPQYPEELTVLEacfhhgNstVELIkeyercmetdghpgldgilARMDHEKAWEYEQKAKQILSQLKIRD 147
Cdd:cd03255 81 RR-HIGFVFQSFNLLPDLTALE------N--VELP-------------------LLLAGVPKKERRERAEELLERVGLGD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 F-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNLTLLMVTHDRYFLDRvCSEII 222
Cdd:cd03255 133 RlNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkeVMELLRELNKEAGTTIVVVTHDPELAEY-ADRII 211
|
....*..
gi 2524717128 223 EIDNRRI 229
Cdd:cd03255 212 ELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-229 |
9.49e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 9.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI----------RVGYLE 76
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgKPLsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 QDPQYPEEltvleacfhhgnsTVElikeyercmetdghpgldgilarmDH-EKAWEY------EQKAKQILSQLKIRD-- 147
Cdd:COG4619 81 QEPALWGG-------------TVR------------------------DNlPFPFQLrerkfdRERALELLERLGLPPdi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT----EWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIE 223
Cdd:COG4619 124 LDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTrrveELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 2524717128 224 IDNRRI 229
Cdd:COG4619 204 LEAGRL 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
2.74e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------RRDI 70
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQDPQ-YPeELTVLEacfhhgNstVELikeyercmetdghpGLDgiLARMDHEkawEYEQKAKQILSQLKIRDF- 148
Cdd:COG1116 81 DRGVVFQEPAlLP-WLTVLD------N--VAL--------------GLE--LRGVPKA---ERRERARELLELVGLAGFe 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRY---FL-DRVC-- 218
Cdd:COG1116 133 DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHDVDeavFLaDRVVvl 212
|
250
....*....|....
gi 2524717128 219 -------SEIIEID 225
Cdd:COG1116 213 sarpgriVEEIDVD 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-229 |
4.03e-36 |
|
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: 133.29 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDIR--VGYLEQ 77
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkePEEVKrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEELTVLEacfhhgnstvelikeyercmetdghpgldgilarmdhekaweyeqkakqilsQLKirdfnqqvksLSG 157
Cdd:cd03230 81 EPSLYENLTVRE----------------------------------------------------NLK----------LSG 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR---RTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03230 99 GMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRelkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-229 |
3.80e-35 |
|
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: 132.46 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR--VGYL 75
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditkknLRELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDP--QYpeeltvleacFhhgNSTVElikeyercmetdghpglDGI---LARMDHEKAwEYEQKAKQILSQLKIRDF-N 149
Cdd:COG1122 81 FQNPddQL----------F---APTVE-----------------EDVafgPENLGLPRE-EIRERVEEALELVGLEHLaD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlnkEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
...
gi 2524717128 227 RRI 229
Cdd:COG1122 210 GRI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-229 |
5.97e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 5.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS--------------- 65
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 66 -FRRDiRVGYLEQDPQYPEELTVLEacfhhgNstVELikeyercmetdghPGLdgiLARMDHEKAweyEQKAKQILSQLK 144
Cdd:COG1136 82 rLRRR-HIGFVFQFFNLLPELTALE------N--VAL-------------PLL---LAGVSRKER---RERARELLERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 145 IRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRTNLTLLMVTHDRYFLDR 216
Cdd:COG1136 134 LGDRlDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDPELAAR 210
|
250
....*....|...
gi 2524717128 217 vCSEIIEIDNRRI 229
Cdd:COG1136 211 -ADRVIRLRDGRI 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-228 |
6.65e-35 |
|
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: 131.05 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSFGDL--VLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-RRDI----------RVGYL 75
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLtklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPqypE----ELTVL-EACFHhgnstvelikeyercMETDGhpgldgilarMDHEKAweyEQKAKQILSQLKIRDF-N 149
Cdd:cd03225 81 FQNP---DdqffGPTVEeEVAFG---------------LENLG----------LPEEEI---EERVEEALELVGLEGLrD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDyLRRTNLTLLMVTHDRYFLDRVCSEIIEID 225
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPagrrELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
...
gi 2524717128 226 NRR 228
Cdd:cd03225 209 DGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-210 |
7.03e-35 |
|
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: 131.44 E-value: 7.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------RRDIRVGYLEQ 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEELTVLEacfhhgNstVELikeyercmetdghpGLDgiLARMDHEKAweyEQKAKQILSQLKIRDF-NQQVKSLS 156
Cdd:cd03293 81 QDALLPWLTVLD------N--VAL--------------GLE--LQGVPKAEA---RERAEELLELVGLSGFeNAYPHQLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-510 |
1.53e-34 |
|
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: 138.76 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 28 FGL---SEGQRVGLIAKNGSGKSTLLNILSG-----------KEGYD------SGTI---SFRR----DIRVGYleqDPQ 80
Cdd:COG1245 91 YGLpvpKKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeEPSWDevlkrfRGTElqdYFKKlangEIKVAH---KPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 YpeeltvleacfhhgnstVELIKEYercmetdghpgLDG----ILARMDHEKaweyeqKAKQILSQLKIRDF-NQQVKSL 155
Cdd:COG1245 168 Y-----------------VDLIPKV-----------FKGtvreLLEKVDERG------KLDELAEKLGLENIlDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDyLRRTNLTLLMVTHDRYFLDRVcSEIIEIdnrrIYQ 231
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRE-LAEEGKYVLVVEHDLAILDYL-ADYVHI----LYG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 232 YKGNY-------------SYYLEK--REERIeaktveierannlyrtelewmrrmpqarghkaRYREDAFyELEKVAKQR 296
Cdd:COG1245 288 EPGVYgvvskpksvrvgiNQYLDGylPEENV--------------------------------RIRDEPI-EFEVHAPRR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 297 FNNdnvkldvkasyiGSKIFEADHLYKSFGDLKILDDFSYIFaRYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDigE 376
Cdd:COG1245 335 EKE------------EETLVEYPDLTKSYGGFSLEVEGGEIR-EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--E 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 TVRFGYYSQDgLQFDEQMKVIDVVQDIaevielgNGKRLTASqFLQHFLFTPETQH----SYVYKLSGGERRRLYLCTVL 452
Cdd:COG1245 400 DLKISYKPQY-ISPDYDGTVEEFLRSA-------NTDDFGSS-YYKTEIIKPLGLEklldKNVKDLSGGELQRVAIAACL 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 453 MRNPNFLVLDEPTNDLD----IVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQ 510
Cdd:COG1245 471 SRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGE 532
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-229 |
3.03e-34 |
|
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: 130.69 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG----DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR--V 72
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrRKAFRrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPqypeeltvlEACFH--HgnsTV-ELIKEYERCMetdghpGLDGILARMDhekaweyeqkakQILSQL----KI 145
Cdd:COG1124 82 QMVFQDP---------YASLHprH---TVdRILAEPLRIH------GLPDREERIA------------ELLEQVglppSF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 146 RD-FNQQvksLSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRTNLTLLMVTHDRYFLDRV 217
Cdd:COG1124 132 LDrYPHQ---LSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqaeiLNL---LKDLREERGLTYLFVSHDLAVVAHL 205
|
250
....*....|..
gi 2524717128 218 CSEIIEIDNRRI 229
Cdd:COG1124 206 CDRVAVMQNGRI 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-243 |
3.48e-34 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 136.95 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDP--QYPEEL 85
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHayDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEacfhhgnstveLIKEYERcmETDGHPGLDGILARMdhekaweyeqkakqILSQlkiRDFNQQVKSLSGGQLKRVAL 165
Cdd:PRK15064 400 TLFD-----------WMSQWRQ--EGDDEQAVRGTLGRL--------------LFSQ---DDIKKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 166 ANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNYSYYLEKR 243
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-222 |
3.58e-34 |
|
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: 129.86 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR-----------VGYL 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDITglppheiarlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLE----ACFHHGNSTVelikeyercmetdghpgldgILARMDHEKAwEYEQKAKQILSQLKIRDF-NQ 150
Cdd:cd03219 81 FQIPRLFPELTVLEnvmvAAQARTGSGL--------------------LLARARREER-EARERAEELLERVGLADLaDR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN---LTLLMVTHDRYFLDRVCSEII 222
Cdd:cd03219 140 PAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRergITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-232 |
2.08e-33 |
|
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: 126.01 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFrrdirvgyleqdpqypeeltvl 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 89 eacfhhgnstvelikeyercmetDGHPgldgiLARMDHEkaweyeQKAK------QILSQLKIRDF-NQQVKSLSGGQLK 161
Cdd:cd03214 59 -----------------------DGKD-----LASLSPK------ELARkiayvpQALELLGLAHLaDRPFNELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 162 RVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDryfLD---RVCSEIIEIDNRRIYQY 232
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNlaaRYADRVILLKDGRIVAQ 179
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
315-585 |
2.36e-33 |
|
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: 134.68 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSF-GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGlQFDEQ 393
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEP-QLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 394 MKVIDVVQD-----------------------------------IAEVIELGNGKRLtASQFLQ--HFLFTPETQHSyVY 436
Cdd:TIGR03719 83 KTVRENVEEgvaeikdaldrfneisakyaepdadfdklaaeqaeLQEIIDAADAWDL-DSQLEIamDALRCPPWDAD-VT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 437 KLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFN-GQGdird 515
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDrGRG---- 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 516 FP--GNYTRYRDWKDAKAAQEREKEKEAAKAQEEKTAKVRLNEKRRMSfKEK---REFEQLEQDIAALEAEKQSI 585
Cdd:TIGR03719 237 IPweGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQA-KSKarlARYEELLSQEFQKRNETAEI 310
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-246 |
5.74e-33 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 133.71 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQ-----DP 79
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQsrdalDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 qypeeltvleacfhhgNSTV-ELIKEyercmetdghpGLDGIlarmdheKAWEYEQKAKQILSQlkirdFN-----QQ-- 151
Cdd:PRK11819 402 ----------------NKTVwEEISG-----------GLDII-------KVGNREIPSRAYVGR-----FNfkggdQQkk 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII--EiDNRRI 229
Cdd:PRK11819 443 VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILafE-GDSQV 521
|
250
....*....|....*..
gi 2524717128 230 YQYKGNYSYYLEKREER 246
Cdd:PRK11819 522 EWFEGNFQEYEEDKKRR 538
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-183 |
6.56e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 123.53 E-value: 6.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 23 FENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI----------RVGYLEQDPQYPEELTVLEAc 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgQDLtdderkslrkEIGYVFQDPQLFPRLTVREN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 92 fhhgnstvelIKEYERCMETDGHpgldgilarmdhekawEYEQKAKQILSQLKIRDFN-----QQVKSLSGGQLKRVALA 166
Cdd:pfam00005 80 ----------LRLGLLLKGLSKR----------------EKDARAEEALEKLGLGDLAdrpvgERPGTLSGGQRQRVAIA 133
|
170
....*....|....*..
gi 2524717128 167 NTLITEPDLLILDEPTN 183
Cdd:pfam00005 134 RALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-211 |
8.50e-33 |
|
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: 125.32 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-----------RRDIrvGYLE 76
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppeRRNI--GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 QDPQ-YPEeLTVLE-ACFhhgnstvelikeyercmetdghpGLDgiLARMDHEKAweyEQKAKQILSQLKIRDF-NQQVK 153
Cdd:cd03259 79 QDYAlFPH-LTVAEnIAF-----------------------GLK--LRGVPKAEI---RARVRELLELVGLEGLlNRYPH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHDR 211
Cdd:cd03259 130 ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQ 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-510 |
1.28e-32 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 133.01 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 28 FGL---SEGQRVGLIAKNGSGKSTLLNILSG-----------KEGYD------SGTI---SFRR----DIRVGyleQDPQ 80
Cdd:PRK13409 91 YGLpipKEGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeEPSWDevlkrfRGTElqnYFKKlyngEIKVV---HKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 YpeeltvleacfhhgnstVELIKEYercmetdghpgLDG----ILARMDHEKAWEyeqkakQILSQLKIRDF-NQQVKSL 155
Cdd:PRK13409 168 Y-----------------VDLIPKV-----------FKGkvreLLKKVDERGKLD------EVVERLGLENIlDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRrtNLTLLMVTHDRYFLDRVcSEIIEIdnrrIYQ 231
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRELAE--GKYVLVVEHDLAVLDYL-ADNVHI----AYG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 232 YKGNY-------------SYYLEK--REE--RIEaktveierannlyRTELEWMRRMPQARGHKARYREdaFYELEKvak 294
Cdd:PRK13409 287 EPGAYgvvskpkgvrvgiNEYLKGylPEEnmRIR-------------PEPIEFEERPPRDESERETLVE--YPDLTK--- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 295 qrfNNDNVKLDVKASYIgskifeadhlYKSfgdlkilddfsyifaryEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI 374
Cdd:PRK13409 349 ---KLGDFSLEVEGGEI----------YEG-----------------EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 375 geTVRFGYYSQDgLQFDEQMKVIDVVQDIAEVIElgngkrltaSQFLQHFLFTPETQH----SYVYKLSGGERRRLYLCT 450
Cdd:PRK13409 399 --ELKISYKPQY-IKPDYDGTVEDLLRSITDDLG---------SSYYKSEIIKPLQLErlldKNVKDLSGGELQRVAIAA 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 451 VLMRNPNFLVLDEPTNDLD----IVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQ 510
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-228 |
1.89e-32 |
|
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: 122.35 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFrrdirvgyleqdpqypeeltvl 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 89 eacfhhgnstvelikeyercmetDGHPGLDgilarmdhekaweyeqkakqiLSQLKIRDFNQQVKSLSGGQLKRVALANT 168
Cdd:cd00267 59 -----------------------DGKDIAK---------------------LPLEELRRRIGYVPQLSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 169 LITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVCSEIIEIDNRR 228
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRElaeEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-502 |
1.95e-31 |
|
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: 128.77 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGY--DSGTISFRRDI--RVGYLE------- 76
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHVALceKCGYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 QDPQYPEELTVLEACFH------------------------HGNSTVelIKEYERCMETDGHPGLDGIlarmdhekawey 132
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWnlsdklrrrirkriaimlqrtfalYGDDTV--LDNVLEALEEIGYEGKEAV------------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 133 eQKAKQILSQLKIRDFNQQV-KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMV 207
Cdd:TIGR03269 147 -GRAVDLIEMVQLSHRITHIaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 208 THDRYFLDRVCSEIIEIDNRRIYQyKGNYSYYLEKREERIEA--KTVEIERANNLYRTelewmrrmpqaRGHKARYreda 285
Cdd:TIGR03269 226 SHWPEVIEDLSDKAIWLENGEIKE-EGTPDEVVAVFMEGVSEveKECEVEVGEPIIKV-----------RNVSKRY---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 286 fYELEK-VAKQRfnnDNVKLDVKASyigskifeadhlyksfgdlkilddfsyifaryEKMGIVGNNGTGKSTFIKILMR- 363
Cdd:TIGR03269 290 -ISVDRgVVKAV---DNVSLEVKEG--------------------------------EIFGIVGTSGAGKTTLSKIIAGv 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 364 ----------------HEQADRGALDIGETVRF-GYYSQDGLQFDEQmkviDVVQDIAEVI------ELGngkRLTASQF 420
Cdd:TIGR03269 334 leptsgevnvrvgdewVDMTKPGPDGRGRAKRYiGILHQEYDLYPHR----TVLDNLTEAIglelpdELA---RMKAVIT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 421 LQHFLFTPETQHS----YVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT--------LNVLEEYLRNFkgcvI 488
Cdd:TIGR03269 407 LKMVGFDEEKAEEildkYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITkvdvthsiLKAREEMEQTF----I 482
|
570
....*....|....
gi 2524717128 489 VVSHDRYFMDKVVD 502
Cdd:TIGR03269 483 IVSHDMDFVLDVCD 496
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-224 |
1.30e-30 |
|
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: 119.53 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI----------- 70
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgKDLlklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 --RVGYLEQD------PQYPEELTVLEACFHHGNSTVELIKEYERCMETDGHPGLDGILARMDHEkaweyeqkakqilsq 142
Cdd:cd03257 81 rkEIQMVFQDpmsslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 143 lkirdfnqqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRTNLTLLMVTHD----R 211
Cdd:cd03257 146 ------------LSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDL---LKKLQEELGLTLLFITHDlgvvA 210
|
250
....*....|....*..
gi 2524717128 212 YFLDRV----CSEIIEI 224
Cdd:cd03257 211 KIADRVavmyAGKIVEE 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-211 |
1.78e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.90 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAvnSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI--------R 71
Cdd:COG3842 1 MAM--PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgRDVtglppekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQD----PQypeeLTVLEacfhhgNstVElikeYercmetdghpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRD 147
Cdd:COG3842 79 VGMVFQDyalfPH----LTVAE------N--VA----F----------GL-----RMRGVPKAEIRARVAELLELVGLEG 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 148 F-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDR 211
Cdd:COG3842 128 LaDRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHDQ 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-231 |
3.28e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.79 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR----------RDIRVGYLEQ 77
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlppRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPqypeeltvleACFHHgnSTVElikeyercmetdghpglDGI---LARMDHEKAwEYEQKAKQILSQLKIRDF-----N 149
Cdd:COG1118 83 HY----------ALFPH--MTVA-----------------ENIafgLRVRPPSKA-EIRARVEELLELVQLEGLadrypS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDR---YfldRVCSEII 222
Cdd:COG1118 133 Q----LSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQeeaL---ELADRVV 205
|
....*....
gi 2524717128 223 EIDNRRIYQ 231
Cdd:COG1118 206 VMNQGRIEQ 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-217 |
7.65e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 118.24 E-value: 7.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------------RRDIR- 71
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdgqdvtalrgraLRRLRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 -VGYLEQDPQYPEELTVLEA----CFHHgnstvelikeyercmetdgHPGLDGILARMDHEkawEYeQKAKQILSQLKIR 146
Cdd:COG3638 81 rIGMIFQQFNLVPRLSVLTNvlagRLGR-------------------TSTWRSLLGLFPPE---DR-ERALEALERVGLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHD-----RYFlDR 216
Cdd:COG3638 138 DKaYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAredgITVVVNLHQvdlarRYA-DR 216
|
.
gi 2524717128 217 V 217
Cdd:COG3638 217 I 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-226 |
1.00e-29 |
|
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: 115.75 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI------------RVGY 74
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLtdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEACfhhgnstvelikeyercmetdGHPgldgilarmdhekaweyeqkakqilsqlkirdfnqqvks 154
Cdd:cd03229 81 VFQDFALFPHLTVLENI---------------------ALG--------------------------------------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR----RTNLTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
315-588 |
1.37e-29 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 123.31 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFG-DLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKIL--MRHE-----QADRGA----------LDIGE 376
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagVDKEfegeaRPAPGIkvgylpqepqLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 TVR--------------------FGYYSQDGLQFDEQMKVIDVVQDIaevIELGNGKRLTaSQFLQ--HFLFTPETQHSy 434
Cdd:PRK11819 86 TVRenveegvaevkaaldrfneiYAAYAEPDADFDALAAEQGELQEI---IDAADAWDLD-SQLEIamDALRCPPWDAK- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 435 VYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLL-VFNGQGdi 513
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILeLDRGRG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 514 rdFP--GNYTRYRDWKDAKAAQEREKEKEAAKAQEEKTAKVRLNEKRRMSfKEK---REFEQLEQdiaalEAEKQSIEEA 588
Cdd:PRK11819 239 --IPweGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQA-KSKarlARYEELLS-----EEYQKRNETN 310
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-230 |
1.63e-29 |
|
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: 116.90 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLV-LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR-----V 72
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinklkGKALRqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPQYPEELTVLEACFHhgnstvelikeyercmetdghpgldGILARMDHEKAW------EYEQKAKQILSQLKIR 146
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLS-------------------------GRLGRRSTWRSLfglfpkEEKQRALAALERVGLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHD----RYFLDRV 217
Cdd:cd03256 136 DKaYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreegITVIVSLHQvdlaREYADRI 215
|
250 260
....*....|....*....|....*.
gi 2524717128 218 -------------CSEIIEIDNRRIY 230
Cdd:cd03256 216 vglkdgrivfdgpPAELTDEVLDEIY 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
317-508 |
3.47e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 113.65 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIgetvrFGYYSQDglQFDEQMKV 396
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----LGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 397 IDVVQDIAEVIElgngkRLTASQFLqhflftpetqhsyvyKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVL 476
Cdd:cd03230 75 IGYLPEEPSLYE-----NLTVRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*
gi 2524717128 477 EEYLRNFK--GC-VIVVSHDRYFMDKVVDHLLVFN 508
Cdd:cd03230 135 WELLRELKkeGKtILLSSHILEEAERLCDRVAILN 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-229 |
4.98e-28 |
|
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: 111.85 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDI-----RVGY 74
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkltddKKNInelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEacfhhgNSTVELIKeyercmetdghpgldgiLARMDHEKAweyEQKAKQILSQLKIRDF-NQQVK 153
Cdd:cd03262 81 VFQQFNLFPHLTVLE------NITLAPIK-----------------VKGMSKAEA---EERALELLEKVGLADKaDAYPA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR---RTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKdlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-229 |
1.33e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.44 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI-------------RVG 73
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPQYPEELTVLEacfhhgNstVEL-IKEYERCMEtdghpgldgilarmdhekaWEYEQKAKQILSQLKIRDFNQQV 152
Cdd:cd03261 81 MLFQSGALFDSLTVFE------N--VAFpLREHTRLSE-------------------EEIREIVLEKLEAVGLRGAEDLY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHDRYFLDRVCSEIIEIDNR 227
Cdd:cd03261 134 PAeLSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkelgLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
..
gi 2524717128 228 RI 229
Cdd:cd03261 214 KI 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-229 |
2.31e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 110.85 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDI-----RVG 73
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedltdsKKDInklrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQD----PQypeeLTVLEacfhhgNSTVELIKeyercmetdghpgldgiLARMDHEKAweyEQKAKQILSQLKIRDF- 148
Cdd:COG1126 81 MVFQQfnlfPH----LTVLE------NVTLAPIK-----------------VKKMSKAEA---EERAMELLERVGLADKa 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LD-MTEwledyLRRTNLTLLMVTHDRYFLDRVCSE 220
Cdd:COG1126 131 DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevLDvMRD-----LAKEGMTMVVVTHEMGFAREVADR 205
|
....*....
gi 2524717128 221 IIEIDNRRI 229
Cdd:COG1126 206 VVFMDGGRI 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-229 |
4.95e-27 |
|
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: 108.84 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDI---------RVGYLEQD 78
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEELTVLEacfHHGNSTVELIKEYERCMETDGHPGLDGIlarmDHEKaweyeqkakqilsqlkirdfnqqVKSLSGG 158
Cdd:cd03268 81 PGFYPNLTARE---NLRLLARLLGIRKKRIDEVLDVVGLKDS----AKKK-----------------------VKGFSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 159 QLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-231 |
1.68e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.92 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLfeNISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIrvgyleqDPQYPEELT 86
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQDL-------TALPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 V--------LeacFHHgnSTVE------LikeyercmetdgHPGLDgiLARMDHekaweyeQKAKQILSQLKIRDFNQQV 152
Cdd:COG3840 73 VsmlfqennL---FPH--LTVAqniglgL------------RPGLK--LTAEQR-------AQVEQALERVGLAGLLDRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KS-LSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfLD---RVCSEIIEI 224
Cdd:COG3840 127 PGqLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVLLV 203
|
....*..
gi 2524717128 225 DNRRIYQ 231
Cdd:COG3840 204 ADGRIAA 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-209 |
1.84e-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: 108.63 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKE-----------GYDSGTISFrRDIR-- 71
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygndvrlfGERRGGEDV-WELRkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYL--EQDPQYPEELTVLEAC---FHhgnSTVELikeYERCMETDghpgldgilarmdhekaweyEQKAKQILSQLKIR 146
Cdd:COG1119 80 IGLVspALQLRFPRDETVLDVVlsgFF---DSIGL---YREPTDEQ--------------------RERARELLELLGLA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 147 DF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTH 209
Cdd:COG1119 134 HLaDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-231 |
2.87e-26 |
|
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: 107.77 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFG-DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR----- 71
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLegtditklrGKKLRklrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQDPQYPEELTVLEACFHHGNSTvelikeyercmetdgHPGLDGILARM-DHEKaweyeQKAKQILSQLKIRDF-N 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGY---------------KPTWRSLLGRFsEEDK-----ERALSALERVGLADKaY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHD----RYFLDRVC--- 218
Cdd:TIGR02315 141 QRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkedgITVIINLHQvdlaKKYADRIVglk 220
|
250 260
....*....|....*....|...
gi 2524717128 219 -SEII------EIDN---RRIYQ 231
Cdd:TIGR02315 221 aGEIVfdgapsELDDevlRHIYG 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-473 |
3.06e-26 |
|
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: 112.86 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKS----TLLNILSGKEGYDSGTISFR---------- 67
Cdd:COG4172 5 PLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgqdllglser 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 --RDIR---VGYLEQDPqypeeLTVLEACFHHGNSTVELIKEyercmetdgHPGLDGILARmdhekaweyeQKAKQILSQ 142
Cdd:COG4172 85 elRRIRgnrIAMIFQEP-----MTSLNPLHTIGKQIAEVLRL---------HRGLSGAAAR----------ARALELLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 143 LKIRDFNQQVKS----LSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRTNLTLLMVTHD- 210
Cdd:COG4172 141 VGIPDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqiLDL---LKDLQRELGMALLLITHDl 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 211 ---RYFLDRVC----SEIIEidnrriyqykgnysyylekreeriEAKTVEIERAnnlyrtelewmrrmPQA--------- 274
Cdd:COG4172 218 gvvRRFADRVAvmrqGEIVE------------------------QGPTAELFAA--------------PQHpytrkllaa 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 275 --RGHKARYREDAfyelEKVAKQRfnndnvklDVKASYIGSKIFeadhLYKSFGDLKILDDFSYIFARYEKMGIVGNNGT 352
Cdd:COG4172 260 epRGDPRPVPPDA----PPLLEAR--------DLKVWFPIKRGL----FRRTVGHVKAVDGVSLTLRRGETLGLVGESGS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 353 GKSTFIKILMRHEQADrgaldiGEtVRFGYYSQDGLQFDE------QMKVidVVQD----------IAEVIELG---NGK 413
Cdd:COG4172 324 GKSTLGLALLRLIPSE------GE-IRFDGQDLDGLSRRAlrplrrRMQV--VFQDpfgslsprmtVGQIIAEGlrvHGP 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 414 RLTASQFLQHFLFT-------PETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD------IVTL 473
Cdd:COG4172 395 GLSAAERRARVAEAleevgldPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqILDL 467
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-221 |
3.39e-26 |
|
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: 106.82 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD---LVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR---------VGY 74
Cdd:cd03263 1 LQIRNLTKTYKKgtkPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgYSIRtdrkaarqsLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEacfhhgnstvelikeyerCMEtdghpgldgILARMDHEKAWEYEQKAKQILSQLKIRDF-NQQVK 153
Cdd:cd03263 80 CPQFDALFDELTVRE------------------HLR---------FYARLKGLPKSEIKEEVELLLRVLGLTDKaNKRAR 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR--RTNLTLLMVTHDRYFLDRVCSEI 221
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILevRKGRSIILTTHSMDEAEALCDRI 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-229 |
3.93e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.66 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------RRDI-RVGYLeqdp 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldPEDRrRIGYL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 qyPEE------LTVLEACFHhgnstvelikeyercmetdghpgldgiLAR---MDHEKAweyEQKAKQILSQLKIRDF-N 149
Cdd:COG4152 77 --PEErglypkMKVGEQLVY---------------------------LARlkgLSKAEA---KRRADEWLERLGLGDRaN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLED---YLRRTNLTLLMVTHDryfLD---RVCSEIIE 223
Cdd:COG4152 125 KKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDvirELAAKGTTVIFSSHQ---MElveELCDRIVI 201
|
....*.
gi 2524717128 224 IDNRRI 229
Cdd:COG4152 202 INKGRK 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-226 |
4.03e-26 |
|
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: 106.19 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSFGDLV-LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDIRVGYLEQDP 79
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYpeeltvleacfHHGNSTV--ELIkeyercmetdghPGLDGilarmdhekAWEYEQKAKQILSQLKIRDF-NQQVKSLS 156
Cdd:cd03226 81 DY-----------QLFTDSVreELL------------LGLKE---------LDAGNEQAETVLKDLDLYALkERHPLSLS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDyLRRTNLTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:cd03226 129 GGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-229 |
5.96e-26 |
|
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: 106.60 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------------RRDIR--V 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqditglsekeLYELRrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQ-----DpqypeELTVLEacfhhgNstVEL-IKEyercmetdgHPGLDgilarmdhekAWEYEQKAKQILSQLKIR 146
Cdd:COG1127 85 GMLFQggalfD-----SLTVFE------N--VAFpLRE---------HTDLS----------EAEIRELVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DFNQQVKS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHDRYFLDRVCSEI 221
Cdd:COG1127 133 GAADKMPSeLSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdelgLTSVVVTHDLDSAFAIADRV 212
|
....*...
gi 2524717128 222 IEIDNRRI 229
Cdd:COG1127 213 AVLADGKI 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-229 |
8.41e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.90 E-value: 8.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKE----------GYDSGTISfRRDI----- 70
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErptsgqvlvnGQDLSRLK-RREIpylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQDPQYPEELTVLEacfhhgNstVELIkeyercMETDGHPgldgilarmdhEKawEYEQKAKQILSQLKIRDF-N 149
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYE------N--VALP------LRVTGKS-----------RK--EIRRRVREVLDLVGLSDKaK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL---TLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:COG2884 133 ALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrgtTVLIATHDLELVDRMPKRVLELED 212
|
...
gi 2524717128 227 RRI 229
Cdd:COG2884 213 GRL 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-210 |
1.51e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 16 SFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQ----DPQYPeeLTVLEAc 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevPDSLP--LTVRDL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 92 fhhgnstVElikeyercMETDGHPGLDGILARMDHekaweyeQKAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLI 170
Cdd:NF040873 78 -------VA--------MGRWARRGLWRRLTRDDR-------AAVDDALERVGLADLaGRQLGELSGGQRQRALLAQGLA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524717128 171 TEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHD 210
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEehaRGATVVVVTHD 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
317-509 |
1.87e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.15 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV---------RFGYYSQD 386
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 gLQFDEQMKVIDVVQDIAEVIELGNGKRLT-ASQFLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:COG1131 82 -PALYPDLTVRENLRFFARLYGLPRKEARErIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 466 NDLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVVDHLLVFNG 509
Cdd:COG1131 160 SGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-234 |
2.73e-25 |
|
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: 103.81 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQrVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDIR--VGYLEQ 77
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqPQKLRrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEELTVLEAcfhhgnstvelikeyercmetdghpgLD--GILARMDHEKAweyEQKAKQILSQLKIRDF-NQQVKS 154
Cdd:cd03264 80 EFGVYPNFTVREF--------------------------LDyiAWLKGIPSKEV---KARVDEVLELVNLGDRaKKKIGS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHDRYFLDRVCSEIIEIDNRRIyQY 232
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKL-VF 209
|
..
gi 2524717128 233 KG 234
Cdd:cd03264 210 EG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-229 |
4.05e-25 |
|
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: 104.05 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 2 AAVNSILQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS------------ 65
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfalded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 66 ----FRRDiRVGYLEQDPQYPEELTVLEacfhhgNSTVELikeyercmETDGHPGldgilARmdhekaweyeQKAKQILs 141
Cdd:COG4181 83 ararLRAR-HVGFVFQSFQLLPTLTALE------NVMLPL--------ELAGRRD-----AR----------ARARALL- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 142 qlkirdfnQQV----------KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNLTLLMV 207
Cdd:COG4181 132 --------ERVglghrldhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAtgeqIIDLLFELNRERGTTLVLV 203
|
250 260
....*....|....*....|..
gi 2524717128 208 THDRYFLDRvCSEIIEIDNRRI 229
Cdd:COG4181 204 THDPALAAR-CDRVLRLRAGRL 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-224 |
4.12e-25 |
|
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: 106.29 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG---KEGYDSGTISFR------------ 67
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDgedllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RDIR---VGYLEQDPqypeeLTVLEACFhhgnsTV-ELIKEyercmetdghpgldGILARMDHEKAwEYEQKAKQILSQL 143
Cdd:COG0444 81 RKIRgreIQMIFQDP-----MTSLNPVM-----TVgDQIAE--------------PLRIHGGLSKA-EARERAIELLERV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 144 KIRDFNQQVKS----LSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRTNLTLLMVTHD-- 210
Cdd:COG0444 136 GLPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLNL---LKDLQRELGLAILFITHDlg 212
|
250 260
....*....|....*....|
gi 2524717128 211 --RYFLDRV----CSEIIEI 224
Cdd:COG0444 213 vvAEIADRVavmyAGRIVEE 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-229 |
8.85e-25 |
|
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: 102.83 E-value: 8.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNIL-------SGK---EGYD--SGTISFRRdiRVGYL 75
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLttllkptSGRatvAGHDvvREPREVRR--RIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEACFHHGnstveliKEYercmetdGHPGLdgilarmdhekawEYEQKAKQILSQLKIRDF-NQQVKS 154
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHA-------RLY-------GVPGA-------------ERRERIDELLDFVGLLEAaDRLVKT 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDpqtrAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-235 |
9.23e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.94 E-value: 9.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR---------RDIRVGYLEQd 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhaRDRKVGFVFQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 pQYpeeltvleACFHHgnSTVelikeyercmetdghpgLDGI------LARMDHEKAWEYEQKAKQILSQLKIRDFNQQV 152
Cdd:PRK10851 82 -HY--------ALFRH--MTV-----------------FDNIafgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHDRyfldrvcSEIIEIDNR 227
Cdd:PRK10851 134 PAqLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHeelkFTSVFVTHDQ-------EEAMEVADR 206
|
....*...
gi 2524717128 228 RIYQYKGN 235
Cdd:PRK10851 207 VVVMSQGN 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
317-506 |
1.33e-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: 103.01 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIgetvrfgyysqDGlqFDEQMKV 396
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-----------DG--EDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 397 IDVVQDIAeVIELGNG--KRLTASQFLQHF--------------------LFT-PETQHSYVYKLSGGERRRLYLCTVLM 453
Cdd:COG4555 70 REARRQIG-VLPDERGlyDRLTVRENIRYFaelyglfdeelkkrieelieLLGlEEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 454 RNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVVDHLLV 506
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVI 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
317-508 |
1.37e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 100.40 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGEtvrfgyysqdglqfdeqmkv 396
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 397 idvvQDIAEVIELGNGKRLtasqflqhflftpetqhSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVL 476
Cdd:cd00267 61 ----KDIAKLPLEELRRRI-----------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*
gi 2524717128 477 EEYLRNF--KGC-VIVVSHDRYFMDKVVDHLLVFN 508
Cdd:cd00267 120 LELLRELaeEGRtVIIVTHDPELAELAADRVIVLK 154
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
316-506 |
1.72e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 101.43 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFG-------------- 381
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG------EIYLDgkplsampppewrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 382 ---YYSQDGLQFDeqmkviDVVQD-IAEVIELGNGK--RLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRN 455
Cdd:COG4619 75 qvaYVPQEPALWG------GTVRDnLPFPFQLRERKfdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 456 PNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV 506
Cdd:COG4619 149 PDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-229 |
5.63e-24 |
|
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: 106.39 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF--GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR--VGY 74
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldEDDLRrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPqypeeltvleACFhhgNSTVelikeyercmetdghpgLDGI-LARMD--HEKAWeyeqkakQILSQLKIRDFNQQ 151
Cdd:COG4987 414 VPQRP----------HLF---DTTL-----------------RENLrLARPDatDEELW-------AALERVGLGDWLAA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VK------------SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDM-TEWLEDYLRRT-NLTLLMVTHDRYFLDRV 217
Cdd:COG4987 457 LPdgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEALaGRTVLLITHRLAGLERM 536
|
250
....*....|..
gi 2524717128 218 cSEIIEIDNRRI 229
Cdd:COG4987 537 -DRILVLEDGRI 547
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-232 |
5.43e-23 |
|
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: 97.35 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI-------SFRRDIRVGYL-EQDP 79
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLpEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYPEElTVLEACFHHGNstvelikeyercmetdghpgldgiLARMDHEKAweyeqkAKQI---LSQLKIRDF-NQQVKSL 155
Cdd:cd03269 81 LYPKM-KVIDQLVYLAQ------------------------LKGLKKEEA------RRRIdewLERLELSEYaNKRVEEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQY 232
Cdd:cd03269 130 SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
317-508 |
6.26e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.15 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDL--KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGAL-----DIGETVRFGYYSQDGL- 388
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkDLTKLSLKELRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 389 ------QF------DE------QMKV--IDVVQDIAEVIELGNgkrltasqfLQHFLftpetqHSYVYKLSGGERRRLYL 448
Cdd:cd03225 81 fqnpddQFfgptveEEvafgleNLGLpeEEIEERVEEALELVG---------LEGLR------DRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 449 CTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-229 |
7.55e-23 |
|
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: 103.38 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD---LVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR--VG 73
Cdd:COG2274 474 IELENVSFRYPGdspPVL-DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidPASLRrqIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPQypeeL---TVLEacfhhgNSTVelikeyercmetdGHPGLDgilarmdhekaweyEQKAKQILSQLKIRDF-- 148
Cdd:COG2274 553 VVLQDVF----LfsgTIRE------NITL-------------GDPDAT--------------DEEIIEAARLAGLHDFie 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 ------NQQV----KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHDRYFLdR 216
Cdd:COG2274 596 alpmgyDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTI-R 674
|
250
....*....|...
gi 2524717128 217 VCSEIIEIDNRRI 229
Cdd:COG2274 675 LADRIIVLDKGRI 687
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-235 |
7.79e-23 |
|
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: 97.80 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------RRDIR---VGYLEQD 78
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatDVPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEELTVLE-ACFhhgnstvelikeyercmetdghpGLDgILARMDHEKAWEYEQKAKQILSQLKIRDFNQQVKS-LS 156
Cdd:cd03296 83 YALFRHMTVFDnVAF-----------------------GLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAqLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHDRyfldrvcSEIIEIDNRRIYQY 232
Cdd:cd03296 139 GGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRlhdeLHVTTVFVTHDQ-------EEALEVADRVVVMN 211
|
...
gi 2524717128 233 KGN 235
Cdd:cd03296 212 KGR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-210 |
8.85e-23 |
|
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: 97.31 E-value: 8.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI--------RVGYLEQD 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgKDItnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEELTVLE-ACFhhgnstvelikeyercmetdghpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRDF-NQQVKSLS 156
Cdd:cd03300 81 YALFPHLTVFEnIAF-----------------------GL-----RLKKLPKAEIKERVAEALDLVQLEGYaNRKPSQLS 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHD 210
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqkeLGITFVFVTHD 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-210 |
1.74e-22 |
|
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: 96.64 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI--------RVGYLEQD 78
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgKDItnlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 pqypeeltvlEACFHHgnSTVELIKEYercmetdghpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRD-FNQQVKSLSG 157
Cdd:cd03299 80 ----------YALFPH--MTVYKNIAY----------GL-----KKRKVDKKEIERKVLEIAEMLGIDHlLNRKPETLSG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHD 210
Cdd:cd03299 133 GEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-229 |
1.98e-22 |
|
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: 96.50 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS----------------F 66
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 RRDIrvGYLEQDPQYPEELTVLEacfhhgNSTVELikeyercmetdghpgldgilaRMDHEKAWEYEQKAKQILSQLKIR 146
Cdd:cd03258 81 RRRI--GMIFQHFNLLSSRTVFE------NVALPL---------------------EIAGVPKAEIEERVLELLELVGLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DFNQQVKS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHDRYFLDRVCSEI 221
Cdd:cd03258 132 DKADAYPAqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINrelgLTIVLITHEMEVVKRICDRV 211
|
....*...
gi 2524717128 222 IEIDNRRI 229
Cdd:cd03258 212 AVMEKGEV 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-547 |
2.22e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 101.12 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 340 RYekmGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDglQFD-EQMKVIDVV------------------ 400
Cdd:PRK15064 29 RY---GLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQD--QFAfEEFTVLDTVimghtelwevkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 -------QDIAEVIELgngkrltASQFLQHFLFT--------------PETQH----SYV---YKLsggerrRLYLCTVL 452
Cdd:PRK15064 104 alpemseEDGMKVADL-------EVKFAEMDGYTaearagelllgvgiPEEQHyglmSEVapgWKL------RVLLAQAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 453 MRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHL--LVFngqGDIRDFPGNYTRYRdwkdAK 530
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMadLDY---GELRVYPGNYDEYM----TA 243
|
250
....*....|....*...
gi 2524717128 531 AAQEREKE-KEAAKAQEE 547
Cdd:PRK15064 244 ATQARERLlADNAKKKAQ 261
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-222 |
2.79e-22 |
|
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: 94.93 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFGLSEGQRVGLIAKNGSGKSTLLNILSGK--EGYDSGTI----------SFRRdiRVGYLEQDPQYPEELTVLEACf 92
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVlingrpldkrSFRK--IIGYVPQDDILHPTLTVRETL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 93 hhgnstvelikeyercmetdghpgldgilarmdhekaweyeqkakqilsqlkirDFNQQVKSLSGGQLKRVALANTLITE 172
Cdd:cd03213 104 ------------------------------------------------------MFAAKLRGLSGGERKRVSIALELVSN 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 173 PDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHD-RYFLDRVCSEII 222
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRladTGRTIICSIHQpSSEIFELFDKLL 183
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
313-510 |
8.42e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.77 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV-----RFGYYSQD 386
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 gLQFDEQ--MKVIDVV-------------------QDIAEVIE-LGngkrltasqfLQHFLftpetqHSYVYKLSGGERR 444
Cdd:COG1121 84 -AEVDWDfpITVRDVVlmgrygrrglfrrpsradrEAVDEALErVG----------LEDLA------DRPIGELSGGQQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 445 RLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK--GC-VIVVSHDRYFMDKVVDHLLVFNGQ 510
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRreGKtILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-210 |
8.63e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.07 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVnsilQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-----------RRD 69
Cdd:COG3839 1 MASL----ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdlppkDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IrvGYLEQDPQ-YPEeLTVLEacfhhgNstvelikeyercMETdghpGLDgiLARMDheKAwEYEQKAKQILSQLKIRDF 148
Cdd:COG3839 77 I--AMVFQSYAlYPH-MTVYE------N------------IAF----PLK--LRKVP--KA-EIDRRVREAAELLGLEDL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 149 -NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDM-TEwLEDYLRRTNLTLLMVTHD 210
Cdd:COG3839 127 lDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMrAE-IKRLHRRLGTTTIYVTHD 193
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-295 |
8.67e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 99.86 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQdpQYPEE 84
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--HQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 LTVLEACFHHgnstvelikeyercmetdghpgldgiLARMDHEkawEYEQKAKQILSQLKIR--DFNQQVKSLSGGQLKR 162
Cdd:PRK10636 388 LRADESPLQH--------------------------LARLAPQ---ELEQKLRDYLGGFGFQgdKVTEETRRFSGGEKAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYKGNYSYY--- 239
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYqqw 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 240 -LEKREERIEAKTVEIERANNLYRTELEWMRRMPQARGHKARYREdafyELEKVAKQ 295
Cdd:PRK10636 519 lSDVQKQENQTDEAPKENNANSAQARKDQKRREAELRTQTQPLRK----EIARLEKE 571
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-228 |
9.90e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 92.45 E-value: 9.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD---LVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR--VG 73
Cdd:cd03228 1 IEFKNVSFSYPGrpkPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdlrdldLESLRknIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPqypeeltvleacfhhgnstvelikeyercmetdghpgldgilarmdhekaweyeqkakqILsqlkirdFNQQVK 153
Cdd:cd03228 80 YVPQDP-----------------------------------------------------------FL-------FSGTIR 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 154 S--LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHdRYFLDRVCSEIIEIDNRR 228
Cdd:cd03228 94 EniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-470 |
1.26e-21 |
|
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: 98.74 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG--KEGYDSGTISFR------RDIR------V 72
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSgsplkaSNIRdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPQYPEELTVLEACFhHGNSTVelikeyercmetdgHPGldgilARMDHEkawEYEQKAKQILSQLKIRDFN--Q 150
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIF-LGNEIT--------------LPG-----GRMAYN---AMYLRAKNLLRELQLDADNvtR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR---RTNLTLLMVTHDRYFLDRVCSEIIEI-DN 226
Cdd:TIGR02633 138 PVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRdlkAHGVACVYISHKLNEVKAVCDTICVIrDG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 227 RRI-YQYKGNYSyylekrEERIEAKTVEIErANNLYRTElewmrrmPQArghkaryredafyelekvakqrfnndnvkld 305
Cdd:TIGR02633 218 QHVaTKDMSTMS------EDDIITMMVGRE-ITSLYPHE-------PHE------------------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 306 vkasyIGSKIFEADHLYKSFGD---LKILDDFSYIFARYEKMGIVGNNGTGKSTFI-------------KILMRHEQAD- 368
Cdd:TIGR02633 253 -----IGDVILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVqalfgaypgkfegNVFINGKPVDi 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 369 RGALD-IGETV--------RFGYYSQDGLQFDEQMKVID------VVQDIAEVIELGNG-KRL---TASQFLQhflftpe 429
Cdd:TIGR02633 328 RNPAQaIRAGIamvpedrkRHGIVPILGVGKNITLSVLKsfcfkmRIDAAAELQIIGSAiQRLkvkTASPFLP------- 400
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2524717128 430 tqhsyVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:TIGR02633 401 -----IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-229 |
1.30e-21 |
|
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: 93.81 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR--VGYLEQDP------------- 79
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldPADLRrnIGYVPQDVtlfygtlrdnitl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 --QYPEELTVLEAcfhhgnSTVELIKEYercmeTDGHP-GLDgilarmdhekaweyeqkakqilsqLKIRDFNQqvkSLS 156
Cdd:cd03245 101 gaPLADDERILRA------AELAGVTDF-----VNKHPnGLD------------------------LQIGERGR---GLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT--NLTLLMVTHdRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
315-506 |
2.22e-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: 93.95 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA--LDiGETV----------RFGY 382
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlLD-GRDLaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 YSQDgLQFDEQMKVIDVV----------------QD---IAEVIE-LGngkrltasqfLQHFlftpetQHSYVYKLSGGE 442
Cdd:COG1120 80 VPQE-PPAPFGLTVRELValgryphlglfgrpsaEDreaVEEALErTG----------LEHL------ADRPVDELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 443 RRRLYLCTVLMRNPNFLVLDEPTNDLDI----VTLNVLEEYLRNFKGCVIVVSHD-----RYFmdkvvDHLLV 506
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDlnlaaRYA-----DRLVL 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-229 |
2.22e-21 |
|
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: 98.29 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD-LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF----RRDI-------RVGYL 75
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdLSDLdpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEElTVLE-ACFHHGNSTVELIkeyERCMETdghPGLDGILARMDHekaweyeqkakQILSQLKIRDFNqqvks 154
Cdd:COG4988 417 PQNPYLFAG-TIREnLRLGRPDASDEEL---EAALEA---AGLDEFVAALPD-----------GLDTPLGEGGRG----- 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDmTEW-LEDYLRR--TNLTLLMVTHDRYFLDRvCSEIIEIDNRRI 229
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE-TEAeILQALRRlaKGRTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-229 |
2.67e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLF---------ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS----------- 65
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgeplaklnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 66 -----FRRDIRVGYleQDPqypeeltvLEAcFHHGNSTVELIKEYERcmetdgHpgldgiLARMDHEkawEYEQKAKQIL 140
Cdd:PRK10419 82 aqrkaFRRDIQMVF--QDS--------ISA-VNPRKTVREIIREPLR------H------LLSLDKA---ERLARASEML 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 141 SQLKIRD--FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFL 214
Cdd:PRK10419 136 RAVDLDDsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
250
....*....|....*
gi 2524717128 215 DRVCSEIIEIDNRRI 229
Cdd:PRK10419 216 ERFCQRVMVMDNGQI 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-229 |
2.72e-21 |
|
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: 94.06 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------------RRDIR--VGYLEQdpqYPE----EL 85
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgrditakkkkkLKDLRkkVGLVFQ---FPEhqlfEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLE-ACFHHGNstvelikeyercmetdghpgldgilarMDHEKAwEYEQKAKQILSQLKIRD--FNQQVKSLSGGQLKR 162
Cdd:TIGR04521 99 TVYKdIAFGPKN---------------------------LGLSEE-EAEERVKEALELVGLDEeyLERSPFELSGGQMRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDpkgrKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-232 |
3.91e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-------FRRDI---------- 70
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdFSQKPsekairllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQdpQY---PEeLTVLEacfhhgNSTVELIKeyercmetdghpgldgiLARMDHEKAWEyeqKAKQILSQLKIRD 147
Cdd:COG4161 83 KVGMVFQ--QYnlwPH-LTVME------NLIEAPCK-----------------VLGLSKEQARE---KAMKLLARLRLTD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 FNQQVK-SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR---RTNLTLLMVTHDRYFLDRVCSEIIE 223
Cdd:COG4161 134 KADRFPlHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRelsQTGITQVIVTHEVEFARKVASQVVY 213
|
....*....
gi 2524717128 224 IDNRRIYQY 232
Cdd:COG4161 214 MEKGRIIEQ 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-210 |
4.21e-21 |
|
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: 92.24 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGY-----DSGTISFR-RDI----------- 70
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDgKDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 -RVGYLEQDPqYPEELTVLE----ACFHHG-NSTVELIKEYERCMETDGhpgLDGILARmdhekaweyeqkakqilsqlk 144
Cdd:cd03260 81 rRVGMVFQKP-NPFPGSIYDnvayGLRLHGiKLKEELDERVEEALRKAA---LWDEVKD--------------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 145 irdfNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR--RTNLTLLMVTHD 210
Cdd:cd03260 136 ----RLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
317-510 |
4.34e-21 |
|
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: 90.52 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGD--LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGYYSQDGLQFDEQM 394
Cdd:cd03228 2 EFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG------EILIDGVDLRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQdiaevielgngkrltasqflqhflftpetQHSYVYK-------LSGGERRRLYLCTVLMRNPNFLVLDEPTND 467
Cdd:cd03228 76 KNIAYVP-----------------------------QDPFLFSgtireniLSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524717128 468 LDIVTLNVLEEYLRNFKGC--VIVVSHdRYFMDKVVDHLLVF-NGQ 510
Cdd:cd03228 127 LDPETEALILEALRALAKGktVIVIAH-RLSTIRDADRIIVLdDGR 171
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
8-229 |
4.43e-21 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 92.96 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-----------RRDIRVGYLE 76
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 QDPQYPEELTVLEACfhhgnstvelikeyercmetdghpgldgILARMDHEKAWEYEQK-----AKQILSQLKIRDF-NQ 150
Cdd:TIGR03873 82 QDSDTAVPLTVRDVV----------------------------ALGRIPHRSLWAGDSPhdaavVDRALARTELSHLaDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDyLRRTNLTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:TIGR03873 134 DMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraqLETLALVRE-LAATGVTVVAALHDLNLAASYCDHVVVLDG 212
|
...
gi 2524717128 227 RRI 229
Cdd:TIGR03873 213 GRV 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-228 |
5.83e-21 |
|
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: 92.11 E-value: 5.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF-----GDLVL--FENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRD-------- 69
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 --------IR---VGYLEQdpqypeELTVLEACfhhgnSTVELIKEyercmetdghpgldGILAR-MDHEKAweyEQKAK 137
Cdd:COG4778 82 aspreilaLRrrtIGYVSQ------FLRVIPRV-----SALDVVAE--------------PLLERgVDREEA---RARAR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 138 QILSQLKIRD---------FnqqvkslSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRtN 201
Cdd:COG4778 134 ELLARLNLPErlwdlppatF-------SGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVEL---IEEAKAR-G 202
|
250 260
....*....|....*....|....*..
gi 2524717128 202 LTLLMVTHDRYFLDRVCSEIIEIDNRR 228
Cdd:COG4778 203 TAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-234 |
6.35e-21 |
|
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: 92.01 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF---------------------GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGtisf 66
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 rrDIRVGYL---EQDPQYPEELTVLeacfhHGNSTvELIKEYercmetdghPGLDG--ILARMDHEKAWEYEQKAKQILS 141
Cdd:cd03267 77 --EVRVAGLvpwKRRKKFLRRIGVV-----FGQKT-QLWWDL---------PVIDSfyLLAAIYDLPPARFKKRLDELSE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 142 QLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFLDR 216
Cdd:cd03267 140 LLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqeNIRNFLKEYNRERGTTVLLTSHYMKDIEA 219
|
250
....*....|....*...
gi 2524717128 217 VCSEIIEIDNRRIyQYKG 234
Cdd:cd03267 220 LARRVLVIDKGRL-LYDG 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
331-466 |
6.47e-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: 89.63 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGET-----------VRFGYYSQDgLQFDEQMKVIDV 399
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 400 VQDIAEVIELGNGKRL-TASQFLQHF---LFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:pfam00005 80 LRLGLLLKGLSKREKDaRAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-233 |
8.51e-21 |
|
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: 91.20 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 15 KSFGDLVLfeNISFGLSEgQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR---------------RDIRVGYLEQdp 79
Cdd:cd03297 8 KRLPDFTL--KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIGLVFQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYpeeltvleACFHHGNSTVELIKEYERCMETDGHPGLDGILARMDhekaweyeqkakqiLSQLKirdfNQQVKSLSGGQ 159
Cdd:cd03297 83 QY--------ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLG--------------LDHLL----NRYPAQLSGGE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 160 LKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT----NLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQYK 233
Cdd:cd03297 137 KQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-210 |
9.12e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.30 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrdirvgylEQDPQYPEELT 86
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYR--------MRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLEAcfhhgnstvelikEYERCMETD-----GHPgLDGIlaRMD-----------------HekaweY---EQKAKQILS 141
Cdd:PRK11701 78 LSEA-------------ERRRLLRTEwgfvhQHP-RDGL--RMQvsaggnigerlmavgarH-----YgdiRATAGDWLE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 142 QLKI---RdFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHD 210
Cdd:PRK11701 137 RVEIdaaR-IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvreLGLAVVIVTHD 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-210 |
1.12e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFG-----DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-----------FRRDI 70
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdvtklpeYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQDPQY--PEELTVLEacfhhgNstveLIKEYERcmetdGHPGldGILARMDHEKAWEYeqkaKQILSQLKI--- 145
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEE------N----LALAYRR-----GKRR--GLRRGLTKKRRELF----RELLATLGLgle 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 146 -RdFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMTEWLedyLRRTNLTLLMVTHD 210
Cdd:COG1101 140 nR-LDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvLELTEKI---VEENNLTTLMVTHN 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-210 |
1.13e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.62 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYD---SGTISFR-RDI--------RVGYL 75
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNgRRLtalpaeqrRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLE-ACFhhgnstvelikeyercmetdghpGLDGILARmdHEKaweyEQKAKQILSQLKIRDF-NQQVK 153
Cdd:COG4136 82 FQDDLLFPHLSVGEnLAF-----------------------ALPPTIGR--AQR----RARVEQALEEAGLAGFaDRDPA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT----EWLEDYLRRTNLTLLMVTHD 210
Cdd:COG4136 133 TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRaqfrEFVFEQIRQRGIPALLVTHD 193
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-229 |
1.30e-20 |
|
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: 96.47 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-------------RRDIrvGYLEQDPQ---------- 80
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLdgvdirqidpadlRRNI--GYVPQDPRlfygtlrdni 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 -----YPEELTVLEAcfhhgnstVEL--IKEYercmeTDGHP-GLDgilaRMDHEKAweyeqkakqilsqlkirdfnqqv 152
Cdd:TIGR03375 560 algapYADDEEILRA--------AELagVTEF-----VRRHPdGLD----MQIGERG----------------------- 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT--NLTLLMVTHDRYFLDRVcSEIIEIDNRRI 229
Cdd:TIGR03375 600 RSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWlaGKTLVLVTHRTSLLDLV-DRIIVMDNGRI 677
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
315-501 |
1.72e-20 |
|
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: 90.64 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSF----GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETV------------ 378
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 379 --RFGYYSQDGLQ-FDEQMKVIDVvqdIAEVIELGNG------KRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLC 449
Cdd:cd03257 81 rkEIQMVFQDPMSsLNPRMTIGEQ---IAEPLRIHGKlskkeaRKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 450 TVLMRNPNFLVLDEPTNDLDIVT----LNVLEEyLRNFKGC-VIVVSHD----RYFMDKVV 501
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVqaqiLDLLKK-LQEELGLtLLFITHDlgvvAKIADRVA 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-229 |
2.07e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.12 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDL----VLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGK----------EGYDSGTISFRRDIRV 72
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlepdagfatvDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPQYPEELTVLEACFHHGnstvelikeyercmetdghpGLDGIlarmdheKAWEYEQKAKQILSQLKIRDF-NQQ 151
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFA--------------------GLYGL-------KGDELTARLEELADRLGMEELlDRR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRR 228
Cdd:cd03266 134 VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFirqLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
.
gi 2524717128 229 I 229
Cdd:cd03266 214 V 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-228 |
2.12e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF----------RRDIRVGYL 75
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsrarHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQ----DPQYP--EELTVLEACFhhGNSTVELIKEYERCMEtdghpgldgiLARMdhekaweyEQKAkqilsqlkirdfN 149
Cdd:PRK13537 86 PQfdnlDPDFTvrENLLVFGRYF--GLSAAAARALVPPLLE----------FAKL--------ENKA------------D 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNlTLLMVTHDRYFLDRVCSEIIEID 225
Cdd:PRK13537 134 AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQarhlMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIE 212
|
...
gi 2524717128 226 NRR 228
Cdd:PRK13537 213 EGR 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-229 |
2.23e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG-DLVLFeNISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-------------------FR 67
Cdd:PRK11124 3 IQLNGINCFYGaHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdfsktpsdkaireLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RDirVGYLEQdpQY---PEeLTVLEacfhhgnstvELIkeyERCMETDGhpgldgilarMDHEKAweyEQKAKQILSQLK 144
Cdd:PRK11124 82 RN--VGMVFQ--QYnlwPH-LTVQQ----------NLI---EAPCRVLG----------LSKDQA---LARAEKLLERLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 145 IRDFNQQVK-SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSE 220
Cdd:PRK11124 131 LKPYADRFPlHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIireLAETGITQVIVTHEVEVARKTASR 210
|
....*....
gi 2524717128 221 IIEIDNRRI 229
Cdd:PRK11124 211 VVYMENGHI 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-227 |
2.95e-20 |
|
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: 87.87 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFrrdirvgyleqdpqypeeltv 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 88 leacfhhgnstvelikeyercmetDGHPgldgiLARMDHEKAWeyeqkakqilsQLKIRDFNQqvksLSGGQLKRVALAN 167
Cdd:cd03216 60 ------------------------DGKE-----VSFASPRDAR-----------RAGIAMVYQ----LSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 168 TLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT---NLTLLMVTHdryFLDrvcsEIIEIDNR 227
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISH---RLD----EVFEIADR 151
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-210 |
4.53e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.17 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQ----DPQY 81
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 82 PeeLTVleacfhhgnstvelikeyERCMETdgHPGLDgilaRMDHEKAWEYEQKAKQIlsqlkirdfNQQVKSLSGGQLK 161
Cdd:PRK09544 83 P--LTV------------------NRFLRL--RPGTK----KEDILPALKRVQAGHLI---------DAPMQKLSGGETQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 162 RVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRT-NLTLLMVTHD 210
Cdd:PRK09544 128 RVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLidqLRRElDCAVLMVSHD 180
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-199 |
4.76e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.71 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIRvgylEQDPQYPEELT 86
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgEPIR----RQRDEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLeacfhhgnstvelikeyercmetdGH-PGLDGILArmdhekAWEY------------EQKAKQILSQLKIRDFNQ-QV 152
Cdd:PRK13538 78 YL------------------------GHqPGIKTELT------ALENlrfyqrlhgpgdDEALWEALAQVGLAGFEDvPV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR 199
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-224 |
5.12e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 5.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR------RDIR------VGY 74
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrfRSPRdaqaagIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEACFhhgnstveLIKEYERcmetdghPGLdgilarMDHEKAweyEQKAKQILSQLKIR-DFNQQVK 153
Cdd:COG1129 84 IHQELNLVPNLSVAENIF--------LGREPRR-------GGL------IDWRAM---RRRARELLARLGLDiDPDTPVG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWL----EDyLRRTNLTLLMVTHdryFLDrvcsEIIEI 224
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKAQGVAIIYISH---RLD----EVFEI 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
317-522 |
6.79e-20 |
|
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: 89.48 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFG----DLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRF----------G 381
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRrrrkafrrrvQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 382 YYSQDG-LQFDEQMKVIDVvqdIAEVI-ELGNGKRL-TASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNF 458
Cdd:COG1124 83 MVFQDPyASLHPRHTVDRI---LAEPLrIHGLPDREeRIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 459 LVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVF-NGQ-------GDIRDFPGN-YTR 522
Cdd:COG1124 160 LLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMqNGRiveeltvADLLAGPKHpYTR 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
316-508 |
1.15e-19 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 86.86 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVrfgyYSQDGLQFDEQM 394
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDL----TDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQDIAEVielgngKRLTASQFLqhflftpetqhsyVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLN 474
Cdd:cd03229 77 RIGMVFQDFALF------PHLTVLENI-------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524717128 475 VLEEYLRNFK---GC-VIVVSHDRYFMDKVVDHLLVFN 508
Cdd:cd03229 138 EVRALLKSLQaqlGItVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-207 |
1.18e-19 |
|
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: 87.87 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR-----------VGYL 75
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEacfhhgNSTVelikeyercmetdghpgldGILARMDHEKAWEYEqKAKQILSQLKIRdFNQQVKSL 155
Cdd:cd03224 81 PEGRRIFPELTVEE------NLLL-------------------GAYARRRAKRKARLE-RVYELFPRLKER-RKQLAGTL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN---LTLLMV 207
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRdegVTILLV 188
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
317-510 |
1.22e-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: 87.70 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDL-KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGAL-----DIGETVRF---GYYSQDg 387
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkPIKAKERRksiGYVMQD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 lqFDEQMKVIDVVQDIAEVIELGNGKRLTASQFLQHF-LFTPETQHSYvyKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:cd03226 80 --VDYQLFTDSVREELLLGLKELDAGNEQAETVLKDLdLYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524717128 467 DLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVVDH-LLVFNGQ 510
Cdd:cd03226 156 GLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRvLLLANGA 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-212 |
1.56e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNIL-------SGK---EGYDSGTISFRRDIR-VGY 74
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTvflGDKPISMLSSRQLARrLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEacfhhgnstveLIkEYERcmetDGHPGLDGILARMDHekaweyeQKAKQILSQLKIRDF-NQQVK 153
Cdd:PRK11231 81 LPQHHLTPEGITVRE-----------LV-AYGR----SPWLSLWGRLSAEDN-------ARVNQAMEQTRINHLaDRRLT 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL---TLLMVTHD-----RY 212
Cdd:PRK11231 138 DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHDlnqasRY 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-209 |
1.68e-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: 87.03 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-RRDIRvgylEQDPQYPEELT 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWnGTPLA----EQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLeacfhhgnstvelikeyercmetdGH-PGLDGILARMDHEKAW----EYEQKA-KQILSQLKIRDFNQQ-VKSLSGGQ 159
Cdd:TIGR01189 77 YL------------------------GHlPGLKPELSALENLHFWaaihGGAQRTiEDALAAVGLTGFEDLpAAQLSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 160 LKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNLTLLmVTH 209
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAgvalLAGLLRAHLARGGIVLL-TTH 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
317-510 |
2.06e-19 |
|
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: 85.95 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVrfgyysqdglqfdEQMK 395
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDL-------------ASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 396 VIDVVQDIA---EVIELGNgkrltasqfLQHFLftpetqHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI-- 470
Cdd:cd03214 68 PKELARKIAyvpQALELLG---------LAHLA------DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIah 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 471 --VTLNVLEEYLRNFKGCVIVVSHD-----RYFmDKVVdhlLVFNGQ 510
Cdd:cd03214 133 qiELLELLRRLARERGKTVVMVLHDlnlaaRYA-DRVI---LLKDGR 175
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
317-516 |
2.48e-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: 87.56 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV-------------RFGY 382
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 YSQDGLQFDEqMKVIDVVQ------------DIAEVIELgngkRLtasqflqHFLFTPETQHSYVYKLSGGERRRLYLCT 450
Cdd:cd03261 82 LFQSGALFDS-LTVFENVAfplrehtrlseeEIREIVLE----KL-------EAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 451 VLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG----CVIVVSHDRYFMDKVVDHLLV-FNG----QGDIRDF 516
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelglTSIMVTHDLDTAFAIADRIAVlYDGkivaEGTPEEL 224
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
559-625 |
3.18e-19 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 81.74 E-value: 3.18e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 559 RMSFKEKREFEQLEQDIAALEAEKQSIEEALCSGALSVD--ELTEKSKRLPELADLIDEKTMRWLELSE 625
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDyeKLQELSAELEELEAELEELYERWEELEE 69
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-211 |
4.16e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 3 AVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDirvgyLEQDPQY 81
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVD-----LSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 82 PEELTVL---EACFHHgnSTVELIKEYercmetdghpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRDF-NQQVKSLSG 157
Cdd:PRK11607 90 QRPINMMfqsYALFPH--MTVEQNIAF----------GL-----KQDKLPKAEIASRVNEMLGLVHMQEFaKRKPHQLSG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE----DYLRRTNLTLLMVTHDR 211
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQ 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
316-520 |
4.50e-19 |
|
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: 86.62 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSF-GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA-----LDIGETVRFGYYSQDGLQ 389
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 390 F---DEQMKVIDVVQDIA----------EVIElgngKRL--TASQF-LQHFLftpetqHSYVYKLSGGERRRLYLCTVLM 453
Cdd:COG1122 81 FqnpDDQLFAPTVEEDVAfgpenlglprEEIR----ERVeeALELVgLEHLA------DRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 454 RNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVVDHLLVFNG-----QGDIRDFPGNY 520
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDgrivaDGTPREVFSDY 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-229 |
4.53e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI--------SFRRDIRVGYleQDP 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMF--QDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYPEELTVLEacfhhgnsTVELikeyercmetdghpGLDGilarmdhekawEYEQKAKQILSQLKIRD-FNQQVKSLSGG 158
Cdd:PRK11247 91 RLLPWKKVID--------NVGL--------------GLKG-----------QWRDAALQALAAVGLADrANEWPAALSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 159 QLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfldrvCSEIIEIDNRRI 229
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD-------VSEAVAMADRVL 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-493 |
4.83e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF--GDLV--LFENISFGLSEGQRVGLIAKNGSGKS-TLLNIL----SGKEGYDSGTISFR---------- 67
Cdd:PRK15134 5 LLAIENLSVAFrqQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHgesllhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 --RDIR---VGYLEQDP------------QYPEELTVleacfHHGNSTVELIKEYERCMETDGhpgldgilarmdhekaw 130
Cdd:PRK15134 85 tlRGVRgnkIAMIFQEPmvslnplhtlekQLYEVLSL-----HRGMRREAARGEILNCLDRVG----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 131 eYEQKAKqilsqlKIRDFNQQvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLM 206
Cdd:PRK15134 143 -IRQAAK------RLTDYPHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 207 VTHDRYFLDRVCseiieiDNRRIYQykgnysyylekreeriEAKTVEIERANNLYRTelewmrrmPQargHkaRYredaf 286
Cdd:PRK15134 213 ITHNLSIVRKLA------DRVAVMQ----------------NGRCVEQNRAATLFSA--------PT---H--PY----- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 287 yelekvAKQRFNNDNVKLDVKASYIGSKIFEADHLYKSF----GDLK-------ILDDFSYIFARYEKMGIVGNNGTGKS 355
Cdd:PRK15134 253 ------TQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFpirkGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 356 TFIKILMRHEQAdRGALDIGETVRFGYYSQDGLQFDEQMKVI------------DVVQDIAEVIELgNGKRLTASQ---- 419
Cdd:PRK15134 327 TTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLPVRHRIQVVfqdpnsslnprlNVLQIIEEGLRV-HQPTLSAAQreqq 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 420 ---FLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD------IVTLnvLEEYLRNFKGCVIVV 490
Cdd:PRK15134 405 viaVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqILAL--LKSLQQKHQLAYLFI 482
|
...
gi 2524717128 491 SHD 493
Cdd:PRK15134 483 SHD 485
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
338-522 |
1.70e-18 |
|
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: 85.15 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 338 FARYEKMGIVGNNGTGKSTFIKILMRHEQADRGalDIGETVRFGYYSQDGLQFDEQMKVIDVVQDIAevielgngKRLTA 417
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG--DIEIELDTVSYKPQYIKADYEGTVRDLLSSIT--------KDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 418 SQFLQHFLFTP----ETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD----IVTLNVLEEYLRNFKGCVIV 489
Cdd:cd03237 92 HPYFKTEIAKPlqieQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFV 171
|
170 180 190
....*....|....*....|....*....|...
gi 2524717128 490 VSHDRYFMDKVVDHLLVFNGQgdirdfPGNYTR 522
Cdd:cd03237 172 VEHDIIMIDYLADRLIVFEGE------PSVNGV 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-210 |
1.75e-18 |
|
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: 84.23 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrDIRVGYLEqdpqyPEE--- 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDLP-----PKDrdi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 LTVLE--ACFHHgnSTVelikeyercMETDGHPgldgilARMDHEKAWEYEQKAKQILSQLKIRDF-NQQVKSLSGGQLK 161
Cdd:cd03301 75 AMVFQnyALYPH--MTV---------YDNIAFG------LKLRKVPKDEIDERVREVAELLQIEHLlDRKPKQLSGGQRQ 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 162 RVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-492 |
1.75e-18 |
|
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: 82.86 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRFGyysqdglqfdeqm 394
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 kvidvvqDIAEVIELGNGkrltasqflqhflftpetqhsYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLN 474
Cdd:cd03216 68 -------SPRDARRAGIA---------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180
....*....|....*....|.
gi 2524717128 475 VLEEYLRNFK--GC-VIVVSH 492
Cdd:cd03216 120 RLFKVIRRLRaqGVaVIFISH 140
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
317-508 |
1.81e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 84.25 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRG-------ALDIGETVRFGYYSQD-GL 388
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGevlfdgkPLDIAARNRIGYLPEErGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 389 QFDeqMKVIDVVQDIAEVieLGNGKRLTASQ---FLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:cd03269 82 YPK--MKVIDQLVYLAQL--KGLKKEEARRRideWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524717128 466 NDLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLN 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-210 |
2.07e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI---------RVGYLE 76
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgQHIeglpghqiaRMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 --QDPQYPEELTVLE----ACFHHGNSTVelikeyercmetdghpgLDGILARMDHEKAwEYE--QKAKQILSQLKIRDF 148
Cdd:PRK11300 85 tfQHVRLFREMTVIEnllvAQHQQLKTGL-----------------FSGLLKTPAFRRA-ESEalDRAATWLERVGLLEH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 149 -NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE---DYLRRT-NLTLLMVTHD 210
Cdd:PRK11300 147 aNRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDeliAELRNEhNVTVLLIEHD 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-229 |
2.09e-18 |
|
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: 85.63 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSF---------GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIRVGYL 75
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELT-VLEACFHHGN--STVE-LIKEYERcmetdgHpgldgiLARMDhekawEYEQKAKqILSQLKIRDFNQQ 151
Cdd:TIGR02769 81 KQRRAFRRDVQlVFQDSPSAVNprMTVRqIIGEPLR------H------LTSLD-----ESEQKAR-IAELLDMVGLRSE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 V-----KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:TIGR02769 143 DadklpRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVA 222
|
....*..
gi 2524717128 223 EIDNRRI 229
Cdd:TIGR02769 223 VMDKGQI 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
2.15e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 88.88 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 2 AAVNSILQVENLTKSFGD-LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI------------SFRR 68
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadaDSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 69 DiRVGYLEQDPQYPEElTVLEAC-FHHGNSTVELIKEyercmetdghpgldgILARMDhekAWEYEQKAKQILsQLKIRD 147
Cdd:TIGR02857 396 D-QIAWVPQHPFLFAG-TIAENIrLARPDASDAEIRE---------------ALERAG---LDEFVAALPQGL-DTPIGE 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 148 fnqQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHDR 211
Cdd:TIGR02857 455 ---GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAlaQGRTVLLVTHRL 517
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-229 |
3.65e-18 |
|
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: 83.61 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS----------------FRRDI 70
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlrgraipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYleQDPQYPEELTVLEacfhhgnsTVELikeyerCMETDGHPGLdgilarmdhekawEYEQKAKQILSQL----KIR 146
Cdd:cd03292 81 GVVF--QDFRLLPDRNVYE--------NVAF------ALEVTGVPPR-------------EIRKRVPAALELVglshKHR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DFNQQvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL---TLLMVTHDRYFLDRVCSEIIE 223
Cdd:cd03292 132 ALPAE---LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIA 208
|
....*.
gi 2524717128 224 IDNRRI 229
Cdd:cd03292 209 LERGKL 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-186 |
4.57e-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: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDirvGYLEQDPQYPEELTV 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 88 LeacfhhgnstvelikeyercmetdGH-PGLDGILARMDHEKAWEYEQKAKQI---LSQLKIRDFNQQ-VKSLSGGQLKR 162
Cdd:cd03231 78 L------------------------GHaPGIKTTLSVLENLRFWHADHSDEQVeeaLARVGLNGFEDRpVAQLSAGQQRR 133
|
170 180
....*....|....*....|....
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLD 186
Cdd:cd03231 134 VALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
345-507 |
5.78e-18 |
|
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: 83.11 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 345 GIVGNNGTGKSTFIKILMRHEQADRGALDIGETV---------------RFGYYSQD---------------GLQFDEQM 394
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQyalfphlnvrenlafGLKRKRNR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQDIAEVIELgngkrltasqflQHFLFtpetqhSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLN 474
Cdd:cd03297 107 EDRISVDELLDLLGL------------DHLLN------RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2524717128 475 VLEEYLR----NFKGCVIVVSHDRYFMDKVVDHLLVF 507
Cdd:cd03297 169 QLLPELKqikkNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-229 |
6.43e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.60 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGtisfrrDIRVGYLE-QDPQYPEEL 85
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKvNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEA--CFHHGNSTVELIkeyercmetdghpGLDGIL---ARMDHEKAWEYEQKAKQILSQLKIRDFNQQVKS-LSGGQ 159
Cdd:PRK09493 75 IRQEAgmVFQQFYLFPHLT-------------ALENVMfgpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSeLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 160 LKRVALANTLITEPDLLILDEPTNHLDLDMT-EWLE--DYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-229 |
6.93e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 82.54 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 33 GQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrDIRVGYLEqdpqyPEELTVlEACFHHGNSTVELikEYERCMETD 112
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAP-----PADRPV-SMLFQENNLFAHL--TVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 113 GHPGLdgilaRMDHEKaweyEQKAKQILSQLKIRDFNQQV-KSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----L 187
Cdd:cd03298 95 LSPGL-----KLTAED----RQAIEVALARVGLAGLEKRLpGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524717128 188 DMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
316-493 |
7.19e-18 |
|
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: 82.53 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG----ETVRFGYYSQ------ 385
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylgh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 386 -DG----------LQFDEQMK-VIDVVQDIAEVIE-LGngkrltasqfLQHFLftpetqHSYVYKLSGGERRRLYLCTVL 452
Cdd:COG4133 83 aDGlkpeltvrenLRFWAALYgLRADREAIDEALEaVG----------LAGLA------DLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524717128 453 MRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK---GCVIVVSHD 493
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQ 190
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-232 |
7.56e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF----------------------GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSG 62
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 63 TIsfRRDIRVGYLeqdpqypeeltvLE--ACFhHGNSTV-ELIKeyercmetdghpgLDGILARMDHEkawEYEQKAKQI 139
Cdd:COG1134 82 RV--EVNGRVSAL------------LElgAGF-HPELTGrENIY-------------LNGRLLGLSRK---EIDEKFDEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 140 L--SQLKirDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDeptnhldldmtEWL---------------EDyLRRTN 201
Cdd:COG1134 131 VefAELG--DFiDQPVKTYSSGMRARLAFAVATAVDPDILLVD-----------EVLavgdaafqkkclariRE-LRESG 196
|
250 260 270
....*....|....*....|....*....|.
gi 2524717128 202 LTLLMVTHDRYFLDRVCSEIIEIDNRRIYQY 232
Cdd:COG1134 197 RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-470 |
7.76e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG--KEGYDSGTISFR------RDIR------V 72
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEgeelqaSNIRdteragI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPQYPEELTVLEACFhHGNstvELikeyercmetdgHPGldgilARMDHEKAWeyeQKAKQILSQLKIR-DFNQQ 151
Cdd:PRK13549 85 AIIHQELALVKELSVLENIF-LGN---EI------------TPG-----GIMDYDAMY---LRAQKLLAQLKLDiNPATP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDY---LRRTNLTLLMVTHDRYFLDRVCSEIIEI-DNR 227
Cdd:PRK13549 141 VGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIirdLKAHGIACIYISHKLNEVKAISDTICVIrDGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 228 RIYQYKGNysyylEKREERIEAKTVEIErANNLYRTElewmrrmPQArghkaryredafyelekvakqrfnndnvkldvk 307
Cdd:PRK13549 221 HIGTRPAA-----GMTEDDIITMMVGRE-LTALYPRE-------PHT--------------------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 308 asyIGSKIFEADHL---YKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILM-----RHEQA---DRGALDI-- 374
Cdd:PRK13549 255 ---IGEVILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgRWEGEifiDGKPVKIrn 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 375 -GETVRFG--YYSQD----GLqfdeqMKVIDVVQDI--AEVIELGNGKRL-------TASQFLQHFLFTPETQHSYVYKL 438
Cdd:PRK13549 332 pQQAIAQGiaMVPEDrkrdGI-----VPVMGVGKNItlAALDRFTGGSRIddaaelkTILESIQRLKVKTASPELAIARL 406
|
490 500 510
....*....|....*....|....*....|..
gi 2524717128 439 SGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-235 |
8.30e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.09 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 27 SFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-----------RRDirVGYLEQDPQYPEELTVLEacfhhg 95
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLngqdhtttppsRRP--VSMLFQENNLFSHLTVAQ------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 96 NSTVELikeyercmetdgHPGLdgilaRMDHEKaweyEQKAKQILSQLKIRDFNQQVKS-LSGGQLKRVALANTLITEPD 174
Cdd:PRK10771 91 NIGLGL------------NPGL-----KLNAAQ----REKLHAIARQMGIEDLLARLPGqLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 175 LLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfLD---RVCSEIIEIDNRRIYqYKGN 235
Cdd:PRK10771 150 ILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEdaaRIAPRSLVVADGRIA-WDGP 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-210 |
1.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSF-GDLVL-FENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR---------RD 69
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaitddnfEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IR--VGYLEQDPQypeeltvleacfhhgNSTVELIKEYercmetDGHPGLDGILARMDhekawEYEQKAKQILSQLKIRD 147
Cdd:PRK13648 81 LRkhIGIVFQNPD---------------NQFVGSIVKY------DVAFGLENHAVPYD-----EMHRRVSEALKQVDMLE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 148 F-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT----NLTLLMVTHD 210
Cdd:PRK13648 135 RaDYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHD 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
324-558 |
1.06e-17 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 87.22 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHeqadrgALD-IGETVRFGYYSQD-------GLQ------ 389
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMH------AIDgIPKNCQILHVEQEvvgddttALQcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 390 ------FDEQMKVIDVVQDIAEVIELGNG---------------------KRLT----------ASQFLQHFLFTPETQH 432
Cdd:PLN03073 260 iertqlLEEEAQLVAQQRELEFETETGKGkgankdgvdkdavsqrleeiyKRLElidaytaearAASILAGLSFTPEMQV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 433 SYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQgD 512
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ-K 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 513 IRDFPGNYTRYRdwkdaKAAQEREKEKEAAKAQEEKTA--------KVRLNEKR 558
Cdd:PLN03073 419 LVTYKGDYDTFE-----RTREEQLKNQQKAFESNERSRshmqafidKFRYNAKR 467
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-303 |
1.16e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-------------GDLVLFE--------NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS 65
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalKGLFRREyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 66 ------FRRdiRVGYLEQ-------------DpqypeeLTVLEacfhhgnsTVELIKE-YercmetdghpgldgilaRMD 125
Cdd:COG4586 81 vlgyvpFKR--RKEFARRigvvfgqrsqlwwD------LPAID--------SFRLLKAiY-----------------RIP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 126 HEkawEYEQKAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT----EWLEDYLRRT 200
Cdd:COG4586 128 DA---EYKKRLDELVELLDLGELlDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKeairEFLKEYNRER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 201 NLTLLMVTHDryfLD---RVCSEIIEIDNRRIyQYKGNysyyLEKREERIEA-KTVEIERANNLYRTELEWMRRMPQARG 276
Cdd:COG4586 205 GTTILLTSHD---MDdieALCDRVIVIDHGRI-IYDGS----LEELKERFGPyKTIVLELAEPVPPLELPRGGEVIEREG 276
|
330 340
....*....|....*....|....*..
gi 2524717128 277 HKARYREDAFYELEKVAKQRFNNDNVK 303
Cdd:COG4586 277 NRVRLEVDPRESLAEVLARLLARYPVR 303
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-222 |
1.42e-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: 86.38 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 12 NLTKSFGDLVLfeNISFG-LSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFrrDIRVGYleqDPQYPE---ELTV 87
Cdd:COG1245 346 DLTKSYGGFSL--EVEGGeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISY---KPQYISpdyDGTV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 88 LEAcfhhgnstveLIKEYERCMETdghpgldgilarmdhekAWEYEQkakqILSQLKIRD-FNQQVKSLSGGQLKRVALA 166
Cdd:COG1245 419 EEF----------LRSANTDDFGS-----------------SYYKTE----IIKPLGLEKlLDKNVKDLSGGELQRVAIA 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 167 NTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-232 |
1.52e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.81 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF----------------------GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS 65
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 66 FRRDIR------VGYleqDPqypeELTVLE----ACFHHGNSTVELIKEYERCMEtdghpgldgilarmdhekaweyeqk 135
Cdd:cd03220 81 VRGRVSsllglgGGF---NP----ELTGREniylNGRLLGLSRKEIDEKIDEIIE------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 136 akqiLSQLKiRDFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPT----NHLDLDMTEWLEDyLRRTNLTLLMVTHDR 211
Cdd:cd03220 129 ----FSELG-DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQRRLRE-LLKQGKTVILVSHDP 202
|
250 260
....*....|....*....|.
gi 2524717128 212 YFLDRVCSEIIEIDNRRIYQY 232
Cdd:cd03220 203 SSIKRLCDRALVLEKGKIRFD 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
317-509 |
1.92e-17 |
|
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: 81.43 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV-----RFGYYSQDgLQF 390
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQR-RSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 DEQMKVidvvqDIAEVIELGN------GKRLTASQF-----------LQHFLftpetqHSYVYKLSGGERRRLYLCTVLM 453
Cdd:cd03235 80 DRDFPI-----SVRDVVLMGLyghkglFRRLSKADKakvdealervgLSELA------DRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 454 RNPNFLVLDEPTNDLDIVTLNVLEEYLR--NFKGC-VIVVSHDRYFMDKVVDHLLVFNG 509
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRelRREGMtILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-209 |
1.94e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrdirvGYLEQDPQYPE---- 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD-----GGDIDDPDVAEachy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 84 ---------ELTVLE-----ACFHHGNstvelikeyercmETDGHPGLDGI-LARMDHEKAweyeqkakqilsqlkirdf 148
Cdd:PRK13539 78 lghrnamkpALTVAEnlefwAAFLGGE-------------ELDIAAALEAVgLAPLAHLPF------------------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 149 nqqvKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTH 209
Cdd:PRK13539 126 ----GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhlaQGGIVIAATH 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-210 |
2.39e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.36 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNsILQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------- 66
Cdd:PRK10584 1 MPAEN-IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmde 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 --RRDIR---VGYLEQDPQYPEELTVLEacfhhgnsTVELikeyercmetdghPGLdgilarMDHEKAWEYEQKAKQILS 141
Cdd:PRK10584 80 eaRAKLRakhVGFVFQSFMLIPTLNALE--------NVEL-------------PAL------LRGESSRQSRNGAKALLE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 142 QLKI-RDFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYL----RRTNLTLLMVTHD 210
Cdd:PRK10584 133 QLGLgKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-210 |
2.41e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI----------RVGYLEQ 77
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgLDVattpsrelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEELTVLE-ACF-----HHGNSTVElikeyercmetdghpgldgilarmDHEKAWEYeqkakqiLSQLKIRDF-NQ 150
Cdd:COG4604 83 ENHINSRLTVRElVAFgrfpySKGRLTAE------------------------DREIIDEA-------IAYLDLEDLaDR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:COG4604 132 YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-210 |
2.76e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGD-----LVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF----------RRdi 70
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpqPAL-QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtgpgaDR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 rvGYLEQDPQYPEELTVLEacfhhgnsTVELikeyercmetdghpGLDgiLARMDHEkawEYEQKAKQILSQLKIRDF-N 149
Cdd:COG4525 79 --GVVFQKDALLPWLNVLD--------NVAF--------------GLR--LRGVPKA---ERRARAEELLALVGLADFaR 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:COG4525 130 RRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQRTGKGVFLITHS 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-231 |
3.74e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.23 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfrrdirvgyleqdpqypee 84
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 ltvleacFHHG-NSTVELIKEYERCM--------------ETDGHpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRDF- 148
Cdd:PRK11432 64 -------FIDGeDVTHRSIQQRDICMvfqsyalfphmslgENVGY-GL-----KMLGVPKEERKQRVKEALELVDLAGFe 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEI 224
Cdd:PRK11432 131 DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
....*..
gi 2524717128 225 DNRRIYQ 231
Cdd:PRK11432 211 NKGKIMQ 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-217 |
5.09e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSF--GDLV--LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-------------- 67
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakae 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 -RDIRVGYLEQdpqypeeltvleacFHHgnstveLIKEYErCMETDGHPGLDGilarmdHEKAWEYEQKAKQILSQLKIR 146
Cdd:PRK11629 84 lRNQKLGFIYQ--------------FHH------LLPDFT-ALENVAMPLLIG------KKKPAEINSRALEMLAAVGLE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 147 DFNQQVKS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFLDRV 217
Cdd:PRK11629 137 HRANHRPSeLSGGERQRVAIARALVNNPRLVLADEPTGNLDArnadSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-181 |
5.58e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI-------R----V 72
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgEDIthlpmhkRarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPQYPEELTVLEacfhhgNstVELIKEyercmetdghpgldgiLARMDHEkawEYEQKAKQILSQL---KIRDfn 149
Cdd:COG1137 81 GYLPQEASIFRKLTVED------N--ILAVLE----------------LRKLSKK---EREERLEELLEEFgitHLRK-- 131
|
170 180 190
....*....|....*....|....*....|..
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEP 181
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-181 |
9.22e-17 |
|
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: 79.89 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------------RRDIRVGYL 75
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditklpmhkRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEacfhhgnstvelikeyercmetdghpGLDGILARMDHEKAwEYEQKAKQILSQLKIRDF-NQQVKS 154
Cdd:cd03218 81 PQEASIFRKLTVEE--------------------------NILAVLEIRGLSKK-EREEKLEELLEEFHITHLrKSKASS 133
|
170 180
....*....|....*....|....*..
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEP 181
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-209 |
1.26e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 78.03 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDL--VLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI--------SFRRDI---RVGY 74
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDpqypeeltvleacfhhgnstVELikeyercmetdghpgLDGILArmdhekaweyeqkaKQILSqlkirdfnqqvks 154
Cdd:cd03246 81 LPQD--------------------DEL---------------FSGSIA--------------ENILS------------- 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 155 lsGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL---TLLMVTH 209
Cdd:cd03246 99 --GGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAH 154
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
330-499 |
1.73e-16 |
|
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: 83.34 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG---------ETVR--FGYYSQDGLQFDEqmkvid 398
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDgidlrqidpASLRrqIGVVLQDVFLFSG------ 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 399 vvqDIAEVIELGNG-----------KRLTASQFLQHFlftPETQHSYVY----KLSGGERRRLYLCTVLMRNPNFLVLDE 463
Cdd:COG2274 564 ---TIRENITLGDPdatdeeiieaaRLAGLHDFIEAL---PMGYDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 464 PTNDLDIVTLNVLEEYLRN-FKGC-VIVVSH--------DR-YFMDK 499
Cdd:COG2274 638 ATSALDAETEAIILENLRRlLKGRtVIIIAHrlstirlaDRiIVLDK 684
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-230 |
2.05e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.06 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGD---LVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRR---------DIR- 71
Cdd:PRK13635 3 EEIIRVEHISFRYPDaatYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwDVRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 -VGYLEQDP--QYPeeltvleacfhhgNSTVEliKEYERCMETDGHPgLDGILARMDhekaweyeqkakQILSQLKIRDF 148
Cdd:PRK13635 82 qVGMVFQNPdnQFV-------------GATVQ--DDVAFGLENIGVP-REEMVERVD------------QALRQVGMEDF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 -NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfLDRVCS--EI 221
Cdd:PRK13635 134 lNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD---LDEAAQadRV 210
|
....*....
gi 2524717128 222 IEIDNRRIY 230
Cdd:PRK13635 211 IVMNKGEIL 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-222 |
2.46e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.55 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLfeNISFG-LSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFrrDIRVGYleqDPQYpeel 85
Cdd:PRK13409 340 LVEYPDLTKKLGDFSL--EVEGGeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISY---KPQY---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 tvLEACFhhgNSTVELIkeyercmetdghpgLDGILARMDheKAWEYEQkakqILSQLKIRD-FNQQVKSLSGGQLKRVA 164
Cdd:PRK13409 409 --IKPDY---DGTVEDL--------------LRSITDDLG--SSYYKSE----IIKPLQLERlLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 165 LANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-207 |
2.70e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 78.49 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDL-VLFeNISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR-----------V 72
Cdd:COG0410 2 PMLEVENLHAGYGGIhVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDITglpphriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLeqdpqyPEE------LTVLE----ACFHHGnstvelikeyercmetdGHPGLDGILARMdhekaweYEqkakqILSQ 142
Cdd:COG0410 81 GYV------PEGrrifpsLTVEEnlllGAYARR-----------------DRAEVRADLERV-------YE-----LFPR 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 143 LKIRdFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTnhLDL------DMTEWLEDyLRRTNLTLLMV 207
Cdd:COG0410 126 LKER-RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS--LGLapliveEIFEIIRR-LNREGVTILLV 192
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-225 |
2.95e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.60 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 13 LTKSFGDLVLfeNISFG-LSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDiRVGYleqDPQYpeeltvLEAC 91
Cdd:cd03237 6 MKKTLGEFTL--EVEGGsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSY---KPQY------IKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 92 FhhgNSTVELIkeyercmetdghpgLDGILARMDHEKAWEYEqkakqILSQLKIRD-FNQQVKSLSGGQLKRVALANTLI 170
Cdd:cd03237 74 Y---EGTVRDL--------------LSSITKDFYTHPYFKTE-----IAKPLQIEQiLDREVPELSGGELQRVAIAACLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 171 TEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEID 225
Cdd:cd03237 132 KDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-217 |
3.56e-16 |
|
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: 77.18 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGY--DSGTISFRRdirvgyleqdpqypEEL 85
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKG--------------EDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEAcfhhgnstvelikeYERcmetdghpgldgilARMDHEKAWEYEQKakqiLSQLKIRDFNQQV-KSLSGGQLKRVA 164
Cdd:cd03217 67 TDLPP--------------EER--------------ARLGIFLAFQYPPE----IPGVKNADFLRYVnEGFSGGEKKRNE 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 165 LANTLITEPDLLILDEPTNHLDLDMTEWLED---YLRRTNLTLLMVTHDRYFLDRV 217
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYI 170
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-218 |
3.64e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------------RR 68
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararlaRA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 69 diRVGYLEQDPQYPEELTVLEACFHHGnstvELIKEYERCMETDGHPGLDgiLARMdhekaweyEQKAkqilsqlkirdf 148
Cdd:PRK13536 115 --RIGVVPQFDNLDLEFTVRENLLVFG----RYFGMSTREIEAVIPSLLE--FARL--------ESKA------------ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVC 218
Cdd:PRK13536 167 DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSllaRGKTILLTTHFMEEAERLC 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-209 |
3.89e-16 |
|
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: 78.08 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYD---SGTISFR---RDI---- 70
Cdd:cd03234 1 QRVLPWWDVGLKAknwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqpRKPdqfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 -RVGYLEQDPQYPEELTVLEACFHhgnsTVELikeyercmetdghpgldgilaRMDHEKAWEYEQK--AKQILSQLKIRD 147
Cdd:cd03234 81 kCVAYVRQDDILLPGLTVRETLTY----TAIL---------------------RLPRKSSDAIRKKrvEDVLLRDLALTR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 148 F-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRtNLTLLMVTH 209
Cdd:cd03234 136 IgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARR-NRIVILTIH 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-263 |
5.17e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS--------------FRRD 69
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShiellgrtvqregrLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IR-----VGYLEQDPQYPEELTVLEACFHHGNSTVELikeYERCMEtdghpgldgilarmdhekaW---EYEQKAKQILS 141
Cdd:PRK09984 81 IRksranTGYIFQQFNLVNRLSVLENVLIGALGSTPF---WRTCFS-------------------WftrEQKQRALQALT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 142 QLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLLMVTHDRYFLDR 216
Cdd:PRK09984 139 RVGMVHFaHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndgITVVVTLHQVDYALR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2524717128 217 VCSEIIEIDNRRIYqYKGNYSYYlekreerieaktvEIERANNLYRT 263
Cdd:PRK09984 219 YCERIVALRQGHVF-YDGSSQQF-------------DNERFDHLYRS 251
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
317-506 |
6.26e-16 |
|
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: 77.71 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV-------------RFGY 382
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDItglsekelyelrrRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 YSQDGLQFDEqMKVIDVVQ---------DIAEVIELGNGKrltasqfLQHF-LftPETQHSYVYKLSGGERRRLYLCTVL 452
Cdd:COG1127 87 LFQGGALFDS-LTVFENVAfplrehtdlSEAEIRELVLEK-------LELVgL--PGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 453 MRNPNFLVLDEPTNDLDIVTLNVLEEYLRN----FKGCVIVVSHDRYFMDKVVDHLLV 506
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVAV 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-513 |
9.34e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.44 E-value: 9.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 27 SFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSG--TISFRRDIRVGyLEQDPQypeeltVLEACFHHGNStvELIKE 104
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerQSQFSHITRLS-FEQLQK------LVSDEWQRNNT--DMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 105 YErcmETDGHPGLDGILarMDHEKAWEYEQKAKQI-LSQLKIRDFnqqvKSLSGGQLKRVALANTLITEPDLLILDEPTN 183
Cdd:PRK10938 94 GE---DDTGRTTAEIIQ--DEVKDPARCEQLAQQFgITALLDRRF----KYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 184 HLDL----DMTEWLEDyLRRTNLTLLMVthdryfLDRVcSEIIEidnrrIYQYKG---NYSYYLEKREERIEAKTV--EI 254
Cdd:PRK10938 165 GLDVasrqQLAELLAS-LHQSGITLVLV------LNRF-DEIPD-----FVQFAGvlaDCTLAETGEREEILQQALvaQL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 255 ERANNLYRTELewmrrmPQARGHKARYR--EDAfyelekvAKQRFNNDNVkldvkasyigskifeadhlykSFGDLKILD 332
Cdd:PRK10938 232 AHSEQLEGVQL------PEPDEPSARHAlpANE-------PRIVLNNGVV---------------------SYNDRPILH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 333 DFSYIFARYEKMGIVGNNGTGKSTFIKILM-RHEQA----------DRGAldiGETV-----RFGYYS-QDGLQFDEQMK 395
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITgDHPQGysndltlfgrRRGS---GETIwdikkHIGYVSsSLHLDYRVSTS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 396 VIDVV-----QDIAEVIELGNGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDi 470
Cdd:PRK10938 355 VRNVIlsgffDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD- 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2524717128 471 vTLN------VLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQGDI 513
Cdd:PRK10938 434 -PLNrqlvrrFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGDI 481
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-237 |
1.03e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLT-KSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYD-SGTI-----------SFRRDIrvGY 74
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQgSLKIngielreldpeSWRKHL--SW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEElTVLEacfhhgNSTVelikeyercmetdGHPGLDgilarmdhekaweyEQKAKQILSQLKIRDF------ 148
Cdd:PRK11174 428 VGQNPQLPHG-TLRD------NVLL-------------GNPDAS--------------DEQLQQALENAWVSEFlpllpq 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 --NQQVK----SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTnlTLLMVTHDRYFLDRvC 218
Cdd:PRK11174 474 glDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHseqlVMQALNAASRRQ--TTLMVTHQLEDLAQ-W 550
|
250
....*....|....*....
gi 2524717128 219 SEIIEIDNRRIYQyKGNYS 237
Cdd:PRK11174 551 DQIWVMQDGQIVQ-QGDYA 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
342-515 |
1.06e-15 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.47 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 342 EKMGIVGNNGTGKSTFIKILMRHEQADRGA-----LDIGE----TVR--FGYYSQDGLQFDEQMKvidvvqdiaEVIELG 410
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgTDIRQldpaDLRrnIGYVPQDVTLFYGTLR---------DNITLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 411 NG-----KRLTASQFLQHFLFTPETQHSYVYK-------LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEE 478
Cdd:cd03245 102 APladdeRILRAAELAGVTDFVNKHPNGLDLQigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKE 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524717128 479 YLRNFKG--CVIVVSHdRYFMDKVVDHLLVFNGQGDIRD 515
Cdd:cd03245 182 RLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-210 |
1.09e-15 |
|
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: 78.99 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 12 NLTKSFGDLVLfeNISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-----------------RRdiRVGY 74
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsargiflpphRR--RIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLeacfhhGNstveLikEY--ERCMETDGHPGLDGILARMDhekaweyeqkakqiLSQLkirdFNQQV 152
Cdd:COG4148 82 VFQEARLFPHLSVR------GN----L--LYgrKRAPRAERRISFDEVVELLG--------------IGHL----LDRRP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:COG4148 132 ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLERLRDELDIPILYVSHS 193
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-227 |
1.41e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDL-VLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEElT 86
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLG-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLEA-CFHHGNSTV---ELIKEYERCmetdghpGLDGILARMDHEKAWEyeqkakqilsqlkirdfnqqvKSLSGGQLKR 162
Cdd:COG4178 442 LREAlLYPATAEAFsdaELREALEAV-------GLGHLAERLDEEADWD---------------------QVLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT--NLTLLMVTHdRYFLDRVCSEIIEIDNR 227
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-209 |
1.41e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR---RDIR---------VGY 74
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpVRIRsprdaialgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEacfhhgNstVELikeyercmetdGHPGLDGIlaRMDHEKAweyEQKAKQILSQ--LKIrDFNQQV 152
Cdd:COG3845 85 VHQHFMLVPNLTVAE------N--IVL-----------GLEPTKGG--RLDRKAA---RARIRELSERygLDV-DPDAKV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTH 209
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRlaaEGKSIIFITH 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
317-508 |
1.42e-15 |
|
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: 76.32 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGyySQD--GLQFDE-- 392
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG------SVLFD--GEDitGLPPHEia 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 ---------------QMKVIDVVQdIAEVIELGNGKRLTASQF-----------------LQHFLFTPetqhsyVYKLSG 440
Cdd:cd03219 74 rlgigrtfqiprlfpELTVLENVM-VAAQARTGSGLLLARARReereareraeellervgLADLADRP------AGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 441 GERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK--GC-VIVVSHDryfMD---KVVDHLLVFN 508
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRerGItVLLVEHD---MDvvmSLADRVTVLD 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
330-528 |
1.53e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 79.81 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG---------ETVR--FGYYSQDGLQF-------- 390
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeDDLRrrIAVVPQRPHLFdttlrenl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 --------DEQM-KVIDVVQdiaevielgngkrltasqfLQHFLFT-PETQHSYVY----KLSGGERRRLYLCTVLMRNP 456
Cdd:COG4987 430 rlarpdatDEELwAALERVG-------------------LGDWLAAlPDGLDTWLGeggrRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 457 NFLVLDEPTNDLDIVT----LNVLEEYLRNfKGcVIVVSHDRYFMDKvVDHLLVF-NG----QGDIRDFPGNYTRYRDWK 527
Cdd:COG4987 491 PILLLDEPTEGLDAATeqalLADLLEALAG-RT-VLLITHRLAGLER-MDRILVLeDGriveQGTHEELLAQNGRYRQLY 567
|
.
gi 2524717128 528 D 528
Cdd:COG4987 568 Q 568
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
317-484 |
2.03e-15 |
|
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: 75.87 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG--------ETVR--FGYYSQD 386
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvrepREVRrrIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 gLQFDEQMKVIDVVQDIAEVIELGNGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:cd03265 82 -LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170
....*....|....*...
gi 2524717128 467 DLDIVTLNVLEEYLRNFK 484
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLK 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-210 |
2.13e-15 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 76.70 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF--GDLVLFENISFGLSEGQRVGLIAKNGSGKSTL---LNIL----SGK---EGYDSGTISFRRDIR--VG 73
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLllptSGKvtvDGLDTLDEENLWEIRkkVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDP--QYpeeltVleacfhhgNSTVElikeyercmeTDGHPGLDGIlaRMDHEkawEYEQKAKQILSQLKIRDF-NQ 150
Cdd:TIGR04520 81 MVFQNPdnQF-----V--------GATVE----------DDVAFGLENL--GVPRE---EMRKRVDEALKLVGMEDFrDR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:TIGR04520 133 EPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrKEVLETIRKLNKEEGITVISITHD 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-210 |
2.29e-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: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI--------SFRRDI---RVGYL 75
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDEvrrRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPqypeeltvleacfHHGNSTVelikeyercmetdghpgLDGI-LARMD--HEKAWEYEQKAKqiLSQLkIRDFNQQV 152
Cdd:TIGR02868 415 AQDA-------------HLFDTTV-----------------RENLrLARPDatDEELWAALERVG--LADW-LRALPDGL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 --------KSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRtnLTLLMVTHD 210
Cdd:TIGR02868 462 dtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDaetaDELLEDLLAALSG--RTVVLITHH 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-246 |
2.45e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfrrdiRVGYLEQDPQYP--E 83
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI------RVGDITIDTARSlsQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 84 ELTVLEAC-------------FHHgNSTVELIKEyercmetdghpgldG--ILARMDHEKAweyEQKAKQILSQLKIR-D 147
Cdd:PRK11264 76 QKGLIRQLrqhvgfvfqnfnlFPH-RTVLENIIE--------------GpvIVKGEPKEEA---TARARELLAKVGLAgK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT-EWLEDY--LRRTNLTLLMVTHDRYFLDRVCSEIIEI 224
Cdd:PRK11264 138 ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
250 260
....*....|....*....|..
gi 2524717128 225 DNRRIYQYKGNYSYYLEKREER 246
Cdd:PRK11264 218 DQGRIVEQGPAKALFADPQQPR 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
324-509 |
2.60e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDgLQFDEQ--------MK 395
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-LYLDTTlpltvnrfLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 396 VIDVVQ--DIAEVIelgngKRLTASQFLQHFLftpetqhsyvYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI--- 470
Cdd:PRK09544 92 LRPGTKkeDILPAL-----KRVQAGHLIDAPM----------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngq 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524717128 471 VTLNVLEEYLRNFKGC-VIVVSHDRYFMDKVVDHLLVFNG 509
Cdd:PRK09544 157 VALYDLIDQLRRELDCaVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
317-494 |
3.29e-15 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 74.86 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV--------RFGYYSQDG 387
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFDeQMKVIDvvqDIAEVIELGNGKRLT----ASQFLQHFLFTPETQHsYVYKLSGGERRRLYLCTVLMRNPNFLVLDE 463
Cdd:cd03259 82 ALFP-HLTVAE---NIAFGLKLRGVPKAEirarVRELLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2524717128 464 PTNDLD----IVTLNVLEEYLRNFKGCVIVVSHDR 494
Cdd:cd03259 157 PLSALDaklrEELREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-515 |
5.13e-15 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 74.18 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 320 HLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRG--ALDIGETVRF--------------GYY 383
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeiTFDGKSYQKNiealrrigalieapGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 sqDGLQFDEQMKVIDVV-----QDIAEVIELGNgkrltasqfLQHflftpeTQHSYVYKLSGGERRRLYLCTVLMRNPNF 458
Cdd:cd03268 85 --PNLTARENLRLLARLlgirkKRIDEVLDVVG---------LKD------SAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 459 LVLDEPTNDLDIVTLNVLEEYLRNFK--GC-VIVVSHDRYFMDKVVDHLLVFNgQGDIRD 515
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRdqGItVLISSHLLSEIQKVADRIGIIN-KGKLIE 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-210 |
5.17e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrDIRV-------GYLEQDP 79
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-GKPVegpgaerGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYPEELTVLEacfhhgnsTVELikeyercmetdghpGLDgiLARMDHEkawEYEQKAKQILSQLKIRDFNQQ-VKSLSGG 158
Cdd:PRK11248 80 GLLPWRNVQD--------NVAF--------------GLQ--LAGVEKM---QRLEIAHQMLKKVGLEGAEKRyIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 159 QLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAftreQMQTLLLKLWQETGKQVLLITHD 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-217 |
5.54e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGY--DSGTISFR-RDIrvgyLEQDP----- 79
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDgEDI----LELSPderar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 -------QYPEELTvleacfhhGNSTVELIKEyercmetdghpgldGILARMDHE-KAWEYEQKAKQILSQLKI------ 145
Cdd:COG0396 77 agiflafQYPVEIP--------GVSVSNFLRT--------------ALNARRGEElSAREFLKLLKEKMKELGLdedfld 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 146 RDFNqqvKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDyLRRTNLTLLMVTHDRYFLDRV 217
Cdd:COG0396 135 RYVN---EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDalriVAEGVNK-LRSPDRGILIITHYQRILDYI 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
316-493 |
7.68e-15 |
|
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: 74.14 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGEtVRFG---YYSQDGLQFDE 392
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGE-VLLDgkdIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 QMKVIDVVQ-------DIAEVIELG---NGKRLTAS------QFLQHFLFTPET-QHSYVYKLSGGERRRLYLCTVLMRN 455
Cdd:cd03260 80 RRRVGMVFQkpnpfpgSIYDNVAYGlrlHGIKLKEElderveEALRKAALWDEVkDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524717128 456 PNFLVLDEPTNDLDIVTLNVLEEYLRNFKG--CVIVVSHD 493
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-218 |
9.80e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILS-------GKEGYDSGTI----SFRRD 69
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIqhyaSKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IRVGYLEQDPQYPEELTVLEACFHHGNSTVELIKEYercmetdghpgldgilaRMDHEKAWEYEQKAKQIlSQLKirdfN 149
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRW-----------------RKEDEEAVTKAMQATGI-THLA----D 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfLDRVC 218
Cdd:PRK10253 139 QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQAC 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
317-493 |
1.34e-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: 73.00 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFAryEKM-GIVGNNGTGKSTFIKILMRHEQADRGAL-----DIGETV-----RFGYYSQ 385
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLG--PGMyGLLGPNGAGKTTLMRILATLTPPSSGTIridgqDVLKQPqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 386 DgLQFDEQMKVIDVVQDIAEVIELGNGK-RLTASQFLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEP 464
Cdd:cd03264 80 E-FGVYPNFTVREFLDYIAWLKGIPSKEvKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 2524717128 465 TNDLD----IVTLNVLEEYLRNfkGCVIVVSHD 493
Cdd:cd03264 158 TAGLDpeerIRFRNLLSELGED--RIVILSTHI 188
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-229 |
1.41e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 74.07 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLL---NILsgkEGYDSGTISFR------RDIRVGYLE-Q 77
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLrciNLL---ETPDSGEIRVGgeeirlKPDRDGELVpA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 DPQYPEEL-TVLEACFHHGN----STVelikeYERCMETDGHpgldgILARmdhEKAwEYEQKAKQILSQLKIRDFNQQV 152
Cdd:COG4598 86 DRRQLQRIrTRLGMVFQSFNlwshMTV-----LENVIEAPVH-----VLGR---PKA-EAIERAEALLAKVGLADKRDAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDldmTEWLEDYLR---------RtnlTLLMVTHDRYFLDRVCSEII 222
Cdd:COG4598 152 PAhLSGGQQQRAAIARALAMEPEVMLFDEPTSALD---PELVGEVLKvmrdlaeegR---TMLVVTHEMGFARDVSSHVV 225
|
....*..
gi 2524717128 223 EIDNRRI 229
Cdd:COG4598 226 FLHQGRI 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-210 |
1.81e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVnsilQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsFRRDIRVGYLEQDPQ 80
Cdd:PRK11000 1 MASV----TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 -----------YPEeLTVLEacfhhgNSTVelikeyercmetdghpGLDgiLARMDheKAwEYEQKAKQILSQLKIRDF- 148
Cdd:PRK11000 76 gvgmvfqsyalYPH-LSVAE------NMSF----------------GLK--LAGAK--KE-EINQRVNQVAEVLQLAHLl 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:PRK11000 128 DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-231 |
1.92e-14 |
|
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: 72.59 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 27 SFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-----------FRRDirVGYLEQDPQYPEELTVLEacfhhg 95
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKvndqshtglapYQRP--VSMLFQENNLFAHLTVRQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 96 NSTVELikeyercmetdgHPGLdgilaRMDHEKaweyEQKAKQILSQLKIRDFNQQV-KSLSGGQLKRVALANTLITEPD 174
Cdd:TIGR01277 90 NIGLGL------------HPGL-----KLNAEQ----QEKVVDAAQQVGIADYLDRLpEQLSGGQRQRVALARCLVRPNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 175 LLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQ 231
Cdd:TIGR01277 149 ILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKV 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-217 |
2.41e-14 |
|
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: 75.88 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-----------GDLVLFENISFGLSEGQRVGLIAKNGSGKSTL----LNILSGkegydSGTISF----- 66
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFdgqdl 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 -----------RRDIRVGYleQDPqY----PEeLTVLEacfhhgnstveLIKEyercmetdG----HPGLDGIlarmdhe 127
Cdd:COG4172 350 dglsrralrplRRRMQVVF--QDP-FgslsPR-MTVGQ-----------IIAE--------GlrvhGPGLSAA------- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 128 kawEYEQKAKQILSQ--LKIRDFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNhlDLDMT------EWLEDYLRR 199
Cdd:COG4172 400 ---ERRARVAEALEEvgLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS--ALDVSvqaqilDLLRDLQRE 474
|
250 260
....*....|....*....|..
gi 2524717128 200 TNLTLLMVTHD----RYFLDRV 217
Cdd:COG4172 475 HGLAYLFISHDlavvRALAHRV 496
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
315-515 |
2.42e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.99 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRG-------ALDIGETVRFGY----- 382
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGevlwdgePLDPEDRRRIGYlpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 --YSqdglqfdeQMKVIDVVQDIAEVielgngKRLTASQFLQ--HFLFT----PETQHSYVYKLSGGERRRLYLCTVLMR 454
Cdd:COG4152 81 glYP--------KMKVGEQLVYLARL------KGLSKAEAKRraDEWLErlglGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 455 NPNFLVLDEPTNDLDIVTLNVLEEYLRNFK--G-CVIVVSHDryfMDKV---VDHLLVFNG-----QGDIRD 515
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAakGtTVIFSSHQ---MELVeelCDRIVIINKgrkvlSGSVDE 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-222 |
2.44e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.39 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGD----LVLFENISFGLSEGQRVGLIAKNGSGKS-TLLNILS-----GK--------EGYDSGTISF- 66
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGlidypGRvmaeklefNGQDLQRISEk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 -RRDI---RVGYLEQDPqypeeLTVLEACFHHGNSTVELIKEyercmetdgHPGldgilarmdHEKAWEYeQKAKQILSQ 142
Cdd:PRK11022 82 eRRNLvgaEVAMIFQDP-----MTSLNPCYTVGFQIMEAIKV---------HQG---------GNKKTRR-QRAIDLLNQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 143 LKIRDFNQQVK----SLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFL 214
Cdd:PRK11022 138 VGIPDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALV 217
|
....*...
gi 2524717128 215 DRVCSEII 222
Cdd:PRK11022 218 AEAAHKII 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-209 |
2.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFglSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-RRDIRVGYLEQDP-----------QYPE----ELTVL 88
Cdd:PRK13634 27 NVSI--PSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLkplrkkvgivfQFPEhqlfEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 89 -EACFHHGNSTVElikeyercmetdghpgldgilarmdHEKAweyEQKAKQILsqlKIRDFNQQV--KS---LSGGQLKR 162
Cdd:PRK13634 105 kDICFGPMNFGVS-------------------------EEDA---KQKAREMI---ELVGLPEELlaRSpfeLSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTH 209
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-493 |
4.14e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKS-TLLNIL-----SGKEGYDSGTISFRRDIRVG 73
Cdd:PRK10261 9 ARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLLRRRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPQ--------------YPEELTVLEACFHHGNSTVELIKEyercmetdgHPGLDgilarmdHEKAWeyeQKAKQI 139
Cdd:PRK10261 89 ELSEQSAaqmrhvrgadmamiFQEPMTSLNPVFTVGEQIAESIRL---------HQGAS-------REEAM---VEAKRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 140 LSQLKIRDfNQQVKS-----LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR----RTNLTLLMVTHD 210
Cdd:PRK10261 150 LDQVRIPE-AQTILSryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 211 RyfldrvcSEIIEIDNRRIYQYKGnysyylekreERIEAKTVE-IERA--NNLYRTELEWMRRMPQARGHK--ARYREDA 285
Cdd:PRK10261 229 M-------GVVAEIADRVLVMYQG----------EAVETGSVEqIFHApqHPYTRALLAAVPQLGAMKGLDypRRFPLIS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 286 FYELEKVAKQRFNNDNVKldvkasyiGSKIFEADHLYKSFG-----------DLKILDDFSYIFARYEKMGIVGNNGTGK 354
Cdd:PRK10261 292 LEHPAKQEPPIEQDTVVD--------GEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 355 STFIKILMRHEQADRGALdIGETVRFGYYSQDGLQ----------------FDEQMKVIDVVQDIAEVIELGNGK--RLT 416
Cdd:PRK10261 364 STTGRALLRLVESQGGEI-IFNGQRIDTLSPGKLQalrrdiqfifqdpyasLDPRQTVGDSIMEPLRVHGLLPGKaaAAR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 417 ASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSH 492
Cdd:PRK10261 443 VAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIrgqiINLLLDLQRDFGIAYLFISH 522
|
.
gi 2524717128 493 D 493
Cdd:PRK10261 523 D 523
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-217 |
5.45e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-FRRDIRvgyleqdpQY-PEEL 85
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlNGRPLA--------DWsPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 ----------TVLEACFhhgnsTVELIKEyercmetdghpgldgiLARMDHEkawEYEQKAKQI---------LSQLKIR 146
Cdd:PRK13548 75 arrravlpqhSSLSFPF-----TVEEVVA----------------MGRAPHG---LSRAEDDALvaaalaqvdLAHLAGR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 147 DFNQqvksLSGGQLKRVALANTL--ITEPD----LLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHD-----R 211
Cdd:PRK13548 131 DYPQ----LSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaR 206
|
....*.
gi 2524717128 212 YfLDRV 217
Cdd:PRK13548 207 Y-ADRI 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-226 |
6.09e-14 |
|
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: 69.88 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLT--KSFGDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEel 85
Cdd:cd03223 1 IELENLSlaTPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 tvleacfhhGNstvelikeyercmetdghpgLDGILARmdhekAWEyeqkakqilsqlkirdfnqqvKSLSGGQLKRVAL 165
Cdd:cd03223 78 ---------GT--------------------LREQLIY-----PWD---------------------DVLSGGEQQRLAF 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 166 ANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHdRYFLDRVCSEIIEIDN 226
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-229 |
7.20e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI----------RVGYLE 76
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgDDVealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 QDpqypeelTVLEACFhhgnsTVELIKEYERcmetdgHPGLdGILARMDHEKaweyEQKAKQILSQLKIRDF-NQQVKSL 155
Cdd:PRK09536 84 QD-------TSLSFEF-----DVRQVVEMGR------TPHR-SRFDTWTETD----RAAVERAMERTGVAQFaDRPVTSL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLDLD---MTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINhqvRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-209 |
7.78e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.39 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFE-----NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-----------RDIR 71
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkkvklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 --VGYLEQDPQYP--EELTVLEACF---HHGNSTVELIKEYERCMETdghPGLDgilarmdhekaweYEqkakqilsqlK 144
Cdd:PRK13637 83 kkVGLVFQYPEYQlfEETIEKDIAFgpiNLGLSEEEIENRVKRAMNI---VGLD-------------YE----------D 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 145 IRDfnqqvKS---LSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTH 209
Cdd:PRK13637 137 YKD-----KSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSH 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
315-506 |
7.84e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV---------RFGYYS 384
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 385 Q-DGLqfDEQMKVIDVVQDIAEVIELGNGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDE 463
Cdd:PRK13537 87 QfDNL--DPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524717128 464 PTNDLDIVTLNVLEEYLRNF--KGCVIVVShdRYFM---DKVVDHLLV 506
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLlaRGKTILLT--THFMeeaERLCDRLCV 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-211 |
8.92e-14 |
|
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: 72.91 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 38 LIAKNGSGKSTLLNILSGKEGYDSGTISFRRdirvgylEQDPQYPEEL----TVLE--ACFHHgnSTVELIKEYercmet 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG-------EDVTNVPPHLrhinMVFQsyALFPH--MTVEENVAF------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 112 dghpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRDFNQQVKS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLD-- 188
Cdd:TIGR01187 66 ----GL-----KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHqLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlr 136
|
170 180
....*....|....*....|....*
gi 2524717128 189 --MTEWLEDYLRRTNLTLLMVTHDR 211
Cdd:TIGR01187 137 dqMQLELKTIQEQLGITFVFVTHDQ 161
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
317-493 |
9.28e-14 |
|
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: 70.61 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDL--KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGET----------VRFGYYS 384
Cdd:cd03263 2 QIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 385 QDGLQFDEqMKVIDVVQDIAEVIELGNGK-RLTASQFLQHFLFTPEtQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDE 463
Cdd:cd03263 82 QFDALFDE-LTVREHLRFYARLKGLPKSEiKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 2524717128 464 PTNDLDIVT----LNVLEEYLRNfkGCVIVVSHD 493
Cdd:cd03263 160 PTSGLDPASrraiWDLILEVRKG--RSIILTTHS 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-229 |
1.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGD-LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG----------KEGYDSGTISFRRDIR--VG 73
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGllrpqkgkvlVSGIDTGDFSKLQGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPQypeeltvleacfhhgnstVELIKeyeRCMETDGHPGLDGILArmdheKAWEYEQKAKQILSQLKIRDFNQQV- 152
Cdd:PRK13644 81 IVFQNPE------------------TQFVG---RTVEEDLAFGPENLCL-----PPIEIRKRVDRALAEIGLEKYRHRSp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEW-LEDY--LRRTNLTLLMVTHDRYFLdRVCSEIIEIDNRRI 229
Cdd:PRK13644 135 KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAvLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-210 |
1.39e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLF--ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR-- 71
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskenLKEIRkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQDP--QYPeeltvleacfhhgNSTVElikeyercmeTDGHPGLDGIlaRMDHEKAW----EYEQKAkQILSQLKi 145
Cdd:PRK13632 85 IGIIFQNPdnQFI-------------GATVE----------DDIAFGLENK--KVPPKKMKdiidDLAKKV-GMEDYLD- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 146 rdfnQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:PRK13632 138 ----KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-232 |
1.53e-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: 70.79 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDL-VLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR----------VGYL 75
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgEDIReqdpvelrrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEacfhhgnsTVELIkeyercmetdghPGLDGilarmdhekaWE---YEQKAKQILS--QLKIRDFNQ 150
Cdd:cd03295 81 IQQIGLFPHMTVEE--------NIALV------------PKLLK----------WPkekIRERADELLAlvGLDPAEFAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVKS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL----TLLMVTHDRYFLDRVCSEIIEID 225
Cdd:cd03295 131 RYPHeLSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelgkTIVFVTHDIDEAFRLADRIAIMK 210
|
....*..
gi 2524717128 226 NRRIYQY 232
Cdd:cd03295 211 NGEIVQV 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-211 |
1.61e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfrrdirvgYLE-QD- 78
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI---------MLDgQDi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEEL----TVLE--ACFHHgnSTVelikeYERCMEtdghpGLdgilaRMDHEKAWEYEQKAKQILSQLKIRDF-NQQ 151
Cdd:PRK09452 79 THVPAENrhvnTVFQsyALFPH--MTV-----FENVAF-----GL-----RMQKTPAAEITPRVMEALRMVQLEEFaQRK 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDR 211
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
317-501 |
1.68e-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: 69.83 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGD----LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGyySQDGLQFDE 392
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSG------EVRVD--GTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 QMKV------IDVV-QD--------IAEVIEL-----GNGKRLTASQFLQhfLFT----PETQHSYVYKLSGGERRRLYL 448
Cdd:cd03255 74 KELAafrrrhIGFVfQSfnllpdltALENVELplllaGVPKKERRERAEE--LLErvglGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 449 CTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYF---MDKVV 501
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELaeyADRII 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
316-513 |
1.80e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.87 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETV-------------RFGY 382
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 YSQdglQFD--EQMKVIDVV---------QDIAEVIElgngkrlTASQFLQHfLFTPETQHSYVYKLSGGERRRLYLCTV 451
Cdd:cd03262 81 VFQ---QFNlfPHLTVLENItlapikvkgMSKAEAEE-------RALELLEK-VGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 452 LMRNPNFLVLDEPTNDLD--IVT--LNVLEEYLRnfKGC-VIVVSHDRYFMDKVVDHlLVFNGQGDI 513
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDpeLVGevLDVMKDLAE--EGMtMVVVTHEMGFAREVADR-VIFMDDGRI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
326-513 |
2.80e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 72.87 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETvrfgyySQDGLQFDEQMKVIDVV-QD-- 402
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV------DLSDLDPASWRRQIAWVpQNpy 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 403 -----IAEVIELGNG-----------KRLTASQF---LQHFLFTPETQHSYvyKLSGGERRRLYLCTVLMRNPNFLVLDE 463
Cdd:COG4988 422 lfagtIRENLRLGRPdasdeeleaalEAAGLDEFvaaLPDGLDTPLGEGGR--GLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 464 PTNDLDIVT----LNVLEEYLRNfkGCVIVVSHDRYFMdKVVDHLLVFNgQGDI 513
Cdd:COG4988 500 PTAHLDAETeaeiLQALRRLAKG--RTVILITHRLALL-AQADRILVLD-DGRI 549
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
316-464 |
2.86e-13 |
|
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: 69.49 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGET----------VRFG--YY 383
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrARLGigYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 SQDGLQFdEQMKVIDVVQDIAEVIELGNGKRLT-ASQFLQHFLFTPeTQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLD 462
Cdd:cd03218 81 PQEASIF-RKLTVEENILAVLEIRGLSKKEREEkLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 2524717128 463 EP 464
Cdd:cd03218 159 EP 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-218 |
2.88e-13 |
|
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: 72.53 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF-----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR------------ 67
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RDIR------VGYLEQD-PQYPEElTVLEacfhhgNST----VELIKEYER--CMETDGHPGLDgilarmdhekaweyEQ 134
Cdd:TIGR03269 357 PDGRgrakryIGILHQEyDLYPHR-TVLD------NLTeaigLELPDELARmkAVITLKMVGFD--------------EE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 135 KAKQILSQLKirdfnqqvKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:TIGR03269 416 KAEEILDKYP--------DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHD 487
|
....*...
gi 2524717128 211 RYFLDRVC 218
Cdd:TIGR03269 488 MDFVLDVC 495
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
317-492 |
3.09e-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: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLK----ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIgetvrfgyysqDGlqfde 392
Cdd:cd03266 3 TADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-----------DG----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 qmkvIDVVQDIAEV---IELGNG-----KRLTASQFLQHF---------------------LFTPETQHSYVYKLSGGER 443
Cdd:cd03266 67 ----FDVVKEPAEArrrLGFVSDstglyDRLTARENLEYFaglyglkgdeltarleeladrLGMEELLDRRVGGFSTGMR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 444 RRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSH 492
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-210 |
3.15e-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: 71.30 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 12 NLTKSFGDLVLfeNISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDI-------RVGYLE 76
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsRKGIflppekrRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 77 QDPQYPEELTVleacfhHGNstveLIKEYERCMETDGHPGLDGILARMDhekaweyeqkakqiLSQLKIRdfnqQVKSLS 156
Cdd:TIGR02142 82 QEARLFPHLSV------RGN----LRYGMKRARPSERRISFERVIELLG--------------IGHLLGR----LPGRLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 157 GGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHD 210
Cdd:TIGR02142 134 GGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERlhaeFGIPILYVSHS 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-229 |
3.32e-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: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG--DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRdirvgyleqdpqypeel 85
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 tvleacfhhgnstvELIKEYERCMEtdghpgldgilarmdhekaweyeqKAKQILSQlKIRDFNQQVKS-----LSGGQL 160
Cdd:cd03247 64 --------------VPVSDLEKALS------------------------SLISVLNQ-RPYLFDTTLRNnlgrrFSGGER 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 161 KRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRrtNLTLLMVTHDRYFLDRVcSEIIEIDNRRI 229
Cdd:cd03247 105 QRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-217 |
3.40e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG-----DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS--FRRDIRVGYLEQDPQ 80
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 YPEELTVLEACFHHGNSTVELIK---------EY---ERCMETDghpgldgIL---ARMDHEKAwEYEQKAKQIL----- 140
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRrvgvvfqfaEYqlfEQTIEKD-------IIfgpVSMGVSKE-EAKKRAAKYIelvgl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 141 --SQLKIRDFNqqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLeDYLRRTNLTLLMVTHDryfL 214
Cdd:PRK13651 155 deSYLQRSPFE-----LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIF-DNLNKQGKTIILVTHD---L 225
|
...
gi 2524717128 215 DRV 217
Cdd:PRK13651 226 DNV 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
329-510 |
4.43e-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: 67.72 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 329 KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETvrfgyysqdglqfdeqmkvidvvqdiaEVIE 408
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV---------------------------PVSD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 409 LGNGKRLTASQFLQH-FLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNf 483
Cdd:cd03247 69 LEKALSSLISVLNQRpYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLKD- 147
|
170 180
....*....|....*....|....*...
gi 2524717128 484 kGCVIVVSHDRYFMDKvVDHLLVF-NGQ 510
Cdd:cd03247 148 -KTLIWITHHLTGIEH-MDKILFLeNGK 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-182 |
4.59e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGdlvlFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR------RDIR------VGY 74
Cdd:COG1129 256 VLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkpvriRSPRdairagIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LeqdpqyPEE---------LTVLEacfhhgNSTVELIKEYERcmetdghpgldGILARMDHEKAWeyeqkAKQILSQLKI 145
Cdd:COG1129 332 V------PEDrkgeglvldLSIRE------NITLASLDRLSR-----------GGLLDRRRERAL-----AEEYIKRLRI 383
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524717128 146 R--DFNQQVKSLSGG-QLKrVALANTLITEPDLLILDEPT 182
Cdd:COG1129 384 KtpSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPT 422
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-226 |
5.90e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.03 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSgkegydsgtisfrrdiRVGYLeqDPqypeELT 86
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN----------------RMNDL--NP----EVT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLEACFHHGNS-------TVELIKE---------------YERCMEtdghpGL--DGILARMDHEKAWEYEQKAKQILSQ 142
Cdd:PRK14239 63 ITGSIVYNGHNiysprtdTVDLRKEigmvfqqpnpfpmsiYENVVY-----GLrlKGIKDKQVLDEAVEKSLKGASIWDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 143 LKIRDFNQQVkSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLED--YLRRTNLTLLMVTH---------DR 211
Cdd:PRK14239 138 VKDRLHDSAL-GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEEtlLGLKDDYTMLLVTRsmqqasrisDR 216
|
250
....*....|....*..
gi 2524717128 212 --YFLDrvcSEIIEIDN 226
Cdd:PRK14239 217 tgFFLD---GDLIEYND 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-243 |
6.65e-13 |
|
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: 68.80 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD-LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSgkEGYD--SGTI-------------SFRRDIr 71
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF--RFYDvsSGSIlidgqdirevtldSLRRAI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 vGYLEQDpqypeelTVLeacFhhgNSTVELIKEYERCMETDGhpgldgilarmdhekawEYEQKAKQILSQLKIRDFNQQ 151
Cdd:cd03253 78 -GVVPQD-------TVL---F---NDTIGYNIRYGRPDATDE-----------------EVIEAAKAAQIHDKIMRFPDG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKS--------LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHdryfldRV---- 217
Cdd:cd03253 127 YDTivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH------RLstiv 200
|
250 260
....*....|....*....|....*..
gi 2524717128 218 -CSEIIEIDNRRIYQyKGNYSYYLEKR 243
Cdd:cd03253 201 nADKIIVLKDGRIVE-RGTHEELLAKG 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
315-508 |
6.99e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.23 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSF-----GDLKI--LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA---------LDIGE-- 376
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 -----TVR---FGYYSQdglqFdeqMKVI------DVVqdiAE-VIELGNGK---RLTASQFLQHF-----LFT--PETq 431
Cdd:COG4778 84 preilALRrrtIGYVSQ----F---LRVIprvsalDVV---AEpLLERGVDReeaRARARELLARLnlperLWDlpPAT- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 432 hsyvykLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK--GCVIV-VSHDRYFMDKVVDHLLVFN 508
Cdd:COG4778 153 ------FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGTAIIgIFHDEEVREAVADRVVDVT 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-186 |
7.11e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 22 LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYD---SGTISF------RRDIRV--GYLEQDPQYPEELTVLEa 90
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLngmpidAKEMRAisAYVQQDDLFIPTLTVRE- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 91 cfhHGNSTVELikeyercmetdghpgldgilaRMD-HEKAWEYEQKAKQILSQLKIRDFNQ-------QVKSLSGGQLKR 162
Cdd:TIGR00955 119 ---HLMFQAHL---------------------RMPrRVTKKEKRERVDEVLQALGLRKCANtrigvpgRVKGLSGGERKR 174
|
170 180
....*....|....*....|....
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLD 186
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-218 |
7.59e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------------RRDIr 71
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 vGYLEQDPQYPEELTVleacfhhgnstvelikeYERCMetdghpgldGILARMDHEKAWEYEQKAKQILSQLKIRDFNQQ 151
Cdd:PRK10895 81 -GYLPQEASIFRRLSV-----------------YDNLM---------AVLQIRDDLSAEQREDRANELMEEFHIEHLRDS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 152 V-KSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEdYLRRTNLTLLMVTHD-RYFLDrVC 218
Cdd:PRK10895 134 MgQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvIDIKRIIE-HLRDSGLGVLITDHNvRETLA-VC 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-229 |
9.23e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.72 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS----------------F 66
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalserelraA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 RRDIrvGYLEQDPQYPEELTVLEacfhhgNstVELikeyerCMETDGHPGLDgILARMDH--------EKAWEYeqkakq 138
Cdd:COG1135 81 RRKI--GMIFQHFNLLSSRTVAE------N--VAL------PLEIAGVPKAE-IRKRVAEllelvglsDKADAY------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 139 iLSQLkirdfnqqvkslSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT----EWLEDYLRRTNLTLLMVTHD---- 210
Cdd:COG1135 138 -PSQL------------SGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKDINRELGLTIVLITHEmdvv 204
|
250
....*....|....*....
gi 2524717128 211 RyfldRVCSEIIEIDNRRI 229
Cdd:COG1135 205 R----RICDRVAVLENGRI 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-217 |
1.12e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF----GdlvLF----------ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI- 70
Cdd:COG4608 7 LLEVRDLKKHFpvrgG---LFgrtvgvvkavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDIt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 ------------RVGYLEQDPQypeelTVLeacfhhgNS--TV-ELIKEyercmetdghpGLD--GILARMdhekawEYE 133
Cdd:COG4608 84 glsgrelrplrrRMQMVFQDPY-----ASL-------NPrmTVgDIIAE-----------PLRihGLASKA------ERR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 134 QKAKQILSQ--LKIRDFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD-------LDMtewLEDYLRRTNLTL 204
Cdd:COG4608 135 ERVAELLELvgLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaqvLNL---LEDLQDELGLTY 211
|
250
....*....|....*..
gi 2524717128 205 LMVTHD----RYFLDRV 217
Cdd:COG4608 212 LFISHDlsvvRHISDRV 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-509 |
1.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 303 KLDVKASYIGSK---IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV 378
Cdd:PRK13536 26 ISEAKASIPGSMstvAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 379 ---------RFGYYSQdglqFDEQMKVIDVVQDIaevIELGNGKRLTASQF------LQHFLFTPETQHSYVYKLSGGER 443
Cdd:PRK13536 106 pararlaraRIGVVPQ----FDNLDLEFTVRENL---LVFGRYFGMSTREIeavipsLLEFARLESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 444 RRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF--KGCVIVVShdRYFM---DKVVDHLLVFNG 509
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILLT--THFMeeaERLCDRLCVLEA 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-222 |
1.40e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-----------GDLVLFENISFGLSEGQRVGLIAKNGSGKST----LLNILS--GKEGYDSGTIS---- 65
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHnlnr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 66 -----FRRDIRVGYleQDPQYP--EELTVLEacfhhgnstveLIKEYERCMetdgHPGLDgilarmdhekAWEYEQKAKQ 138
Cdd:PRK15134 355 rqllpVRHRIQVVF--QDPNSSlnPRLNVLQ-----------IIEEGLRVH----QPTLS----------AAQREQQVIA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 139 ILSQLKIRDFNQQ--VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRY 212
Cdd:PRK15134 408 VMEEVGLDPETRHryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLH 487
|
250
....*....|
gi 2524717128 213 FLDRVCSEII 222
Cdd:PRK15134 488 VVRALCHQVI 497
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-242 |
1.66e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGD-----LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrDIRVG-YLEQDPQ 80
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-DIYIGdKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 YPEELTVLEACFHHGNSTVELI---KEYERCMETDGHPGLDGILARMDHEKawEYEQKAKQILSQLKIRD--FNQQVKSL 155
Cdd:PRK13631 100 ITNPYSKKIKNFKELRRRVSMVfqfPEYQLFKDTIEKDIMFGPVALGVKKS--EAKKLAKFYLNKMGLDDsyLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYlRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQ 231
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgeHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 2524717128 232 YKGNYSYYLEK 242
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-209 |
1.85e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.19 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 18 GDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKegYD--SGTISF-RRDIR----------VGYLEQDPQypee 84
Cdd:COG1132 352 DRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRF--YDptSGRILIdGVDIRdltleslrrqIGVVPQDTF---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 L---TVLEacfhhgNstvelIKeyercmetdghpgldgiLARMDHEKAwEYEQKAKQilSQLK--IRDF----NQQV--- 152
Cdd:COG1132 425 LfsgTIRE------N-----IR-----------------YGRPDATDE-EVEEAAKA--AQAHefIEALpdgyDTVVger 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 153 -KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDmTE-WLEDYLRR--TNLTLLMVTH 209
Cdd:COG1132 474 gVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE-TEaLIQEALERlmKGRTTIVIAH 533
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
1.89e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSFGD-LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-FRRDI----------R 71
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQDPQypeeltvlEACFhhgNSTV-ELIKEYERCMETDGHpgldgilarmdhekawEYEQKAKQILSQLKIRDFNQ 150
Cdd:PRK13647 81 VGLVFQDPD--------DQVF---SSTVwDDVAFGPVNMGLDKD----------------EVERRVEEALKAVRMWDFRD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVK-SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN---LTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:PRK13647 134 KPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKE 213
|
....*....
gi 2524717128 227 RRIYQYKGN 235
Cdd:PRK13647 214 GRVLAEGDK 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-222 |
1.92e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIRV-----GYLEQD 78
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgQTINLvrdkdGQLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEEL--TVLEACFHHGNsTVELIKEYERCMETDGHP-GLDGILARmdhEKAWEYeqkakqiLSQLKIrDFNQQVK-- 153
Cdd:PRK10619 83 DKNQLRLlrTRLTMVFQHFN-LWSHMTVLENVMEAPIQVlGLSKQEAR---ERAVKY-------LAKVGI-DERAQGKyp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 154 -SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT-EWLE--DYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:PRK10619 151 vHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
331-508 |
2.22e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.97 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETV----RFGYYSQDGLQFDEQ------MKVIDVV 400
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRIGVVFGQKtqlwwdLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 QDIAEVIEL------GNGKRLTASQFLQHFLFTPetqhsyVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT-L 473
Cdd:cd03267 117 YLLAAIYDLpparfkKRLDELSELLDLEELLDTP------VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAqE 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524717128 474 NV---LEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:cd03267 191 NIrnfLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-209 |
2.26e-12 |
|
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: 66.73 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSF---GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfrrdirvgYLEQDPq 80
Cdd:cd03248 8 LKGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV---------LLDGKP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 ypeeLTVLEACFHH-------------GNSTVELI------KEYERCMETDGHPGLDGILARMDHEKAWEYEQKAKQils 141
Cdd:cd03248 78 ----ISQYEHKYLHskvslvgqepvlfARSLQDNIayglqsCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQ--- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 142 qlkirdfnqqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTH 209
Cdd:cd03248 151 -------------LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAH 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
315-510 |
2.42e-12 |
|
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: 66.91 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVR-----------FGY 382
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 YSQDGLQFDEqmkvIDVVQDIAEVIELGngKRLTASQ-------FLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRN 455
Cdd:TIGR04406 81 LPQEASIFRK----LTVEENIMAVLEIR--KDLDRAEreerleaLLEEFQIS-HLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 456 PNFLVLDEPTNDLD-IVTLNV--LEEYLRNFKGCVIVVSHDRYFMDKVVDH-LLVFNGQ 510
Cdd:TIGR04406 154 PKFILLDEPFAGVDpIAVGDIkkIIKHLKERGIGVLITDHNVRETLDICDRaYIISDGK 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-210 |
2.83e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 26 ISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYdSGTISFR-RDIRvgyleqdpQYP-EELTVLEACFHHGNSTVELIK 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNgRPLS--------DWSaAELARHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 104 EYERcmetdghpgLDgiLARMDHEKAWEYEQKAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLI-----TEPD--L 175
Cdd:COG4138 86 VFQY---------LA--LHQPAGASSEAVEQLLAQLAEALGLEDKlSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524717128 176 LILDEPTNHLD------LDmtEWLEdYLRRTNLTLLMVTHD 210
Cdd:COG4138 155 LLLDEPMNSLDvaqqaaLD--RLLR-ELCQQGITVVMSSHD 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-222 |
2.94e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI-------------SFRRdiR 71
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsskAFAR--K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQDPQYPEELTVLEacfhhgnstVELIKEYErcmetdGHPGLdGILARMDHEKAweyeqkaKQILSQLKIRDFNQQ 151
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRE---------LVAIGRYP------WHGAL-GRFGAADREKV-------EEAISLVGLKPLAHR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 152 -VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:PRK10575 144 lVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLV 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-210 |
3.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.55 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-----------------FRRDIRVGYleqdpQYPE--- 83
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlkkLRKKVSLVF-----QFPEaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 84 -ELTVLEacfhhgnsTVELikeyercmetdghpgldGILARMDHEKawEYEQKAKQILSQLKIRD--FNQQVKSLSGGQL 160
Cdd:PRK13641 99 fENTVLK--------DVEF-----------------GPKNFGFSED--EAKEKALKWLKKVGLSEdlISKSPFELSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 161 KRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYlRRTNLTLLMVTHD 210
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDpegrKEMMQLFKDY-QKAGHTVILVTHN 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-186 |
3.22e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKE--GYDSGTI---------SFRRd 69
Cdd:cd03232 1 GSVLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEIlingrpldkNFQR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 iRVGYLEQDPQYPEELTVLEAcfhhgnstvelikeyercmetdghpgldgilarmdhekaweyeqkakqilsqlkIRdFN 149
Cdd:cd03232 80 -STGYVEQQDVHSPNLTVREA------------------------------------------------------LR-FS 103
|
170 180 190
....*....|....*....|....*....|....*..
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD 186
Cdd:cd03232 104 ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-210 |
3.77e-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: 66.34 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrdirvGYLEQDPQyPEELTVLEacfhhGNSTVELIK 103
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-----GKQITEPG-PDRMVVFQ-----NYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 104 EYERCmetdgHPGLDGILARMDHEkawEYEQKAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPT 182
Cdd:TIGR01184 71 VRENI-----ALAVDRVLPDLSKS---ERRAIVEEHIALVGLTEAaDKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190
....*....|....*....|....*....|..
gi 2524717128 183 NHLDLDMTEWLEDYLRR----TNLTLLMVTHD 210
Cdd:TIGR01184 143 GALDALTRGNLQEELMQiweeHRVTVLMVTHD 174
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
324-492 |
3.80e-12 |
|
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: 66.65 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMR-HEQADRGALDI------GETV-----RFGYYSQD-GLQF 390
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgerrgGEDVwelrkRIGLVSPAlQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 DEQMKVIDVV----------------QDIAEVIELgngkrLTASQfLQHFLftpetQHSYvYKLSGGERRRLYLCTVLMR 454
Cdd:COG1119 92 PRDETVLDVVlsgffdsiglyreptdEQRERAREL-----LELLG-LAHLA-----DRPF-GTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524717128 455 NPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSH 492
Cdd:COG1119 160 DPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
330-492 |
4.14e-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: 66.09 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGE---------TVR--FGYYSQDGLQF-DEQMKVI 397
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkSLRsmIGVVLQDTFLFsGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 DVVQDIA---EVIELgnGKRLTASQFLQHFlftPETQHSYVYK----LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:cd03254 98 RLGRPNAtdeEVIEA--AKEAGAHDFIMKL---PNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180
....*....|....*....|....
gi 2524717128 471 VTLNVLEEYLRN-FKG-CVIVVSH 492
Cdd:cd03254 173 ETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-244 |
6.05e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLV-LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDI----- 70
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFdgkpidysRKGLmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQDPQYPEELTVLEACFHHGNSTVELIKeyercmetdghpglDGILARMDHekaweyeQKAKQILSQLKirdfNQ 150
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPE--------------DEVRKRVDN-------ALKRTGIEHLK----DK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDN 226
Cdd:PRK13636 138 PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
250
....*....|....*...
gi 2524717128 227 RRIYqYKGNYSYYLEKRE 244
Cdd:PRK13636 218 GRVI-LQGNPKEVFAEKE 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
331-502 |
6.18e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 68.47 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV----------RFGYYSQDGLQFDeqmkvidv 399
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWVPQHPFLFA-------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 400 vQDIAEVIELGNG-----------KRLTASQFLQHFlftPETQHSYVYK----LSGGERRRLYLCTVLMRNPNFLVLDEP 464
Cdd:TIGR02857 410 -GTIAENIRLARPdasdaeirealERAGLDEFVAAL---PQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524717128 465 TNDLDIVTLNVLEEYLRNFKG--CVIVVSHDR---YFMDKVVD 502
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQgrTVLLVTHRLalaALADRIVV 528
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
6.95e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR---------RDIR--VGY 74
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgepitkeniREVRkfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQypeeltvlEACFhhgNSTVELIKEYERCmetdgHPGLDgilarmdhEKAweYEQKAKQILSQLKIRDFNQQV-K 153
Cdd:PRK13652 83 VFQNPD--------DQIF---SPTVEQDIAFGPI-----NLGLD--------EET--VAHRVSSALHMLGLEELRDRVpH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
...
gi 2524717128 230 YQY 232
Cdd:PRK13652 217 VAY 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-210 |
7.18e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKS----TLLNILSgKEGYDSGTISFR-RDI- 70
Cdd:PRK09473 6 QQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-ANGRIGGSATFNgREIl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 -------------RVGYLEQDPqypeeLTVLEACFHHGNSTVELIKEyercmetdgHPGldgilarMDHEKAWEyeqKAK 137
Cdd:PRK09473 85 nlpekelnklraeQISMIFQDP-----MTSLNPYMRVGEQLMEVLML---------HKG-------MSKAEAFE---ESV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 138 QILSQLKIRDFNQQVK----SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD-----MTeWLEDYLRRTNLTLLMVT 208
Cdd:PRK09473 141 RMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTvqaqiMT-LLNELKREFNTAIIMIT 219
|
..
gi 2524717128 209 HD 210
Cdd:PRK09473 220 HD 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-210 |
8.65e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNsilqvenLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSG------------------ 62
Cdd:PRK14271 22 MAAVN-------LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 63 -TISFRRdiRVGYLEQDPQyPEELTVLEACFHhGNSTVELI--KEYERCMEtdghpgldgilARMDHEKAWEyeqKAKQI 139
Cdd:PRK14271 95 dVLEFRR--RVGMLFQRPN-PFPMSIMDNVLA-GVRAHKLVprKEFRGVAQ-----------ARLTEVGLWD---AVKDR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 140 LSQLKIRdfnqqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHD 210
Cdd:PRK14271 157 LSDSPFR--------LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSlaDRLTVIIVTHN 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
317-492 |
9.13e-12 |
|
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: 65.33 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGD-LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRfgYYSQDGLQfdeqm 394
Cdd:cd03253 2 EFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIR--EVTLDSLR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVV-QD-------IAEVIELGngkRLTASQ--------------FLQHFLFTPETQhsyV----YKLSGGERRRLYL 448
Cdd:cd03253 75 RAIGVVpQDtvlfndtIGYNIRYG---RPDATDeevieaakaaqihdKIMRFPDGYDTI---VgergLKLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524717128 449 CTVLMRNPNFLVLDEPTNDLDIVT-LNVLEEYLRNFKG-CVIVVSH 492
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTeREIQAALRDVSKGrTTIVIAH 194
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-221 |
9.26e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 9.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR------------RDIRVGYL 75
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhklaAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEACFhhgnstvelikeyercmetdghpgldgiLARMDHEKAW--------EYEQKAKQILSQLKI-R 146
Cdd:PRK09700 86 YQELSVIDELTVLENLY----------------------------IGRHLTKKVCgvniidwrEMRVRAAMMLLRVGLkV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 147 DFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWL---EDYLRRTNLTLLMVTHDRYFLDRVCSEI 221
Cdd:PRK09700 138 DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
317-509 |
9.93e-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: 64.80 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGD----LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGYYSQDGLQFDe 392
Cdd:cd03293 2 EVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG------EVLVDGEPVTGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 qmkVIDVVQD--------IAEVIELG-NGKRLTASQF------------LQHFLftpetqHSYVYKLSGGERRRLYLCTV 451
Cdd:cd03293 75 ---RGYVFQQdallpwltVLDNVALGlELQGVPKAEAreraeellelvgLSGFE------NAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 452 LMRNPNFLVLDEPTNDLDIVTLNVLEEYL----RNFKGCVIVVSHDryfMDKVV---DHLLVFNG 509
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD---IDEAVflaDRVVVLSA 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-186 |
1.05e-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: 65.20 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 21 VLFENISFGLSEGQRVGLIAKNGSGKSTLLNIL-------SGK---EGYDSGTI---SFRRdiRVGYLEQDpqypeelTV 87
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyvpeNGRvlvDGHDLALAdpaWLRR--QVGVVLQE-------NV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 88 LEacfhhgNSTVElikeyERCMETDGHPGLDGIL--ARMD--HEKAWEYEQKAKQILSQlkirdfnqQVKSLSGGQLKRV 163
Cdd:cd03252 87 LF------NRSIR-----DNIALADPGMSMERVIeaAKLAgaHDFISELPEGYDTIVGE--------QGAGLSGGQRQRI 147
|
170 180
....*....|....*....|...
gi 2524717128 164 ALANTLITEPDLLILDEPTNHLD 186
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALD 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-243 |
1.28e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 64.55 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSF--GDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI-------------SFRRdiRVG 73
Cdd:cd03254 4 EFENVNFSYdeKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrkSLRS--MIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPqYPEELTVLEAC-FHHGNSTVELIKeyERCMETDGHPGLdgilarMDHEKAWEYEqkakqilsqlkirdFNQQV 152
Cdd:cd03254 81 VVLQDT-FLFSGTIMENIrLGRPNATDEEVI--EAAKEAGAHDFI------MKLPNGYDTV--------------LGENG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT--NLTLLMVTHdRYFLDRVCSEIIEIDNRRIY 230
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAH-RLSTIKNADKILVLDDGKII 216
|
250
....*....|...
gi 2524717128 231 QyKGNYSYYLEKR 243
Cdd:cd03254 217 E-EGTHDELLAKK 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-509 |
1.59e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 345 GIVGNNGTGKSTFIKILMRHEQADRGALDIGETV-----------RFGYYSQDgLQFDEQMKVIDVV------------- 400
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQQ-LPAAEGMTVRELVaigrypwhgalgr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 ------QDIAEVIELGNGKRLTasqflqhflftpetqHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI---V 471
Cdd:PRK10575 120 fgaadrEKVEEAISLVGLKPLA---------------HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqV 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524717128 472 TLNVLEEYLRNFKG-CVIVVSHDRYFMDKVVDHLLVFNG 509
Cdd:PRK10575 185 DVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRG 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
316-509 |
1.68e-11 |
|
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: 64.51 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 316 FEADHLYKSFGDLK-ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETV--------------RF 380
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 381 GYYSQDgLQFDEQMKVIDVVqdiaevielgNGKRLTASQFLQHF--LFTPETQH------------SYVYK----LSGGE 442
Cdd:cd03256 81 GMIFQQ-FNLIERLSVLENV----------LSGRLGRRSTWRSLfgLFPKEEKQralaalervgllDKAYQradqLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 443 RRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF---KGCVIVVS-HD----RYFMDKVV---DHLLVFNG 509
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQvdlaREYADRIVglkDGRIVFDG 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-182 |
2.21e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIrvgyleqdPQYPE 83
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgKDI--------TDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 84 ELTVLEAcfhhgnstVELIKEYERC---METDGHPGLDGILARMDhekawEYEQKAKQILsQLKIRDFN---QQVKSLSG 157
Cdd:PRK11614 75 AKIMREA--------VAIVPEGRRVfsrMTVEENLAMGGFFAERD-----QFQERIKWVY-ELFPRLHErriQRAGTMSG 140
|
170 180
....*....|....*....|....*
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPT 182
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-209 |
2.44e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 22 LFeNISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI----------SFRRDIR-----VGYLEQDP--QYPEE 84
Cdd:PRK13649 23 LF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstSKNKDIKqirkkVGLVFQFPesQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 LTVLEACFHHGNSTVEliKEyercmetdghpgldgilarmdhekawEYEQKAKQILSQLKIRD--FNQQVKSLSGGQLKR 162
Cdd:PRK13649 102 TVLKDVAFGPQNFGVS--QE--------------------------EAEALAREKLALVGISEslFEKNPFELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 163 VALANTLITEPDLLILDEPTNHLDLD-----MTewLEDYLRRTNLTLLMVTH 209
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKgrkelMT--LFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-210 |
2.46e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.71 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGD-LVLFENISFGLSEGQRVGLIAKNGSGKSTLL----NILSGKEG----------YD-SGTISFRRdi 70
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFlhfnGILKPTSGevlikgepikYDkKSLLEVRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQDPQypEEL---TVLE-ACFhhGNSTVELIKEyercmetdghpgldgilarmdhekawEYEQKAKQILSQLKIR 146
Cdd:PRK13639 79 TVGIVFQNPD--DQLfapTVEEdVAF--GPLNLGLSKE--------------------------EVEKRVKEALKAVGME 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 147 DFNQQV-KSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDyLRRTNLTLLMVTHD 210
Cdd:PRK13639 129 GFENKPpHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYD-LNKEGITIIISTHD 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
327-491 |
2.56e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.83 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 327 DLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRheQADRGALDIGETV-------------RFGYysqdGLQFDEQ 393
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTSGQILfngqprkpdqfqkCVAY----VRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 394 MKVIDVVQDIAEVIELGNGKRLTASQFLQHFLFTPETQ-------HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*..
gi 2524717128 467 DLDIVTLNVLEEYLRNF--KGCVIVVS 491
Cdd:cd03234 173 GLDSFTALNLVSTLSQLarRNRIVILT 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
317-493 |
2.64e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 63.43 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQD---GLQFDE- 392
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiAMVFQNy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 ----QMKVIDvvqDIAEVIELGNGKR-------LTASQFLQ--HFLftpetqHSYVYKLSGGERRRLYLCTVLMRNPNFL 459
Cdd:cd03301 82 alypHMTVYD---NIAFGLKLRKVPKdeidervREVAELLQieHLL------DRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524717128 460 VLDEPTNDLD----IVTLNVLEEYLRNFKGCVIVVSHD 493
Cdd:cd03301 153 LMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-209 |
2.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.16 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILS-----------GKEGYDSGTISFRRDI---- 70
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielypearvSGEVYLDGQDIFKMDVielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 -RVGYLEQDPQYPEELTVLEacfhhgnsTVELikeyercmetdghpGLDgiLARMDHEKAwEYEQKAKQILSQLKIRD-- 147
Cdd:PRK14247 82 rRVQMVFQIPNPIPNLSIFE--------NVAL--------------GLK--LNRLVKSKK-ELQERVRWALEKAQLWDev 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 148 ---FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYL--RRTNLTLLMVTH 209
Cdd:PRK14247 137 kdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFleLKKDMTIVLVTH 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
324-492 |
3.06e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 66.34 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SF---GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG---------ETVR--FGYYSQDGLQ 389
Cdd:COG1132 346 SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirdltlESLRrqIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 390 FDEqmkvidvvqDIAEVIELGNG-----------KRLTASQFLQHFlftPETQHSYV----YKLSGGERRRLYLCTVLMR 454
Cdd:COG1132 426 FSG---------TIRENIRYGRPdatdeeveeaaKAAQAHEFIEAL---PDGYDTVVgergVNLSGGQRQRIAIARALLK 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524717128 455 NPNFLVLDEPTNDLDIVTLNVLEEYLRNF-KGC-VIVVSH 492
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLmKGRtTIVIAH 533
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
315-510 |
3.20e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGE------------------ 376
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarrlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 ----------TVR-------------FGYYSQDglqfDEQMkvIDVVQDIAEVIELGNgKRLTAsqflqhflftpetqhs 433
Cdd:PRK11231 82 pqhhltpegiTVRelvaygrspwlslWGRLSAE----DNAR--VNQAMEQTRINHLAD-RRLTD---------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 434 yvykLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI---VTLNVLEEYLRNFKGCVIVVSHD-----RYfmdkvVDHLL 505
Cdd:PRK11231 139 ----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqVELMRLMRELNTQGKTVVTVLHDlnqasRY-----CDHLV 209
|
....*.
gi 2524717128 506 VF-NGQ 510
Cdd:PRK11231 210 VLaNGH 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-247 |
3.28e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSfgDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-FRRDIR-----------VGY 74
Cdd:PRK09700 265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlNGKDISprspldavkkgMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQypeeltvlEACFHHGNSTVELIKeYERCMETDGHPGLDGILARMDHEKAWEYEQKakqiLSQLKIRDFNQQVKS 154
Cdd:PRK09700 343 ITESRR--------DNGFFPNFSIAQNMA-ISRSLKDGGYKGAMGLFHEVDEQRTAENQRE----LLALKCHSVNQNITE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQ 231
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQladDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
250
....*....|....*.
gi 2524717128 232 YKGNYSyylEKREERI 247
Cdd:PRK09700 490 ILTNRD---DMSEEEI 502
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
317-493 |
4.49e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.64 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGYYSQDGLQFDEQMKV 396
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG------EVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 397 IDVV-Q--------DIAEVIELG---------NGKRLTASQF----LQHFlftpetQHSYVYKLSGGERRRLYLCTVLMR 454
Cdd:PRK13548 78 RAVLpQhsslsfpfTVEEVVAMGraphglsraEDDALVAAALaqvdLAHL------AGRDYPQLSGGEQQRVQLARVLAQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2524717128 455 ------NPNFLVLDEPTNDLDI----VTLNVLEEYLRNFKGCVIVVSHD 493
Cdd:PRK13548 152 lwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
315-510 |
6.42e-11 |
|
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: 62.37 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSF--GDLK--ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV------RFGYY 383
Cdd:TIGR02211 1 LLKCENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFnGQSLsklssnERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 SQDGL----QFDEQMKVIDVVQDIAEVIELGNGKRLTASQFLQHFLFTPETQHSYVYK---LSGGERRRLYLCTVLMRNP 456
Cdd:TIGR02211 81 RNKKLgfiyQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRpseLSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 457 NFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFNGQ 510
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNakiiFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-501 |
6.47e-11 |
|
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: 62.16 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 320 HLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHE--QADRG----------ALDIGETVRFGYYsqdg 387
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGeilfkgeditDLPPEERARLGIF---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFDEQMKVIDVvqdiaevielgngkrlTASQFLQhflftpetqhsYV-YKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:cd03217 81 LAFQYPPEIPGV----------------KNADFLR-----------YVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524717128 467 DLDIVTLNVLEE---YLRNFKGCVIVVSHDRYFMDKVV 501
Cdd:cd03217 134 GLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYIK 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-229 |
7.35e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-------FR--RD-----IRVG 73
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILidgqemrFAstTAalaagVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YleQDPQYPEELTVLEACFHhgnstvelikeyercmetdGH-PGLDGILarmdHEKAWEYEqkAKQILSQLKIR-DFNQQ 151
Cdd:PRK11288 85 Y--QELHLVPEMTVAENLYL-------------------GQlPHKGGIV----NRRLLNYE--AREQLEHLGVDiDPDTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE---DYLRRTNLTLLMVTHDRYFLDRVCSEI-IEIDNR 227
Cdd:PRK11288 138 LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFrviRELRAEGRVILYVSHRMEEIFALCDAItVFKDGR 217
|
..
gi 2524717128 228 RI 229
Cdd:PRK11288 218 YV 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-217 |
8.43e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.21 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLT---KSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI-------------SFRRD 69
Cdd:PRK13650 3 NIIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IRVGYLEQDPQYPeeltvleacfhhgNSTVElikeyercmeTDGHPGLDGilARMDHEkawEYEQKAKQILSQLKIRDF- 148
Cdd:PRK13650 83 IGMVFQNPDNQFV-------------GATVE----------DDVAFGLEN--KGIPHE---EMKERVNEALELVGMQDFk 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfLDRV 217
Cdd:PRK13650 135 EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEV 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
318-493 |
1.11e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 318 ADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTF---------------------IKILMRHEQADRGaldige 376
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTfymvvgivprdagniiiddedISLLPLHARARRG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 tvrFGYYSQDGLQF------DEQMKVIDVVQDIAEvielgNGKRLTASQFLQHFLFTpETQHSYVYKLSGGERRRLYLCT 450
Cdd:PRK10895 80 ---IGYLPQEASIFrrlsvyDNLMAVLQIRDDLSA-----EQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524717128 451 VLMRNPNFLVLDEPTNDLD---IVTLNVLEEYLRNFKGCVIVVSHD 493
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
329-492 |
1.25e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.86 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 329 KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVR----------FGYYSQDGLQFDEQmkvi 397
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRdytlaslrrqIGLVSQDVFLFNDT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 dVVQDIA---------EVIELGngKRLTASQFLQHFlftPETQHSYV----YKLSGGERRRLYLCTVLMRNPNFLVLDEP 464
Cdd:cd03251 92 -VAENIAygrpgatreEVEEAA--RAANAHEFIMEL---PEGYDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190
....*....|....*....|....*....|
gi 2524717128 465 TNDLDIVTLNVLEEYLRNF-KG-CVIVVSH 492
Cdd:cd03251 166 TSALDTESERLVQAALERLmKNrTTFVIAH 195
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-247 |
1.38e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.11 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLN------------------ILSGKEGYDSG 62
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 63 T--ISFRRdiRVGYLEQDPQ-YPEeltvleacfhhgnSTVELIKEYERcmeTDGHPG-LDGILARMDHEKAWEYEQKAKq 138
Cdd:PRK14243 84 VdpVEVRR--RIGMVFQKPNpFPK-------------SIYDNIAYGAR---INGYKGdMDELVERSLRQAALWDEVKDK- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 139 ilsqlkirdFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR--RTNLTLLMVTHDRYFLDR 216
Cdd:PRK14243 145 ---------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHelKEQYTIIIVTHNMQQAAR 215
|
250 260 270
....*....|....*....|....*....|..
gi 2524717128 217 VcSEIIEIDNRRIYQYKGNYSYYLE-KREERI 247
Cdd:PRK14243 216 V-SDMTAFFNVELTEGGGRYGYLVEfDRTEKI 246
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-186 |
1.40e-10 |
|
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: 63.91 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLT--KSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDI--RVGY 74
Cdd:TIGR01842 317 LSVENVTivPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdRETFgkHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDpqypeeltvleacfhhgnstVEL----IKEYercmetdghpgldgiLARMDhEKAweyeqKAKQILSQLKIRDFNQ 150
Cdd:TIGR01842 397 LPQD--------------------VELfpgtVAEN---------------IARFG-ENA-----DPEKIIEAAKLAGVHE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 151 QVKS---------------LSGGQLKRVALANTLITEPDLLILDEPTNHLD 186
Cdd:TIGR01842 436 LILRlpdgydtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-210 |
1.60e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGK--EGYDSGTISFRRDIRvgyLEQDPQY--- 81
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltGGGAPRGARVTGDVT---LNGEPLAaid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 82 PEELTVLEA--------CFHHGNSTVELIKEYErcmetdgHPGLDGILARMDHEKAWEYEQKAKQilSQLKIRDfnqqVK 153
Cdd:PRK13547 78 APRLARLRAvlpqaaqpAFAFSAREIVLLGRYP-------HARRAGALTHRDGEIAWQALALAGA--TALVGRD----VT 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 154 SLSGGQLKRVALANTL---------ITEPDLLILDEPTNHLDLDMTEWLEDYLRRT----NLTLLMVTHD 210
Cdd:PRK13547 145 TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLardwNLGVLAIVHD 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-210 |
1.75e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSF---GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI-------------SFR 67
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgelltaenvwNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RDIRVGYLEQDPQYPeeltvleacfhhgNSTVEliKEYERCMETDGHPgLDGILARMDhekaweyeqkakQILSQLKIRD 147
Cdd:PRK13642 81 RKIGMVFQNPDNQFV-------------GATVE--DDVAFGMENQGIP-REEMIKRVD------------EALLAVNMLD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 148 F-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:PRK13642 133 FkTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-210 |
1.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSFGD--LVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG----------KEGYDSGTISFRR--D 69
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnsKITVDGITLTAKTvwD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IR--VGYLEQDP--QYPEELTVLEACFHHGNSTV---ELIKeyercmetdghpgldgILArmdhekaweyeqkakQILSQ 142
Cdd:PRK13640 82 IRekVGIVFQNPdnQFVGATVGDDVAFGLENRAVprpEMIK----------------IVR---------------DVLAD 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 143 LKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHD 210
Cdd:PRK13640 131 VGMLDYiDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkkkNNLTVISITHD 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
326-494 |
1.97e-10 |
|
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: 60.88 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV------RFGYYSQD-GLQFDEQMKVI 397
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKiGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 D--VVQDIA---EVIELGN---GKRLTASQFLqhfLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD 469
Cdd:cd03292 92 DrnVYENVAfalEVTGVPPreiRKRVPAALEL---VGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190
....*....|....*....|....*....|
gi 2524717128 470 IVT----LNVLEEYlrNFKGCVIVVS-HDR 494
Cdd:cd03292 169 PDTtweiMNLLKKI--NKAGTTVVVAtHAK 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-229 |
2.10e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.09 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 18 GDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR----------VGYLEQDpqypeelT 86
Cdd:cd03251 14 GPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDgHDVRdytlaslrrqIGLVSQD-------V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLeacFhhgNSTVELIKEYERCMETDGhpgldgilarmdhekawEYEQKAKQILSQLKIRDFNQQVKS--------LSGG 158
Cdd:cd03251 86 FL---F---NDTVAENIAYGRPGATRE-----------------EVEEAARAANAHEFIMELPEGYDTvigergvkLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 159 QLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHdRYFLDRVCSEIIEIDNRRI 229
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAH-RLSTIENADRIVVLEDGKI 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-217 |
2.18e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGY--DSGTISFR-RDIrvgyLEQDP---- 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKgKDL----LELSPedra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 --------QYPEELTVLEACFHHgNSTVELIKEYErcmetdGHPGLDgilaRMDHEKAWEYEQKAKQILSQLKIRDFNQq 151
Cdd:PRK09580 77 gegifmafQYPVEIPGVSNQFFL-QTALNAVRSYR------GQEPLD----RFDFQDLMEEKIALLKMPEDLLTRSVNV- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 152 vkSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE---DYLRRTNLTLLMVTHDRYFLDRV 217
Cdd:PRK09580 145 --GFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
222-294 |
2.84e-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: 56.81 E-value: 2.84e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 222 IEIDNRRIYQYKGNYSYYLEKREERIEAKTVEIERANNLYRTELEWMRRMPqARGHKARY---REDAFYELEKVAK 294
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFR-AKASKAKQaqsRIKALEKMERIEK 75
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-209 |
3.47e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 17 FGDLVLFEnISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI----------SFRRDIR-----VGYLEQDP-- 79
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstSKQKEIKpvrkkVGVVFQFPes 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYPEELTVLEACFhhGNSTVELIKEyercmetdghpgldgilarmdhekawEYEQKAKQILSQLKI-RDFNQQVK-SLSG 157
Cdd:PRK13643 96 QLFEETVLKDVAF--GPQNFGIPKE--------------------------KAEKIAAEKLEMVGLaDEFWEKSPfELSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDyLRRTNLTLLMVTH 209
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVTH 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-217 |
3.85e-10 |
|
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: 62.84 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLT--KSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-RRDIR----------VGY 74
Cdd:COG4618 331 LSVENLTvvPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdGADLSqwdreelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPqypeEL---TVLE--ACFhhGNSTVELIKEYERcmetdghpgldgiLARMdHEkaweyeqkakQILSqlkirdFN 149
Cdd:COG4618 411 LPQDV----ELfdgTIAEniARF--GDADPEKVVAAAK-------------LAGV-HE----------MILR------LP 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 150 Q----QV----KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE---DYLRRTNLTLLMVTHDRYFLDRV 217
Cdd:COG4618 455 DgydtRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAaaiRALKARGATVVVITHRPSLLAAV 533
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-182 |
5.26e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 11 ENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG----KEG--------YDSGTISFRRdiRVGYLEQD 78
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGllpaSEGeawlfgqpVDAGDIATRR--RVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEELTVLEacfhhgNstVELikeyercmetdgHpgldgilARMDHEKAWEYEQKAKQILSQLKIRDF-NQQVKSLSG 157
Cdd:NF033858 348 FSLYGELTVRQ------N--LEL------------H-------ARLFHLPAAEIAARVAEMLERFDLADVaDALPDSLPL 400
|
170 180
....*....|....*....|....*
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPT 182
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-182 |
5.33e-10 |
|
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: 59.85 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDI-------RV----GYL 75
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgEDItklppheRAragiAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 76 EQDPQYPEELTVLEacfhhgNstvelikeyercMETdghpGLDGILARMDHEKAWEYEQKAkqILSQLKIRdfnqQVKSL 155
Cdd:TIGR03410 81 PQGREIFPRLTVEE------N------------LLT----GLAALPRRSRKIPDEIYELFP--VLKEMLGR----RGGDL 132
|
170 180
....*....|....*....|....*..
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPT 182
Cdd:TIGR03410 133 SGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-230 |
5.50e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.89 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF----------------RRD 69
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghditrlknrevpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IrvGYLEQDPQYPEELTVLEacfhhgNSTVELIkeyercmeTDGHPGLDgilarmdhekaweYEQKAKQILSQL----KI 145
Cdd:PRK10908 81 I--GMIFQDHHLLMDRTVYD------NVAIPLI--------IAGASGDD-------------IRRRVSAALDKVglldKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 146 RDFNQQvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTE---WLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:PRK10908 132 KNFPIQ---LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLISRRSYRML 208
|
....*...
gi 2524717128 223 EIDNRRIY 230
Cdd:PRK10908 209 TLSDGHLH 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-227 |
5.82e-10 |
|
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: 60.35 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 11 ENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNIL-------SGK---EGYDSGTIS------FRRDiRVGY 74
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKvliDGQDIAAMSrkelreLRRK-KISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQD----PQypeeLTVLEacfhhgNSTVelikeyercmetdghpGLDgiLARMDHEkawEYEQKAKQILSQLKIRDF-N 149
Cdd:cd03294 107 VFQSfallPH----RTVLE------NVAF----------------GLE--VQGVPRA---EREERAAEALELVGLEGWeH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDryfLDrvcsEIIEID 225
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD---LD----EALRLG 228
|
..
gi 2524717128 226 NR 227
Cdd:cd03294 229 DR 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-211 |
6.06e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrdirvgyleqdpq 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 yPEELTVLeacfhhgnSTVELIKEYERCMETdghPGLDGILARMDHEKAWEYEQKAKQI------LSQLKIRD--FNQQV 152
Cdd:PRK10247 68 -GEDISTL--------KPEIYRQQVSYCAQT---PTLFGDTVYDNLIFPWQIRNQQPDPaiflddLERFALPDtiLTKNI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNLTLLMVTHDR 211
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDK 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
317-513 |
6.19e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.25 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV--------RFGYYSQDG 387
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFdEQMKVIDvvqDIAEVIE-LGNGKRLTA---SQFLQHFLFTPETQH---SYVYKLSGGERRRLYLCTVLMRNPNFLV 460
Cdd:PRK10851 84 ALF-RHMTVFD---NIAFGLTvLPRRERPNAaaiKAKVTQLLEMVQLAHladRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 461 LDEPTNDLDIVTLNVLEEYLRN----FKGCVIVVSHDRYFMDKVVDHLLVFNgQGDI 513
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVVMS-QGNI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
317-493 |
6.59e-10 |
|
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: 59.66 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKiLDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGAL-----DIG----ETVRFGYYSQD- 386
Cdd:cd03299 2 KVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkDITnlppEKRDISYVPQNy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 ----------GLQFDEQMKVIDVVQDIAEVIELgngkrltaSQFL--QHFLftpetqHSYVYKLSGGERRRLYLCTVLMR 454
Cdd:cd03299 81 alfphmtvykNIAYGLKKRKVDKKEIERKVLEI--------AEMLgiDHLL------NRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524717128 455 NPNFLVLDEPTNDLDIVTLNVLEEYL----RNFKGCVIVVSHD 493
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-209 |
6.64e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.06 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKS--FGDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF---------RRDIR-- 71
Cdd:TIGR01193 471 NGDIVINDVSYSygYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdidRHTLRqf 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQDPqYPEELTVLEACF--HHGNSTVELIKEYERCMETDGhpgldgilarmDHEKaweyeqkakqiLSQLKIRDFN 149
Cdd:TIGR01193 550 INYLPQEP-YIFSGSILENLLlgAKENVSQDEIWAACEIAEIKD-----------DIEN-----------MPLGYQTELS 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLdMTEW--LEDYLRRTNLTLLMVTH 209
Cdd:TIGR01193 607 EEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT-ITEKkiVNNLLNLQDKTIIFVAH 667
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
330-492 |
7.21e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 59.81 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGAL-----DIG----ETVR--FGYYSQDGLQFD----EQM 394
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghDLAladpAWLRrqVGVVLQENVLFNrsirDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQDIAEVIELGngKRLTASQFLQHFlftPETQHSYVYK----LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:cd03252 97 ALADPGMSMERVIEAA--KLAGAHDFISEL---PEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180
....*....|....*....|....
gi 2524717128 471 VTLNVLEEYLRNF-KG-CVIVVSH 492
Cdd:cd03252 172 ESEHAIMRNMHDIcAGrTVIIIAH 195
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
326-506 |
7.27e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 58.72 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILM--RHEQADRGaldigeTVRFGYYSQDGLQFDEQMkvIDVVQDI 403
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSG------EVLINGRPLDKRSFRKII--GYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 404 aevIELGNgkrLTASQFLQhflFTPETQhsyvyKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF 483
Cdd:cd03213 92 ---ILHPT---LTVRETLM---FAAKLR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180
....*....|....*....|....*..
gi 2524717128 484 --KGCVIVVS-HD-RYFMDKVVDHLLV 506
Cdd:cd03213 158 adTGRTIICSiHQpSSEIFELFDKLLL 184
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
320-508 |
8.02e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 320 HLYKsfGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIK------------ILMRHEQADRGalDIGETVRFGyysqdG 387
Cdd:PRK13652 11 YSYS--GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRhfngilkptsgsVLIRGEPITKE--NIREVRKFV-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQF---DEQMKVIDVVQDIA-EVIELGNGKRLTASQFLQ--HFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVL 461
Cdd:PRK13652 82 LVFqnpDDQIFSPTVEQDIAfGPINLGLDEETVAHRVSSalHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 462 DEPTNDLDIVTLNVLEEYLRNFKG----CVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-223 |
8.97e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLtkSFG-----DLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSgkEGYD--SGTISFR-RDIrvgyleqdP 79
Cdd:PRK11160 339 LTLNNV--SFTypdqpQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLT--RAWDpqQGEILLNgQPI--------A 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 QYPEE-----LTVLEACFHHGNSTvelikeyercmetdghpgLDGILARMDHEKAweyEQKAKQILSQLKIRDFNQQVKS 154
Cdd:PRK11160 406 DYSEAalrqaISVVSQRVHLFSAT------------------LRDNLLLAAPNAS---DEALIEVLQQVGLEKLLEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 155 L-----------SGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRrtNLTLLMVTHDRYFL---DR 216
Cdd:PRK11160 465 LnawlgeggrqlSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAEterqILELLAEHAQ--NKTVLMITHRLTGLeqfDR 542
|
250
....*....|.
gi 2524717128 217 VC----SEIIE 223
Cdd:PRK11160 543 ICvmdnGQIIE 553
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
321-523 |
1.08e-09 |
|
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: 57.97 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 321 LYKSFGDLKILDDFSyIFARYEKMGIVGNNGTGKSTFIKILMRHEQADrgaldigetvrfgyysQDGLQFDeqmkvidvv 400
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------GDNDEWD--------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 qdiaevielgngkrltasqflqhfLFTPETQHSYVyKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYL 480
Cdd:cd03222 60 ------------------------GITPVYKPQYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 481 RNF----KGCVIVVSHDRYFMDKVVDHLLVFNGQgdirdfPGNYTRY 523
Cdd:cd03222 115 RRLseegKKTALVVEHDLAVLDYLSDRIHVFEGE------PGVYGIA 155
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
330-492 |
1.09e-09 |
|
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: 58.66 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGE---------------------------TVR--- 379
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsrisiipqdpvlfsgTIRsnl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 380 --FGYYSqdglqfDEqmkvidvvqDIAEVIELGNGKRLTASQFLQHflftpETQHSYVYK-LSGGERRRLYLCTVLMRNP 456
Cdd:cd03244 99 dpFGEYS------DE---------ELWQALERVGLKEFVESLPGGL-----DTVVEEGGEnLSVGQRQLLCLARALLRKS 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524717128 457 NFLVLDEPTNDLDIVTLNVLEEYLR-NFKGC-VIVVSH 492
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIReAFKDCtVLTIAH 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
313-510 |
1.12e-09 |
|
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: 59.43 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGyySQDGLQFD- 391
Cdd:TIGR02769 9 THTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQG------TVSFR--GQDLYQLDr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 392 EQMKVID-----VVQD----------IAEVI--ELGNGKRLTASQFL---QHFL----FTPETQHSYVYKLSGGERRRLY 447
Cdd:TIGR02769 81 KQRRAFRrdvqlVFQDspsavnprmtVRQIIgePLRHLTSLDESEQKariAELLdmvgLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 448 LCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVF-NGQ 510
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVlqavILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMdKGQ 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
303-502 |
1.30e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.86 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 303 KLDVKASYIGSKIFEADHLYKSFGD-----LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKI---LMRHEQADRGALDI 374
Cdd:PRK13631 9 KLKVPNPLSDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHfngLIKSKYGTIQVGDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 375 --GETVRFGYYSQDGLQ-----FDEQMKVIDVV------QDIAEVIE---------LGNGKrLTASQFLQHFLFTPETQH 432
Cdd:PRK13631 89 yiGDKKNNHELITNPYSkkiknFKELRRRVSMVfqfpeyQLFKDTIEkdimfgpvaLGVKK-SEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 433 SYV----YKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSHDryfMDKVVD 502
Cdd:PRK13631 168 SYLerspFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHT---MEHVLE 241
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
12-209 |
1.36e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.27 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 12 NLTKSFGDLVLFENIS---------FGLSegqrvgliaknGSGKSTLLNILSGKEGYDSGTISF--------RRDI---- 70
Cdd:PRK11144 5 NFKQQLGDLCLTVNLTlpaqgitaiFGRS-----------GAGKTSLINAISGLTRPQKGRIVLngrvlfdaEKGIclpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 ---RVGYLEQD----PQYPEELTVLEACFH----HGNSTVELIkeyercmetdghpGLDGILARMDHekaweyeqkakqi 139
Cdd:PRK11144 74 ekrRIGYVFQDarlfPHYKVRGNLRYGMAKsmvaQFDKIVALL-------------GIEPLLDRYPG------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 140 lsqlkirdfnqqvkSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTH 209
Cdd:PRK11144 128 --------------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-209 |
1.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTL---LNIL----SGK---EGYDSGTISFRRDIR--VGYLEQDPQYPEELTVLE-- 89
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIakhMNALlipsEGKvyvDGLDTSDEENLWDIRnkAGMVFQNPDNQIVATIVEed 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 90 ACFHHGNSTVELIKEYERcmetdghpgLDGILARMDhekAWEYEQKAKQILSqlkirdfnqqvkslsGGQLKRVALANTL 169
Cdd:PRK13633 107 VAFGPENLGIPPEEIRER---------VDESLKKVG---MYEYRRHAPHLLS---------------GGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524717128 170 ITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTH 209
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
345-506 |
1.43e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 60.13 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 345 GIVGNNGTGKSTFIKILMRHEQADRGALDIGETV---------------RFGYYSQDGLQFDE---------QMKVIDVV 400
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQEARLFPHlsvrgnlryGMKRARPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 QDI---AEVIELGNgkrltasqfLQHFLftpetqHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLE 477
Cdd:TIGR02142 107 ERRisfERVIELLG---------IGHLL------GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|...
gi 2524717128 478 EYLRN----FKGCVIVVSHDRYFMDKVVDHLLV 506
Cdd:TIGR02142 172 PYLERlhaeFGIPILYVSHSLQEVLRLADRVVV 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
313-514 |
1.52e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.23 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEADHLYKSFGDLK--ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIgetvrFGY-YSQDGLQ 389
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-----DGItISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 390 F------------DEQMKVIDVVQDIAEVIElgnGKRLTASQ----------------FLQHflftpETQhsyvyKLSGG 441
Cdd:PRK13632 80 EirkkigiifqnpDNQFIGATVEDDIAFGLE---NKKVPPKKmkdiiddlakkvgmedYLDK-----EPQ-----NLSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 442 ERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF----KGCVIVVSHDryfMDKVV--DHLLVFNGQGDIR 514
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD---MDEAIlaDKVIVFSEGKLIA 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
317-493 |
1.59e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.95 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSF----GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETV-----RFGYYSQD 386
Cdd:COG1116 9 ELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPVtgpgpDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 ---------------GLQFdEQMKVIDVVQDIAEVIEL-GngkrltasqfLQHFLftpetqHSYVYKLSGGERRRLYLCT 450
Cdd:COG1116 89 pallpwltvldnvalGLEL-RGVPKAERRERARELLELvG----------LAGFE------DAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 451 VLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF---KGC-VIVVSHD 493
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqeTGKtVLFVTHD 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-215 |
1.81e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 32 EGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfrrdirvgyleQDPqyPEELTVLEacFHHGNstvELIKEYERCMET 111
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF------------DDP--PDWDEILD--EFRGS---ELQNYFTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 112 DGHP------------GLDG----ILARMDHEKAWEYeqkakqILSQLKIRD-FNQQVKSLSGGQLKRVALANTLITEPD 174
Cdd:cd03236 86 DVKVivkpqyvdlipkAVKGkvgeLLKKKDERGKLDE------LVDQLELRHvLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524717128 175 LLILDEPTNHLD----LDMTEWLEDYLRRTNlTLLMVTHDRYFLD 215
Cdd:cd03236 160 FYFFDEPSSYLDikqrLNAARLIRELAEDDN-YVLVVEHDLAVLD 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
330-492 |
1.91e-09 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 57.23 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVR----------FGYYSQDGLQFDEQmkvid 398
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISqwdpnelgdhVGYLPQDDELFSGS----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 399 vvqdIAEVIelgngkrltasqflqhflftpetqhsyvykLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEE 478
Cdd:cd03246 92 ----IAENI------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170
....*....|....*..
gi 2524717128 479 YLRNFKGC---VIVVSH 492
Cdd:cd03246 138 AIAALKAAgatRIVIAH 154
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-189 |
2.18e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSF---------GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR------- 67
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 ----RDIRVGYLEQDPQypeelTVLEAcfhhgNSTVELIKEYERCMETDghpgLDGIlarmdhekawEYEQKAKQILSQL 143
Cdd:PRK15112 81 dysyRSQRIRMIFQDPS-----TSLNP-----RQRISQILDFPLRLNTD----LEPE----------QREKQIIETLRQV 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524717128 144 KIR--DFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDM 189
Cdd:PRK15112 137 GLLpdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-229 |
2.60e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSfGDLVLFENISFGLSEGQRVGLIAKNGSGKS----TLLNILSGKEGYDSGTIsfrrdirvgYLEQDPQ 80
Cdd:PRK10418 2 PQQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRV---------LLDGKPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 YPEEL------TVLE---ACF-------HHGNSTvelikeyerCMETdGHPGLDGILARMDHEKAWEYEQKAkqilsqLK 144
Cdd:PRK10418 72 APCALrgrkiaTIMQnprSAFnplhtmhTHARET---------CLAL-GKPADDATLTAALEAVGLENAARV------LK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 145 IRDFnqqvkSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSE 220
Cdd:PRK10418 136 LYPF-----EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHDMGVVARLADD 210
|
....*....
gi 2524717128 221 IIEIDNRRI 229
Cdd:PRK10418 211 VAVMSHGRI 219
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
320-492 |
2.72e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 58.04 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 320 HLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQ------------ADRGALDIGETVRFGYYSqdG 387
Cdd:TIGR01978 5 DLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevtsgtilfkgQDLLELEPDERARAGLFL--A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFDEQM---KVIDVVQDIAEVIELGNGK-RLTASQFLQHFL-------FTPETQHSYV-YKLSGGERRRLYLCTVLMRN 455
Cdd:TIGR01978 83 FQYPEEIpgvSNLEFLRSALNARRSARGEePLDLLDFEKLLKeklalldMDEEFLNRSVnEGFSGGEKKRNEILQMALLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524717128 456 PNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSH 492
Cdd:TIGR01978 163 PKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITH 202
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-226 |
2.77e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGD--LVLfENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfRRDIR-------------V 72
Cdd:PRK10790 341 IDIDNVSFAYRDdnLVL-QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI--RLDGRplsslshsvlrqgV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDPqypeelTVLEACFHhGNSTvelikeyercmetdghpgldgiLAR-MDHEKAWEYEQKAKqiLSQLkIRDF--- 148
Cdd:PRK10790 418 AMVQQDP------VVLADTFL-ANVT----------------------LGRdISEEQVWQALETVQ--LAEL-ARSLpdg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 -----NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR--RTNLTLLMVTHdryfldRVcSEI 221
Cdd:PRK10790 466 lytplGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAavREHTTLVVIAH------RL-STI 538
|
....*
gi 2524717128 222 IEIDN 226
Cdd:PRK10790 539 VEADT 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-243 |
3.25e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR----RDIRVGYLEqdpqypEELTVLEACFHHGNSTV 99
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASLR------NQVALVSQNVHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 100 ELIKEYERcmetDGHPGLDGIL--ARMDHekAWEYEQKAKQILSQLkirdFNQQVKSLSGGQLKRVALANTLITEPDLLI 177
Cdd:PRK11176 434 ANNIAYAR----TEQYSREQIEeaARMAY--AMDFINKMDNGLDTV----IGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 178 LDEPTNHLDLDMTEWLE---DYLRRtNLTLLMVTHdRYFLDRVCSEIIEIDNRRIYQyKGNYSYYLEKR 243
Cdd:PRK11176 504 LDEATSALDTESERAIQaalDELQK-NRTSLVIAH-RLSTIEKADEILVVEDGEIVE-RGTHAELLAQN 569
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
317-493 |
3.26e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.79 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSyifARYEKMGI---VGNNGTGKSTFIKILMRHEQADRGA-----LDIGE------------ 376
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVS---LTIPKGGItalIGPNGAGKSTLLSMISRLLPPDSGEvlvdgLDVATtpsrelakrlai 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 -----------TVR----FG-Y-YSQDGL-QFDEQMkvidvvqdIAEVIELGNgkrltasqfLQHFlftpetQHSYVYKL 438
Cdd:COG4604 80 lrqenhinsrlTVRelvaFGrFpYSKGRLtAEDREI--------IDEAIAYLD---------LEDL------ADRYLDEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 439 SGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI----VTLNVLEEYLRNFKGCVIVVSHD 493
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-232 |
3.49e-09 |
|
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: 57.04 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG-DL--VLfENISFGLSEGQRVGLIAKNGSGKSTL-------LNILSGK---EGYDSGTISFRR-DIRVG 73
Cdd:cd03369 7 IEVENLSVRYApDLppVL-KNVSFKVKAGEKIGIVGRTGAGKSTLilalfrfLEAEEGKieiDGIDISTIPLEDlRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 YLEQDPqypeelTVLEACFHhgnSTVELIKEYercmeTDghpgldgilarmdhekaweyeqkaKQILSQLKIRDFNQqvk 153
Cdd:cd03369 86 IIPQDP------TLFSGTIR---SNLDPFDEY-----SD------------------------EEIYGALRVSEGGL--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTHD-RYFLDrvCSEIIEIDNRRIY 230
Cdd:cd03369 125 NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHRlRTIID--YDKILVMDAGEVK 202
|
..
gi 2524717128 231 QY 232
Cdd:cd03369 203 EY 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-226 |
3.67e-09 |
|
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: 57.09 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLT-----KSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRdiRVGYLEQDP--Q 80
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 ypeeltvleacfhhgNSTVElikeyercmetdghpglDGIL--ARMDHEKaweYEQ--KAkqilSQLKiRDFNQQVK--- 153
Cdd:cd03250 79 ---------------NGTIR-----------------ENILfgKPFDEER---YEKviKA----CALE-PDLEILPDgdl 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 154 --------SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL----TLLMVTHDRYFLDRvCSEI 221
Cdd:cd03250 119 teigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLlnnkTRILVTHQLQLLPH-ADQI 197
|
....*
gi 2524717128 222 IEIDN 226
Cdd:cd03250 198 VVLDN 202
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
317-481 |
4.27e-09 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 57.30 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIgetvrFGY-YSQDGLQFDEQMK 395
Cdd:TIGR03864 3 EVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISV-----AGHdLRRAPRAALARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 396 VidVVQDIAEVIEL-------------GNGKRLTAS---QFLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRNPNFL 459
Cdd:TIGR03864 78 V--VFQQPTLDLDLsvrqnlryhaalhGLSRAEARAriaELLARLGLA-ERADDKVRELNGGHRRRVEIARALLHRPALL 154
|
170 180
....*....|....*....|..
gi 2524717128 460 VLDEPTNDLDIVTLNVLEEYLR 481
Cdd:TIGR03864 155 LLDEPTVGLDPASRAAITAHVR 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
321-515 |
4.49e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 321 LYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRFgYYSQDGlqfdeQMKVID- 398
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINL-VRDKDG-----QLKVADk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 399 ------------------------VVQDIAE--VIELGNGK---RLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLC 449
Cdd:PRK10619 85 nqlrllrtrltmvfqhfnlwshmtVLENVMEapIQVLGLSKqeaRERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 450 TVLMRNPNFLVLDEPTNDLD--IV--TLNVLEEYLRNFKgCVIVVSHDRYFMDKVVDHlLVFNGQGDIRD 515
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDpeLVgeVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSH-VIFLHQGKIEE 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-243 |
4.60e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 6 SILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYD--SGTISFR-RDIrvgyLEQDP--- 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKgESI----LDLEPeer 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 ---------QYPEELTvleacfhhGNSTVELIK-EYERCMETDGHPGLDGIlarmdhekawEYEQKAKQILSQLKI---- 145
Cdd:CHL00131 82 ahlgiflafQYPIEIP--------GVSNADFLRlAYNSKRKFQGLPELDPL----------EFLEIINEKLKLVGMdpsf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 146 --RDFNQqvkSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE---DYLRRTNLTLLMVTHDRYFLDRVCSE 220
Cdd:CHL00131 144 lsRNVNE---GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYIKPD 220
|
250 260
....*....|....*....|....*
gi 2524717128 221 IIEI--DNRRIYQYKGNYSYYLEKR 243
Cdd:CHL00131 221 YVHVmqNGKIIKTGDAELAKELEKK 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-215 |
4.62e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 22 LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG--KEGYDSGTISFrrdirvgyleQDPQYPEELTVLEACFHHGNstv 99
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------PDNQFGREASLIDAIGRKGD--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 100 elIKEyercmetdghpgldgilarmdhekaweyeqkAKQILSQLKIRD---FNQQVKSLSGGQLKRVALANTLITEPDLL 176
Cdd:COG2401 112 --FKD-------------------------------AVELLNAVGLSDavlWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524717128 177 ILDEPTNHLDLDMTEW----LEDYLRRTNLTLLMVTHDRYFLD 215
Cdd:COG2401 159 VIDEFCSHLDRQTAKRvarnLQKLARRAGITLVVATHHYDVID 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
317-513 |
6.10e-09 |
|
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: 56.96 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG------ETVR-------FGYY 383
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdVPVQernvgfvFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 S-------QDGLQFDEQMKVIDVVQDIAEVielgngkRLTASQFLQhFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNP 456
Cdd:cd03296 84 AlfrhmtvFDNVAFGLRVKPRSERPPEAEI-------RAKVHELLK-LVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 457 NFLVLDEPTNDLDIVTLNVLEEYLRNFKGCV----IVVSHDRYFMDKVVDHLLVFNgQGDI 513
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMN-KGRI 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
317-513 |
6.18e-09 |
|
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: 58.98 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFG-DLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA----------LDIGETVRF-GYYS 384
Cdd:TIGR01193 475 VINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillngfslkdIDRHTLRQFiNYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 385 QDGLQFD---------------EQMKVIDVVqDIAEV---IE---LGNGKRLTASQFlqhflftpetqhsyvyKLSGGER 443
Cdd:TIGR01193 555 QEPYIFSgsilenlllgakenvSQDEIWAAC-EIAEIkddIEnmpLGYQTELSEEGS----------------SISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 444 RRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK-GCVIVVSHdRYFMDKVVDHLLVFNgQGDI 513
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAH-RLSVAKQSDKIIVLD-HGKI 686
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
326-493 |
6.47e-09 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 58.91 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGYYSQDGLQFDEQMKVIDVV-QD-- 402
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG------EVTLDGVPVSSLDQDEVRRRVSVCaQDah 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 403 -----IAEVIELGNG--------KRLTASQFLQHFLFTPETQHSYVY----KLSGGERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:TIGR02868 420 lfdttVRENLRLARPdatdeelwAALERVGLADWLRALPDGLDTVLGeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|....*.
gi 2524717128 466 NDLDIVT--------LNVLEEYLrnfkgcVIVVSHD 493
Cdd:TIGR02868 500 EHLDAETadelledlLAALSGRT------VVLITHH 529
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-232 |
6.51e-09 |
|
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: 58.99 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 21 VLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQ-----------YPEELtvlE 89
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYmtlgtlrdqiiYPDSS---E 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 90 ACFHHGNSTVELIKEYERCMetdghpgLDGILARmdhEKAWEYEQKAKQILSqlkirdfnqqvkslsGGQLKRVALANTL 169
Cdd:TIGR00954 543 DMKRRGLSDKDLEQILDNVQ-------LTHILER---EGGWSAVQDWMDVLS---------------GGEKQRIAMARLF 597
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 170 ITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTHdRYFLDRVCSEIIEIDNRRIYQY 232
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
317-501 |
6.57e-09 |
|
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: 57.76 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSF----GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRheQADRGALDIGEtVRFGyySQDGLQFDE 392
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG--LLPPPGITSGE-ILFD--GEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 393 -----------QMkvidVVQD--------------IAEVIELGNGkrLTASQFLQH--------FLFTPETQ-HSYVYKL 438
Cdd:COG0444 78 kelrkirgreiQM----IFQDpmtslnpvmtvgdqIAEPLRIHGG--LSKAEARERaiellervGLPDPERRlDRYPHEL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 439 SGGERRRLYLCTVLMRNPNFLVLDEPTNDLDiVT-----LNVLEEYLRNFKGCVIVVSHD----RYFMDKVV 501
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALD-VTiqaqiLNLLKDLQRELGLAILFITHDlgvvAEIADRVA 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
326-514 |
6.69e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.68 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG---------ETVR--FGYYSQ--------- 385
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNgqpiadyseAALRqaISVVSQrvhlfsatl 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 386 -DGLQF------DEQMkvIDVVQDIaevielGNGKRLTASQFLQHFLFTPETQhsyvykLSGGERRRLYLCTVLMRNPNF 458
Cdd:PRK11160 431 rDNLLLaapnasDEAL--IEVLQQV------GLEKLLEDDKGLNAWLGEGGRQ------LSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 459 LVLDEPTNDLDIVT----LNVLEEYLRNfKgCVIVVSHDRYFMDKvVDHLLVFNgQGDIR 514
Cdd:PRK11160 497 LLLDEPTEGLDAETerqiLELLAEHAQN-K-TVLMITHRLTGLEQ-FDRICVMD-NGQII 552
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-185 |
7.28e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 2 AAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVG-------- 73
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpakahq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 74 ---YL-EQDPQYPEELTVLEacfhhgnstvelikeyercmetdghpgldGILARM-DHEKAweyEQKAKQILSQLKIR-D 147
Cdd:PRK15439 86 lgiYLvPQEPLLFPNLSVKE-----------------------------NILFGLpKRQAS---MQKMKQLLAALGCQlD 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524717128 148 FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHL 185
Cdd:PRK15439 134 LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
315-517 |
7.86e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRFGYY--SQD-GLQF 390
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPrdAQAaGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 deqmkvidVVQD--------IAEVIELGNGK-----------RLTASQFLQHFLFT--PETQhsyVYKLSGGERRRLYLC 449
Cdd:COG1129 84 --------IHQElnlvpnlsVAENIFLGREPrrgglidwramRRRARELLARLGLDidPDTP---VGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 450 TVLMRNPNFLVLDEPT---NDLDIVTL-NVLEEyLRNfKGCVIV-VSHdryFMD---KVVDHLLVF-NGQ----GDIRDF 516
Cdd:COG1129 153 RALSRDARVLILDEPTaslTEREVERLfRIIRR-LKA-QGVAIIyISH---RLDevfEIADRVTVLrDGRlvgtGPVAEL 227
|
.
gi 2524717128 517 P 517
Cdd:COG1129 228 T 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
317-517 |
9.01e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRFG------------YY 383
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAsttaalaagvaiIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 SQdgLQFDEQMKVidvvqdiAEVIELG---------NGKRL--TASQFLQHF--LFTPETQHSYvykLSGGERRRLYLCT 450
Cdd:PRK11288 86 QE--LHLVPEMTV-------AENLYLGqlphkggivNRRLLnyEAREQLEHLgvDIDPDTPLKY---LSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 451 VLMRNPNFLVLDEPTNDL---DIVTLNVLEEYLRNFKGCVIVVSHdRyfMDKV---VDHLLVFNGQGDIRDFP 517
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH-R--MEEIfalCDAITVFKDGRYVATFD 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-182 |
9.25e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI----------SFRRDI--RVGY 74
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmadaRHRRAVcpRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LeqdPQ------YPeELTVLE-----AC-FHHGNStvelikEYERCME-----TdghpGLDGILARmdhekaweyeQKAK 137
Cdd:NF033858 81 M---PQglgknlYP-TLSVFEnldffGRlFGQDAA------ERRRRIDellraT----GLAPFADR----------PAGK 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524717128 138 qilsqlkirdfnqqvksLSGGQLKRVALANTLITEPDLLILDEPT 182
Cdd:NF033858 137 -----------------LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
322-492 |
9.57e-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: 56.39 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 322 YKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVR----------FGYYSQDGLQF 390
Cdd:cd03249 10 YPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 DeqmkvidvvQDIAEVIELGNGKRLT------ASQFLQHFLFT--PETQHSYV----YKLSGGERRRLYLCTVLMRNPNF 458
Cdd:cd03249 90 D---------GTIAENIRYGKPDATDeeveeaAKKANIHDFIMslPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2524717128 459 LVLDEPTNDLDIVTLNVLEEYLRNFKG--CVIVVSH 492
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
306-510 |
9.91e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 306 VKASYIGSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRFG--Y 382
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdGKVLYFGkdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 YSQDGLQFDEQMKVI----------DVVQDIAE------VIELGNGKRLTASQFLQHFLFTP--ETQHSYVYKLSGGERR 444
Cdd:PRK14246 81 FQIDAIKLRKEVGMVfqqpnpfphlSIYDNIAYplkshgIKEKREIKKIVEECLRKVGLWKEvyDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 445 RLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG--CVIVVSHDRYFMDKVVDHL-LVFNGQ 510
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVaFLYNGE 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-186 |
1.08e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 14 TKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGK---EGYDSGTISFRRDI------RVGYLEQDPQYPEE 84
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqgNNFTGTILANNRKPtkqilkRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 85 LTVLEACFHhgnstVELIKeyercmetdghpgLDGILARMDHEKAweyeqkAKQILSQLKIRDF------NQQVKSLSGG 158
Cdd:PLN03211 155 LTVRETLVF-----CSLLR-------------LPKSLTKQEKILV------AESVISELGLTKCentiigNSFIRGISGG 210
|
170 180
....*....|....*....|....*...
gi 2524717128 159 QLKRVALANTLITEPDLLILDEPTNHLD 186
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-221 |
1.26e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG--KEGYDSGTISFRRDiRVGYLEQDPQ 80
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtKDNWRVTADRMRFD-DIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 81 YPEELTvleacfhhGNSTVELIKEYERCMETDGHPGLDGILARmdheKAWEYE-----------QKAKQILSQLKIRDFN 149
Cdd:PRK15093 82 ERRKLV--------GHNVSMIFQEPQSCLDPSERVGRQLMQNI----PGWTYKgrwwqrfgwrkRRAIELLHRVGIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKS----LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR----TNLTLLMVTHDRYFLDRVCSEI 221
Cdd:PRK15093 150 DAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnqnNNTTILLISHDLQMLSQWADKI 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-227 |
1.27e-08 |
|
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: 54.75 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSfgdlVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------------RRDIRVGY 74
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQypEELTVLEAcfhhgnSTVELIkeyercmetdghpgldgilarmdhekaweyeqkakqILSQLkirdfnqqvks 154
Cdd:cd03215 80 VPEDRK--REGLVLDL------SVAENI------------------------------------ALSSL----------- 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEwlEDY-----LRRTNLTLLMVTHDryfLDrvcsEIIEIDNR 227
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA--EIYrlireLADAGKAVLLISSE---LD----ELLGLCDR 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-227 |
1.34e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLT--KSFGDLVLfENISFGLSEGQRVGL--IAknGSGKSTLLNILSGKEGYDSGTISF------------RRDI 70
Cdd:COG3845 257 VLEVENLSvrDDRGVPAL-KDVSLEVRAGEILGIagVA--GNGQSELAEALAGLRPPASGSIRLdgeditglspreRRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 RVGYLEQDPQypeeltvleacfHHG---NSTVE---LIKEYERcmETDGHPGLdgilarMDHEKAweyEQKAKQILSQLK 144
Cdd:COG3845 334 GVAYIPEDRL------------GRGlvpDMSVAenlILGRYRR--PPFSRGGF------LDRKAI---RAFAEELIEEFD 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 145 IR--DFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYL---RRTNLTLLMVTHDryfLDrvcs 219
Cdd:COG3845 391 VRtpGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlelRDAGAAVLLISED---LD---- 463
|
....*...
gi 2524717128 220 EIIEIDNR 227
Cdd:COG3845 464 EILALSDR 471
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-232 |
1.51e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF---GDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNI---LSGKEG--------YDSGTI-SFRRDIRV 72
Cdd:TIGR01271 1218 MDVQGLTAKYteaGRAVL-QDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGeiqidgvsWNSVTLqTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 gyleqdpqYPEELTVLEACFHhgnstvelikeyercMETDGHpgldgilARMDHEKAWEYEQKA--KQILSQLKIR-DFn 149
Cdd:TIGR01271 1297 --------IPQKVFIFSGTFR---------------KNLDPY-------EQWSDEEIWKVAEEVglKSVIEQFPDKlDF- 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 150 QQVKS---LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRT--NLTLLMVTHdryfldRV-----CS 219
Cdd:TIGR01271 1346 VLVDGgyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEH------RVealleCQ 1419
|
250
....*....|...
gi 2524717128 220 EIIEIDNRRIYQY 232
Cdd:TIGR01271 1420 QFLVIEGSSVKQY 1432
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
327-508 |
1.70e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 327 DLKILDDFSYIFARYEKMGIVGNNGTGKSTFIkilmrheQADRGAL--DIGETVRFGYYSQDGL---------------- 388
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMI-------QLTNGLIisETGQTIVGDYAIPANLkkikevkrlrkeiglv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 389 -QFDEQMKVIDVVQ-DIA-EVIELGNGKRlTASQFLQHFLFTPETQHSYV----YKLSGGERRRLYLCTVLMRNPNFLVL 461
Cdd:PRK13645 96 fQFPEYQLFQETIEkDIAfGPVNLGENKQ-EAYKKVPELLKLVQLPEDYVkrspFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 462 DEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:PRK13645 175 DEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMH 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
330-493 |
1.70e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILmrheqadrGALDI---GETVrFGYYSQDGL-----------------Q 389
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL--------GGLDTptsGDVI-FNGQPMSKLssaakaelrnqklgfiyQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 390 FDEQMKVIDVVQDIAEVIELGNGKRLTASQFLQHFLFTPETQHSYVYK---LSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:PRK11629 95 FHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRpseLSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|.
gi 2524717128 467 DLDIVT----LNVLEEYLRNFKGCVIVVSHD 493
Cdd:PRK11629 175 NLDARNadsiFQLLGELNRLQGTAFLVVTHD 205
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-212 |
1.89e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF--------RRDIRVGYLEQD 78
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgktatrgDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 79 PQYPEELTVLEAcFHHGNstvelikeyercmetdghpGLDGILARmdhekaweyeQKAKQILSQLKIRDFNQQ-VKSLSG 157
Cdd:PRK13543 91 PGLKADLSTLEN-LHFLC-------------------GLHGRRAK----------QMPGSALAIVGLAGYEDTlVRQLSA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNLTLLmVTHDRY 212
Cdd:PRK13543 141 GQKKRLALARLWLSPAPLWLLDEPYANLDLEgitlVNRMISAHLRGGGAALV-TTHGAY 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-510 |
2.03e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 292 VAKQRFNNDNVKLDVKASyigSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA 371
Cdd:PRK14271 1 MACERLGGQSGAADVDAA---APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 372 LDIGETVRFG---YYSQDGLQFDEQ------------MKVIDVVQDIAEVIELGNGKR---LTASQFLQHFLF--TPETQ 431
Cdd:PRK14271 78 RYSGDVLLGGrsiFNYRDVLEFRRRvgmlfqrpnpfpMSIMDNVLAGVRAHKLVPRKEfrgVAQARLTEVGLWdaVKDRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 432 HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF--KGCVIVVSHDRYFMDKVVDH-LLVFN 508
Cdd:PRK14271 158 SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLAQAARISDRaALFFD 237
|
..
gi 2524717128 509 GQ 510
Cdd:PRK14271 238 GR 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-217 |
2.18e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.81 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDS-----GTISF------RRD 69
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfnqniyERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IRVGYLEQDPQ--YPEELTVLEACFHHGNSTVELIkeyercmetDGHPG--LDGILarmdhekawEYEQKAKQILSQLKi 145
Cdd:PRK14258 81 VNLNRLRRQVSmvHPKPNLFPMSVYDNVAYGVKIV---------GWRPKleIDDIV---------ESALKDADLWDEIK- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 146 RDFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRV 217
Cdd:PRK14258 142 HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
7-217 |
2.42e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSF---GDLVLF----------ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF------- 66
Cdd:PRK15079 8 LLEVADLKVHFdikDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkdllg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 67 ---------RRDIRVGYleQDPqypeeLTVLEACFHHGNSTVELIKEYercmetdgHPGLdgilarmdheKAWEYEQKAK 137
Cdd:PRK15079 88 mkddewravRSDIQMIF--QDP-----LASLNPRMTIGEIIAEPLRTY--------HPKL----------SRQEVKDRVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 138 QILSQLKIRD--FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDM----TEWLEDYLRRTNLTLLMVTHD- 210
Cdd:PRK15079 143 AMMLKVGLLPnlINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIqaqvVNLLQQLQREMGLSLIFIAHDl 222
|
250
....*....|
gi 2524717128 211 ---RYFLDRV 217
Cdd:PRK15079 223 avvKHISDRV 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-209 |
2.82e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.04 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLL---N---------------ILSGKEGYDSG 62
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndlipgarvegeiLLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 63 T--ISFRRdiRVGYLEQDPQyPEELTVleacfhhgnstvelikeYE------RcmetdghpgLDGILAR--MDH--EKA- 129
Cdd:COG1117 85 VdvVELRR--RVGMVFQKPN-PFPKSI-----------------YDnvayglR---------LHGIKSKseLDEivEESl 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 130 -----WEyEQKAKqilsqLKirdfnQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR--RTNL 202
Cdd:COG1117 136 rkaalWD-EVKDR-----LK-----KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILelKKDY 204
|
....*..
gi 2524717128 203 TLLMVTH 209
Cdd:COG1117 205 TIVIVTH 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
333-506 |
2.84e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 333 DFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIG---------ETVRFGYYSQDGLQ----------FDEQ 393
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrQVIELSEQSAAQMRhvrgadmamiFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 394 MK----VIDVVQDIAEVIELGNG----KRLTASQFLQHFLFTPETQ---HSYVYKLSGGERRRLYLCTVLMRNPNFLVLD 462
Cdd:PRK10261 114 MTslnpVFTVGEQIAESIRLHQGasreEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524717128 463 EPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV 506
Cdd:PRK10261 194 EPTTALDVTiqaqILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-229 |
3.06e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.96 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 9 QVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTI----------------SFRR 68
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltalsekelrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 69 DIrvGYLeqdpqypeeltvleacFHHGN----STVelikeYERC---METDGHPgldgilarmdheKAwEYEQKAKQILS 141
Cdd:PRK11153 83 QI--GMI----------------FQHFNllssRTV-----FDNValpLELAGTP------------KA-EIKARVTELLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 142 QLKIRDFNQQVKS-LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMT----EWLEDYLRRTNLTLLMVTHDRYFLDR 216
Cdd:PRK11153 127 LVGLSDKADRYPAqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINRELGLTIVLITHEMDVVKR 206
|
250
....*....|...
gi 2524717128 217 VCSEIIEIDNRRI 229
Cdd:PRK11153 207 ICDRVAVIDAGRL 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-209 |
3.13e-08 |
|
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: 56.65 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG--DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR----RDIRVGYLEQDPQY 81
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 82 PEELTVLeacFhhgNSTVELIKEYERCMETDghpgldgilaRMDHEKAWEyEQKAKQILSQLKiRDFNQQVKS----LSG 157
Cdd:TIGR02203 411 VSQDVVL---F---NDTIANNIAYGRTEQAD----------RAEIERALA-AAYAQDFVDKLP-LGLDTPIGEngvlLSG 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 158 GQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTH 209
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERlmQGRTTLVIAH 526
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-248 |
3.24e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAVNSILQVENLTKSF---GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILS-------GKEGYDSGTISFRRDI 70
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 ----------RVGYLEQDPQYPEELTVLEACFH----HG-NSTVELIKEYERCMETDGhpgldgilarmdhekAWeyeqk 135
Cdd:PRK14246 81 fqidaiklrkEVGMVFQQPNPFPHLSIYDNIAYplksHGiKEKREIKKIVEECLRKVG---------------LW----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 136 aKQILSQLkirdfNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR--RTNLTLLMVTHDRYF 213
Cdd:PRK14246 141 -KEVYDRL-----NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITelKNEIAIVIVSHNPQQ 214
|
250 260 270
....*....|....*....|....*....|....*
gi 2524717128 214 LDRVCSEIIEIDNRRIYQYKGNYSYYLEKREERIE 248
Cdd:PRK14246 215 VARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
313-493 |
3.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEAdhlyKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILmrheqadrGALDIGE--TVRFGYYSQdglQF 390
Cdd:PRK13651 9 VKIFNK----KLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHL--------NALLLPDtgTIEWIFKDE---KN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 DEQMKVIDVVQDiAEVIELGNGKRL-----------TASQFLQHFLF--TPETQ-------------------------- 431
Cdd:PRK13651 74 KKKTKEKEKVLE-KLVIQKTRFKKIkkikeirrrvgVVFQFAEYQLFeqTIEKDiifgpvsmgvskeeakkraakyielv 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 432 ---HSYVYK----LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD----IVTLNVLEEYLRNFKgCVIVVSHD 493
Cdd:PRK13651 153 gldESYLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQGK-TIILVTHD 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
346-516 |
4.18e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILmrheqADRGALDIGE-TVRFGYYSQdgLQFDEQMKVI-----------------DVVQDIAEVI 407
Cdd:PRK10938 34 FVGANGSGKSALARAL-----AGELPLLSGErQSQFSHITR--LSFEQLQKLVsdewqrnntdmlspgedDTGRTTAEII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 408 ELGNGKRLTASQFLQHFLFTPETQHSYVYkLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLR--NFKG 485
Cdd:PRK10938 107 QDEVKDPARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAslHQSG 185
|
170 180 190
....*....|....*....|....*....|.
gi 2524717128 486 CVIVvshdryfmdkvvdhlLVFNGQGDIRDF 516
Cdd:PRK10938 186 ITLV---------------LVLNRFDEIPDF 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
326-510 |
4.56e-08 |
|
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: 54.08 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVR--FGYysqdGLQFDEQMKVID----- 398
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSslLGL----GGGFNPELTGREniyln 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 399 -------------VVQDIAEVIELGNgkrltasqflqhFLFTPetqhsyVYKLSGGERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:cd03220 109 grllglsrkeideKIDEIIEFSELGD------------FIDLP------VKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524717128 466 NDLDIVT----LNVLEEYLRNFKGcVIVVSHDRYFMDKVVDHLLVF-NGQ 510
Cdd:cd03220 171 AVGDAAFqekcQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLeKGK 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
317-464 |
4.82e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.26 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA--LDiGETV---------RFG--YY 383
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRifLD-GEDIthlpmhkraRLGigYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 SQDGLQFdEQMKVIDVVQDIAEVIELGNGKR---LTA--SQF-LQHFlftpetQHSYVYKLSGGERRRLYLCTVLMRNPN 457
Cdd:COG1137 84 PQEASIF-RKLTVEDNILAVLELRKLSKKEReerLEEllEEFgITHL------RKSKAYSLSGGERRRVEIARALATNPK 156
|
....*..
gi 2524717128 458 FLVLDEP 464
Cdd:COG1137 157 FILLDEP 163
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
322-509 |
5.03e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.01 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 322 YKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA--LD------------------IG-ETVRF 380
Cdd:cd03248 21 YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlLDgkpisqyehkylhskvslVGqEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 381 GYYSQDGLQFDEQMKVIDVVQDIAEVIELGNgkrltasqflqhflFTPETQHSYVY-------KLSGGERRRLYLCTVLM 453
Cdd:cd03248 101 ARSLQDNIAYGLQSCSFECVKEAAQKAHAHS--------------FISELASGYDTevgekgsQLSGGQKQRVAIARALI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 454 RNPNFLVLDEPTNDLDIVTLNVLEEYLR--NFKGCVIVVSHdRYFMDKVVDHLLVFNG 509
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAH-RLSTVERADQILVLDG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
315-493 |
5.05e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRfgYYSQDGLQFD-EQ 393
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAG------EVH--YRMRDGQLRDlYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 394 MKVID-----------VVQDIAE-----VIELGN-GKRL-------------TASQFLQHFLFTPETQHSYVYKLSGGER 443
Cdd:PRK11701 78 LSEAErrrllrtewgfVHQHPRDglrmqVSAGGNiGERLmavgarhygdiraTAGDWLERVEIDAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 444 RRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHD 493
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHD 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-210 |
5.27e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.17 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 26 ISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYdSGTISF---------------RRdirvGYLEQDPQYPEELTVlea 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFagqpleawsaaelarHR----AYLSQQQTPPFAMPV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 91 cFHHgnstvelikeyercmetdghpgldgiLARMDHEKAWEYEQKA--KQILSQLKIRDF-NQQVKSLSGGQLKRVALAN 167
Cdd:PRK03695 87 -FQY--------------------------LTLHQPDKTRTEAVASalNEVAEALGLDDKlGRSVNQLSGGEWQRVRLAA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 168 TLI-----TEPD--LLILDEPTNHLDLDMTEWLEDYLR---RTNLTLLMVTHD 210
Cdd:PRK03695 140 VVLqvwpdINPAgqLLLLDEPMNSLDVAQQAALDRLLSelcQQGIAVVMSSHD 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
346-511 |
5.84e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILMRHE--QADRGALDIGEtvrfgyysqdgLQFDEQMKVIDVV---QDIAEVIELGNGKRLTASQF 420
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD-----------NQFGREASLIDAIgrkGDFKDAVELLNAVGLSDAVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 421 lqhFLFTPETqhsyvykLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD-----IVTLNVLEEyLRNFKGCVIVVSHDRY 495
Cdd:COG2401 130 ---WLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtakRVARNLQKL-ARRAGITLVVATHHYD 198
|
170
....*....|....*.
gi 2524717128 496 FMDKVVDHLLVFNGQG 511
Cdd:COG2401 199 VIDDLQPDLLIFVGYG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
317-492 |
5.99e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRF-----------GYYS 384
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIrsprdaialgiGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 385 QDGLQFDEqMKVidvvqdiAEVIELGNG-------------KRLTAsqFLQHFLFT--PetqHSYVYKLSGGERRRLYLC 449
Cdd:COG3845 87 QHFMLVPN-LTV-------AENIVLGLEptkggrldrkaarARIRE--LSERYGLDvdP---DAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 450 TVLMRNPNFLVLDEPTndldivtlNVL---E-----EYLRNFK--GC-VIVVSH 492
Cdd:COG3845 154 KALYRGARILILDEPT--------AVLtpqEadelfEILRRLAaeGKsIIFITH 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
324-469 |
6.02e-08 |
|
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: 55.60 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SFG---DLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRfgYYSQDGLQfdeqmKVIDV 399
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIR--DVTQASLR-----AAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 400 V-QD-------IAEVIELGngkRLTASQ--------------FLQHflfTPETQHSYV----YKLSGGERRRLYLCTVLM 453
Cdd:COG5265 437 VpQDtvlfndtIAYNIAYG---RPDASEeeveaaaraaqihdFIES---LPDGYDTRVgergLKLSGGEKQRVAIARTLL 510
|
170
....*....|....*.
gi 2524717128 454 RNPNFLVLDEPTNDLD 469
Cdd:COG5265 511 KNPPILIFDEATSALD 526
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-513 |
6.16e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 53.65 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 333 DFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGEtVRFGYYS----------QDGLQFDEqmkvIDVVQD 402
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPpadrpvsmlfQENNLFAH----LTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 403 IAevIELGNGKRLTASQF-----------LQHFLF-TPETqhsyvykLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:cd03298 91 VG--LGLSPGLKLTAEDRqaievalarvgLAGLEKrLPGE-------LSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524717128 471 V----TLNVLEEYLRNFKGCVIVVSHdrYFMD-KVVDHLLVFNGQGDI 513
Cdd:cd03298 162 AlraeMLDLVLDLHAETKMTVLMVTH--QPEDaKRLAQRVVFLDNGRI 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
315-500 |
7.24e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.74 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSF-----------GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGyy 383
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSG------EILFD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 SQDGLQFDE----------QMkvidVVQD--------------IAEVIEL-GNGKRLTASQFLQHFLFT----PETQHSY 434
Cdd:COG4608 79 GQDITGLSGrelrplrrrmQM----VFQDpyaslnprmtvgdiIAEPLRIhGLASKAERRERVAELLELvglrPEHADRY 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 435 VYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI-----VtLNVLEEYLRNFKGCVIVVSHD----RYFMDKV 500
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaqV-LNLLEDLQDELGLTYLFISHDlsvvRHISDRV 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-210 |
8.39e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-----RRDIR---VGYLEQDPQYPEELTVLEacfhhgn 96
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptRQALQknlVAYVPQSEEVDWSFPVLV------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 97 STVELIKEYercmetdGHPGLDGILARMDHekaweyeQKAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDL 175
Cdd:PRK15056 98 EDVVMMGRY-------GHMGWLRRAKKRDR-------QIVTAALARVDMVEFrHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524717128 176 LILDEPTNHLDLDmTEW----LEDYLRRTNLTLLMVTHD 210
Cdd:PRK15056 164 ILLDEPFTGVDVK-TEAriisLLRELRDEGKTMLVSTHN 201
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-211 |
9.17e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.97 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNIL-------SGK---EGYDSGTI---SFRRDIRVGYleQDPqypeeltvleA 90
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRiliDGTDIRTVtraSLRRNIAVVF--QDA----------G 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 91 CFhhgNSTvelIKEYERCmetdGHPglDGILARMdhEKAWEYEQKAKQILSQLKIRDFN--QQVKSLSGGQLKRVALANT 168
Cdd:PRK13657 420 LF---NRS---IEDNIRV----GRP--DATDEEM--RAAAERAQAHDFIERKPDGYDTVvgERGRQLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524717128 169 LITEPDLLILDEPTNHLDLDmTEwledylRRTNLTLLMVTHDR 211
Cdd:PRK13657 486 LLKDPPILILDEATSALDVE-TE------AKVKAALDELMKGR 521
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-493 |
9.19e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 52.62 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGlQFDEQM--KVIDVVQdIAEVIELGNGKRLTA------ 417
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRS-EVPDSLplTVRDLVA-MGRWARRGLWRRLTRddraav 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 418 SQFLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSHD 493
Cdd:NF040873 101 DDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
317-509 |
9.56e-08 |
|
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: 53.46 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDL-KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRfgyySQDGLQFDEQM 394
Cdd:cd03295 2 EFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIR----EQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 K-VID---------VVQDIAEVIELGNGKRLT----ASQFLQHFLFTPET-QHSYVYKLSGGERRRLYLCTVLMRNPNFL 459
Cdd:cd03295 78 GyVIQqiglfphmtVEENIALVPKLLKWPKEKirerADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 460 VLDEPTNDLDIVTLNVLEEYLRNFK---GCVIV-VSHDryfMD---KVVDHLLVFNG 509
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQqelGKTIVfVTHD---IDeafRLADRIAIMKN 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-229 |
1.11e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 5 NSILQVENLTKSF----GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGT----------------I 64
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvatldadalA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 65 SFRRDiRVGYLEQDPQYPEELTVLEacfhhgnsTVELIKEYercmetdghPGLdgilarmdhEKAwEYEQKAKQILSQLK 144
Cdd:PRK10535 82 QLRRE-HFGFIFQRYHLLSHLTAAQ--------NVEVPAVY---------AGL---------ERK-QRLLRAQELLQRLG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 145 IRD-FNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTE---WLEDYLRRTNLTLLMVTHDRYFLDRVcSE 220
Cdd:PRK10535 134 LEDrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRDRGHTVIIVTHDPQVAAQA-ER 212
|
....*....
gi 2524717128 221 IIEIDNRRI 229
Cdd:PRK10535 213 VIEIRDGEI 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-234 |
1.17e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 26 ISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGtisfrrDIRVGYLEQDPQYPEELTVL-EACFhhgnSTVELike 104
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG------EILLDGKPVTAEQPEDYRKLfSAVF----TDFHL--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 105 YERCMETDGHPGLDGILArmdhekAW--EYEQKAKQILSQLKIRDFNqqvksLSGGQLKRVALANTLITEPDLLILDept 182
Cdd:PRK10522 409 FDQLLGPEGKPANPALVE------KWleRLKMAHKLELEDGRISNLK-----LSKGQKKRLALLLALAEERDILLLD--- 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 183 nhldldmtEWLED---------------YLRRTNLTLLMVTH-DRYFL--DRvcseIIEIDNRRIYQYKG 234
Cdd:PRK10522 475 --------EWAADqdphfrrefyqvllpLLQEMGKTIFAISHdDHYFIhaDR----LLEMRNGQLSELTG 532
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-186 |
1.44e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 52.93 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 23 FENISFGLSEGQRVGLIAKNGSGKSTLLNILsgKEGYD--SGTISF-RRDIR----------VGYLEQDPqypeeltVLE 89
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERFYDptSGEILLdGVDIRdlnlrwlrsqIGLVSQEP-------VLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 90 ACfhhgnSTVELIKeYERCMETDGhpgldgilarmdhekawEYEQKAKQILSQLKIRD----FNQQV----KSLSGGQLK 161
Cdd:cd03249 90 DG-----TIAENIR-YGKPDATDE-----------------EVEEAAKKANIHDFIMSlpdgYDTLVgergSQLSGGQKQ 146
|
170 180
....*....|....*....|....*
gi 2524717128 162 RVALANTLITEPDLLILDEPTNHLD 186
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALD 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
329-490 |
1.45e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.41 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 329 KILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGAL-----DIG----ETVR--FGYYSQDGLQFDEQMKV- 396
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeidgiDIStiplEDLRssLTIIPQDPTLFSGTIRSn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 397 IDVV-----QDIAEVIELGNGKRltasqflqhflftpetqhsyvyKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV 471
Cdd:cd03369 102 LDPFdeysdEEIYGALRVSEGGL----------------------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180
....*....|....*....|
gi 2524717128 472 TLNVLEEYLRN-FKGCVIVV 490
Cdd:cd03369 160 TDALIQKTIREeFTNSTILT 179
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
321-513 |
1.64e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 321 LYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKST-FIKI--LMRHEQ------------ADRGALDIGETVRFGYysQ 385
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTlFMNLsgLLRPQKgavlwqgkpldySKRGLLALRQQVATVF--Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 386 DGlqfDEQMKVIDVVQDIA------EVIELGNGKRLTASQFL---QHFlftpetQHSYVYKLSGGERRRLYLCTVLMRNP 456
Cdd:PRK13638 85 DP---EQQIFYTDIDSDIAfslrnlGVPEAEITRRVDEALTLvdaQHF------RHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 457 NFLVLDEPTNDLDIVTLNVLEEYLRNFKGC---VIVVSHDRYFMDKVVDHLLVFNgQGDI 513
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLR-QGQI 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
346-513 |
1.84e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.39 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILmrheqadrgaldigetvrfgyysqdglqfdeqmkvidvvqdiAEVIELGNGK--RLTASqflqH 423
Cdd:cd03223 32 ITGPSGTGKSSLFRAL------------------------------------------AGLWPWGSGRigMPEGE----D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 424 FLFTPetQHSY----------VY----KLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIV 489
Cdd:cd03223 66 LLFLP--QRPYlplgtlreqlIYpwddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVIS 143
|
170 180
....*....|....*....|....
gi 2524717128 490 VSHdRYFMDKVVDHLLVFNGQGDI 513
Cdd:cd03223 144 VGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
436-508 |
1.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 436 YKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:PRK13637 143 FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeiLNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMN 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-228 |
1.96e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFG-----------DLVLFENISFGLSEGQRVGLIAKNGSGKST----LLNILSGKEGY------------ 59
Cdd:PRK10261 313 ILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQGGEiifngqridtls 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 60 DSGTISFRRDIRvgYLEQDP--QYPEELTVleacfhhGNSTVELIKEyercmetdgHPGLDGILAR-----------MDH 126
Cdd:PRK10261 393 PGKLQALRRDIQ--FIFQDPyaSLDPRQTV-------GDSIMEPLRV---------HGLLPGKAAAarvawllervgLLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 127 EKAWEYEQKakqilsqlkirdfnqqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDLD----MTEWLEDYLRRTNL 202
Cdd:PRK10261 455 EHAWRYPHE-------------------FSGGQRQRICIARALALNPKVIIADEAVSALDVSirgqIINLLLDLQRDFGI 515
|
250 260 270
....*....|....*....|....*....|....
gi 2524717128 203 TLLMVTHDRYFLDRVC--------SEIIEIDNRR 228
Cdd:PRK10261 516 AYLFISHDMAVVERIShrvavmylGQIVEIGPRR 549
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
345-503 |
2.21e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.81 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 345 GIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGL-----------QFDE-QMKVIDVVQDIAEVIE-LGN 411
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIkpvrkkvgvvfQFPEsQLFEETVLKDVAFGPQnFGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 412 GKRLT---ASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI---VTLNVLEEYLRNFKG 485
Cdd:PRK13643 116 PKEKAekiAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkarIEMMQLFESIHQSGQ 195
|
170
....*....|....*...
gi 2524717128 486 CVIVVSHdryFMDKVVDH 503
Cdd:PRK13643 196 TVVLVTH---LMDDVADY 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-186 |
2.35e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 15 KSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGydsGTISFRRDIRVGYLEQDPqypeeltvlEACFHH 94
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHYNGIPYKE---------FAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 95 GnstvelikEYERCMETDGHPgldgilarmdhekaweyeqkakqilSQLKIR---DF------NQQVKSLSGGQLKRVAL 165
Cdd:cd03233 83 G--------EIIYVSEEDVHF-------------------------PTLTVRetlDFalrckgNEFVRGISGGERKRVSI 129
|
170 180
....*....|....*....|.
gi 2524717128 166 ANTLITEPDLLILDEPTNHLD 186
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
346-499 |
2.44e-07 |
|
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: 51.45 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIkilmrheqadrgaldigETVRFGYY-----SQDGLQFDEqmKVIDVVQDIAEV---IELGNGKRLTA 417
Cdd:cd03240 27 IVGQNGAGKTTII-----------------EALKYALTgelppNSKGGAHDP--KLIREGEVRAQVklaFENANGKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 418 SQFLQHFL----------FTPETQHsyVYKLSGGERR------RLYLCTVLMRNPNFLVLDEPTNDLD-----IVTLNVL 476
Cdd:cd03240 88 TRSLAILEnvifchqgesNWPLLDM--RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieESLAEII 165
|
170 180
....*....|....*....|...
gi 2524717128 477 EEYLRNFKGCVIVVSHDRYFMDK 499
Cdd:cd03240 166 EERKSQKNFQLIVITHDEELVDA 188
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
323-469 |
2.46e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 323 KSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILmrheqadrgALDIGETVRF-GYYSQDGLQFDE-----QMKV 396
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL---------ANRTEGNVSVeGDIHYNGIPYKEfaekyPGEI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 397 IDVVQD---IAEvielgngkrLTASQFLQhflFTPETQ-HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD 469
Cdd:cd03233 86 IYVSEEdvhFPT---------LTVRETLD---FALRCKgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-520 |
2.69e-07 |
|
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: 52.37 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 344 MGIVGNNGTGKSTFIKILMRHEQADRGAL----DIGETVRfgYYSQDGLQ------FDEQMKVIDVVQDIAEVIELGNGK 413
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEILD--EFRGSELQnyftklLEGDVKVIVKPQYVDLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 414 ------RLTASQFLQHFLFTPETQH---SYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI---VTLNVLEEYLR 481
Cdd:cd03236 107 vgellkKKDERGKLDELVDQLELRHvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIRELA 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524717128 482 NFKGCVIVVSHDRYFMDKVVDHLLVFNGQgdirdfPGNY 520
Cdd:cd03236 187 EDDNYVLVVEHDLAVLDYLSDYIHCLYGE------PGAY 219
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
152-224 |
2.78e-07 |
|
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: 51.45 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 152 VKSLSGGQ------LKRVALANTLITEPDLLILDEPTNHLDLD-----MTEWLEDYLRRTNLTLLMVTHDRYFLDRVcSE 220
Cdd:cd03240 113 RGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEEnieesLAEIIEERKSQKNFQLIVITHDEELVDAA-DH 191
|
....
gi 2524717128 221 IIEI 224
Cdd:cd03240 192 IYRV 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-209 |
3.67e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.19 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 19 DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISfrrdirvgyLEQDPqypeeLTVLEACFHHgnST 98
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL---------LDGVP-----LVQYDHHYLH--RQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 99 VELIKE----YERCMETDGHPGLDgiLARMDHEKAWEYEQKAKQILSQLKiRDFNQQVKS----LSGGQLKRVALANTLI 170
Cdd:TIGR00958 557 VALVGQepvlFSGSVRENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFP-NGYDTEVGEkgsqLSGGQKQRIAIARALV 633
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524717128 171 TEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLTLLMVTH 209
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-470 |
4.06e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR---------RDIR---VGY 74
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLgkevtfngpKSSQeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDPQYPEELTVLEACFhhgnstveLIKEYErcmetdghpgldGILARMDHEKAWeyeQKAKQILSQLKIRDFNQQ-VK 153
Cdd:PRK10762 84 IHQELNLIPQLTIAENIF--------LGREFV------------NRFGRIDWKKMY---AEADKLLARLNLRFSSDKlVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 154 SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWL-----EdyLRRTNLTLLMVTHdryfldRVcSEIIEIDNR- 227
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLfrvirE--LKSQGRGIVYISH------RL-KEIFEICDDv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 228 ---RIYQYKGnysyylekreERIEAKTVEieraNNLyrteLEWM--RRMpqarghkaryrEDAFYELEKVAKQrfnndnV 302
Cdd:PRK10762 212 tvfRDGQFIA----------EREVADLTE----DSL----IEMMvgRKL-----------EDQYPRLDKAPGE------V 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 303 KLDVKaSYIGSKIfeadhlyksfgdlkilDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVR-- 379
Cdd:PRK10762 257 RLKVD-NLSGPGV----------------NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtr 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 380 ---------FGYYSQD--------GLQFDEQMKVIDVVQDIAEVIELGNGK-RLTASQFLQHF-LFTPeTQHSYVYKLSG 440
Cdd:PRK10762 320 spqdglangIVYISEDrkrdglvlGMSVKENMSLTALRYFSRAGGSLKHADeQQAVSDFIRLFnIKTP-SMEQAIGLLSG 398
|
490 500 510
....*....|....*....|....*....|
gi 2524717128 441 GERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
438-510 |
4.09e-07 |
|
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: 52.83 E-value: 4.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK---GCVIVVSHDRYFMdKVVDHLLVF-NGQ 510
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLL-AAVDKLLVLrDGR 543
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-244 |
4.61e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSfGdlvlFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIR----VGYLEQDPQY 81
Cdd:PRK15439 268 VLTVEDLTGE-G----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgKEINalstAQRLARGLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 82 -PEELTV----LEACFHhgnstvelikeYERCMETDGHPGLdgilarmdhekaWEYEQKAKQILSQ------LKIRDFNQ 150
Cdd:PRK15439 343 lPEDRQSsglyLDAPLA-----------WNVCALTHNRRGF------------WIKPARENAVLERyrralnIKFNHAEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL----DMTEWLEDyLRRTNLTLLMVTHDryfLDrvcsEIIEIDN 226
Cdd:PRK15439 400 AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVsarnDIYQLIRS-IAAQNVAVLFISSD---LE----EIEQMAD 471
|
250
....*....|....*...
gi 2524717128 227 RRIYQYKGNYSYYLEKRE 244
Cdd:PRK15439 472 RVLVMHQGEISGALTGAA 489
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-222 |
5.84e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIS-------------FRRDIR--VGYLEQDP--QYPEELTV 87
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkYIRPVRkrIGMVFQFPesQLFEDTVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 88 LEACFHHGNstvelikeyercmetdghpgldgilARMDHEKAWEYeqkAKQILSQLKI-RDFNQQVK-SLSGGQLKRVAL 165
Cdd:PRK13646 105 REIIFGPKN-------------------------FKMNLDEVKNY---AHRLLMDLGFsRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 166 ANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVI 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
322-532 |
6.30e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.42 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 322 YKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI---------------------GETVRF 380
Cdd:TIGR00958 488 YPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdgvplvqydhhylhrqvalvgQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 381 GYYSQD----GLQFDEQMKVIDVVqdiaevielgngKRLTASQFLQHFlftPETQHSYV----YKLSGGERRRLYLCTVL 452
Cdd:TIGR00958 568 SGSVREniayGLTDTPDEEIMAAA------------KAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 453 MRNPNFLVLDEPTNDLDIVTLNVLEEyLRNFKG-CVIVVSHDRYFMDKvVDHLLVFNgQGDIRDFpGNYTRYRDWKDAKA 531
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQE-SRSRASrTVLLIAHRLSTVER-ADQILVLK-KGSVVEM-GTHKQLMEDQGCYK 708
|
.
gi 2524717128 532 A 532
Cdd:TIGR00958 709 H 709
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-226 |
6.75e-07 |
|
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: 50.57 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSF---GDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNIL-------SGK---EGYDSGTISfRRDIR--V 72
Cdd:cd03244 3 IEFKNVSLRYrpnLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlvelsSGSiliDGVDISKIG-LHDLRsrI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 73 GYLEQDP---------------QYPEEltvleacfhhgnstvELIKEYERCmetdghpgldgilarmdheKAWEY-EQKA 136
Cdd:cd03244 81 SIIPQDPvlfsgtirsnldpfgEYSDE---------------ELWQALERV-------------------GLKEFvESLP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 137 KQILSQLKIRDFNqqvksLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRR--TNLTLLMVTH----- 209
Cdd:cd03244 127 GGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAHrldti 201
|
250 260
....*....|....*....|..
gi 2524717128 210 -DryfLDRVC----SEIIEIDN 226
Cdd:cd03244 202 iD---SDRILvldkGRVVEFDS 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
346-510 |
7.69e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 50.84 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILMRHE--QADRG----------ALDIGETVRFGYysqdGLQFdeQ-------MKVIDVVQDIAEV 406
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMGHPkyEVTSGsilldgedilELSPDERARAGI----FLAF--QypveipgVSVSNFLRTALNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 407 IelgNGKRLTASQFL-------------QHFLftpetqHSYV-YKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT 472
Cdd:COG0396 105 R---RGEELSAREFLkllkekmkelgldEDFL------DRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524717128 473 LNVLEEY---LRNFKGCVIVVSHDRYFMDKVV-DHLLVF-NGQ 510
Cdd:COG0396 176 LRIVAEGvnkLRSPDRGILIITHYQRILDYIKpDFVHVLvDGR 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
346-469 |
8.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGL-----------QFDE-QMKVIDVVQDIA-EVIELGNG 412
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLkplrkkvgivfQFPEhQLFEETVEKDICfGPMNFGVS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 413 K---RLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD 469
Cdd:PRK13634 118 EedaKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-53 |
8.77e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.01 E-value: 8.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2524717128 8 LQVENLTKSF---GDLVLfENISFGLSEGQRVGLIAKNGSGKSTLLNIL 53
Cdd:cd03289 3 MTVKDLTAKYtegGNAVL-ENISFSISPGQRVGLLGRTGSGKSTLLSAF 50
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
314-493 |
9.01e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.16 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 314 KIFEADHLYKSFGD----LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILmrheqadrGALDIGETVRFGYYSQDGLQ 389
Cdd:PRK10584 5 NIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAIL--------AGLDDGSSGEVSLVGQPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 390 FDEQMKVIDVVQDIAEVI-----------------------ELGNGKRLTASQFLQHFLFTPETQHsYVYKLSGGERRRL 446
Cdd:PRK10584 77 MDEEARAKLRAKHVGFVFqsfmliptlnalenvelpallrgESSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 447 YLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYL----RNFKGCVIVVSHD 493
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-230 |
9.54e-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: 52.32 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFglSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-RDIRVGY------LEQDPQYP---EELTVLEACFHH 94
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgKDIETNLdavrqsLGMCPQHNilfHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 95 ----GNSTVELIKEYERCMETDGhpgldgilarMDHEKaweyeqkakqilsqlkirdfNQQVKSLSGGQLKRVALANTLI 170
Cdd:TIGR01257 1028 aqlkGRSWEEAQLEMEAMLEDTG----------LHHKR--------------------NEEAQDLSGGMQRKLSVAIAFV 1077
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 171 TEPDLLILDEPTNHLDLDMTEWLEDYL--RRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIY 230
Cdd:TIGR01257 1078 GDAKVVVLDEPTSGVDPYSRRSIWDLLlkYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
317-505 |
1.00e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETvRFGYySQD---------- 386
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGH-QFDF-SQKpsekairllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 387 ---GLQFDE-----QMKVID-------VVQDIAEVIELGNGKRLTASQFLQHFLftpetqHSYVYKLSGGERRRLYLCTV 451
Cdd:COG4161 82 qkvGMVFQQynlwpHLTVMEnlieapcKVLGLSKEQAREKAMKLLARLRLTDKA------DRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 452 LMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVI---VVSHDRYFMDKVVDHLL 505
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVV 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-209 |
1.28e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNI------------------LSGKEGY--DSGTISFR 67
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrLFGRNIYspDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 68 RdiRVGYLEQDPQYPEELTVLEacfhhgNSTVELikeyercmetdghpGLDGIL-ARMDHEKAWEYEQKAKQILSQLKIR 146
Cdd:PRK14267 85 R--EVGMVFQYPNPFPHLTIYD------NVAIGV--------------KLNGLVkSKKELDERVEWALKKAALWDEVKDR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 147 dFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYL--RRTNLTLLMVTH 209
Cdd:PRK14267 143 -LNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfeLKKEYTIVLVTH 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
317-493 |
1.41e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.08 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYSQDGLQFDEQ--M 394
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEglL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQDIAEVIEL---GNGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV 471
Cdd:PRK11248 83 PWRNVQDNVAFGLQLagvEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*.
gi 2524717128 472 TLNVLEEYL----RNFKGCVIVVSHD 493
Cdd:PRK11248 163 TREQMQTLLlklwQETGKQVLLITHD 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-216 |
1.49e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISF-RRDI---RVGYLEQ----- 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIkkdLCTYQKQlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 78 -----DPQypeeLTVLEACFH--HGNSTVELIKEYERcmetdghpgldgiLARMDHekaweyeqkakqilsqlkIRDFNQ 150
Cdd:PRK13540 81 hrsgiNPY----LTLRENCLYdiHFSPGAVGITELCR-------------LFSLEH------------------LIDYPC 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 151 QVksLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYlRRTNLTLLMVTHDRYFLDR 216
Cdd:PRK13540 126 GL--LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelslLTIITKIQEH-RAKGGAVLLTSHQDLPLNK 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-193 |
1.49e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 19 DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFR-----RDI-------RVGYLEQDP------- 79
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDInlkwwrsKIGVVSQDPllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 ----QYP----EELTVLEACFHH-GNSTVELIKEYERCmETDGHPGLDGILARMDHEKAWEYEQKAKQI--------LSQ 142
Cdd:PTZ00265 477 knniKYSlyslKDLEALSNYYNEdGNDSQENKNKRNSC-RAKCAGDLNDMSNTTDSNELIEMRKNYQTIkdsevvdvSKK 555
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 143 LKIRDF------------NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDlDMTEWL 193
Cdd:PTZ00265 556 VLIHDFvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYL 617
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
331-508 |
1.90e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.75 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFGYYSQDGLQFDEQMKVIDVVQDIAEVIELG 410
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG------EIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 411 NGKRLTASQFLQHFLFTPETQHSYVYK-----------------LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTL 473
Cdd:PRK13648 99 SIVKYDVAFGLENHAVPYDEMHRRVSEalkqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524717128 474 NVLEEYLRNFKG----CVIVVSHDryfMDKVV--DHLLVFN 508
Cdd:PRK13648 179 QNLLDLVRKVKSehniTIISITHD---LSEAMeaDHVIVMN 216
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-224 |
1.96e-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: 48.47 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 149 NQQVKSLSGGQLKRVALANTLI--TEPDLLILDEPTNHLDLDMTEWLEDYLRR---TNLTLLMVTHDRYFLDRvCSEIIE 223
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGlidLGNTVILIEHNLDVLSS-ADWIID 160
|
.
gi 2524717128 224 I 224
Cdd:cd03238 161 F 161
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
326-515 |
2.02e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 326 GDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMrheqadrGAL----DIGETVRFgyysqDGLQF----------- 390
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALM-------GLLaangRIGGSATF-----NGREIlnlpekelnkl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 -DEQMKVIdvVQD--------------IAEVIELGNG-----------KRLTASQFlqhflftPETQHS---YVYKLSGG 441
Cdd:PRK09473 95 rAEQISMI--FQDpmtslnpymrvgeqLMEVLMLHKGmskaeafeesvRMLDAVKM-------PEARKRmkmYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 442 ERRRLYLCTVLMRNPNFLVLDEPTNDLD------IVTLnvLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV-FNGQ---- 510
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDvtvqaqIMTL--LNELKREFNTAIIMITHDLGVVAGICDKVLVmYAGRtmey 243
|
....*
gi 2524717128 511 GDIRD 515
Cdd:PRK09473 244 GNARD 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
317-465 |
2.05e-06 |
|
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: 48.97 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMR---------------------HEQADRG----- 370
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllpprsgsirfdgrditglppHERARAGigyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 371 -------ALDIGETVRFGYYSQDGLQFDEqmkvidvvqDIAEVIELgngkrltasqF--LQhflftpETQHSYVYKLSGG 441
Cdd:cd03224 82 egrrifpELTVEENLLLGAYARRRAKRKA---------RLERVYEL----------FprLK------ERRKQLAGTLSGG 136
|
170 180
....*....|....*....|....
gi 2524717128 442 ERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPS 160
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-515 |
2.07e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 50.61 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTfikiLMRheqADRGALDIGE-TVRFGYYSQDGLQFDE-QMKVIDVVQ 401
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLR---AINGTLTPTAgTVLVAGDDVEALSARAaSRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 402 DIA--------EVIELGNGKRLTasqflqHFLFTPETQHSYVYK-----------------LSGGERRRLYLCTVLMRNP 456
Cdd:PRK09536 85 DTSlsfefdvrQVVEMGRTPHRS------RFDTWTETDRAAVERamertgvaqfadrpvtsLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 457 NFLVLDEPTNDLDI----VTLNVLEEYLRNFKGCVIVVsHDRYFMDKVVDHLLVFNGqGDIRD 515
Cdd:PRK09536 159 PVLLLDEPTASLDInhqvRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLAD-GRVRA 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
306-494 |
2.21e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.22 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 306 VKASYIGSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGAL-----DIGET--- 377
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvDLSHVppy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 378 -----VRFGYYSQDGLQFDEQMKVIDVVQDIAEVIELGNgkRLTASQFLQHFL-FTPETQHsyvyKLSGGERRRLYLCTV 451
Cdd:PRK11607 90 qrpinMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIAS--RVNEMLGLVHMQeFAKRKPH----QLSGGQRQRVALARS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524717128 452 LMRNPNFLVLDEPTNDLDI-----VTLNVLEEYLRNFKGCVIvVSHDR 494
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKklrdrMQLEVVDILERVGVTCVM-VTHDQ 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
331-472 |
2.48e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.34 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVR----------FGYYSQDGLQFDeqmkvidv 399
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRtvtraslrrnIAVVFQDAGLFN-------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 400 vQDIAEVIELGN-----------GKRLTASQFLqhfLFTPETQHSYV----YKLSGGERRRLYLCTVLMRNPNFLVLDEP 464
Cdd:PRK13657 423 -RSIEDNIRVGRpdatdeemraaAERAQAHDFI---ERKPDGYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEA 498
|
....*...
gi 2524717128 465 TNDLDIVT 472
Cdd:PRK13657 499 TSALDVET 506
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
344-520 |
2.49e-06 |
|
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: 50.55 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 344 MGIVGNNGTGKSTFIKILM--------RHEqadrGALDIGETVRfgYYSQDGLQ------FDEQMKV------IDV---- 399
Cdd:COG1245 102 TGILGPNGIGKSTALKILSgelkpnlgDYD----EEPSWDEVLK--RFRGTELQdyfkklANGEIKVahkpqyVDLipkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 400 ----VQDIAE-VIELGNGKRLTASQFLQHFLftpetqHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT-L 473
Cdd:COG1245 176 fkgtVRELLEkVDERGKLDELAEKLGLENIL------DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQrL 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524717128 474 NV---LEEYLRNFKGcVIVVSHDRYFMDKVVDHLLVFNGQgdirdfPGNY 520
Cdd:COG1245 250 NVarlIRELAEEGKY-VLVVEHDLAILDYLADYVHILYGE------PGVY 292
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-186 |
3.02e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 18 GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKE--GYDSGTI----------SFRRdiRVGYLEQDPQYPEEL 85
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttGVITGGDrlvngrpldsSFQR--SIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 86 TVLEAcfhhgnstveLIkeyercmetdghpgldgILARMDHEKAWEYEQK---AKQILSQLKIRDFNQQVKSLSGG---- 158
Cdd:TIGR00956 852 TVRES----------LR-----------------FSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYADAVVGVPGEglnv 904
|
170 180 190
....*....|....*....|....*....|
gi 2524717128 159 -QLKRVALANTLITEPDLLI-LDEPTNHLD 186
Cdd:TIGR00956 905 eQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-222 |
3.27e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 10 VENLTKSFGDLVLFE-----NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSG--------------TISFRRDI 70
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 71 R--VGYLEQDPQYpeeltvleacfhhgnstveliKEYERCMETDGHPGLDGILArmDHEKAWeyeQKAKQILSQLKI-RD 147
Cdd:PRK13645 89 RkeIGLVFQFPEY---------------------QLFQETIEKDIAFGPVNLGE--NKQEAY---KKVPELLKLVQLpED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 FNQQVK-SLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNLT----LLMVTHDRYFLDRVCSEII 222
Cdd:PRK13645 143 YVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykkrIIMVTHNMDQVLRIADEVI 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-509 |
3.51e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.88 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 324 SFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFG---YYSQDGL-QFDEQMKVI-- 397
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNqniYERRVNLnRLRRQVSMVhp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 -------DVVQDIAEVIEL-GNGKRLTASQFLQHFLFTPE-------TQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLD 462
Cdd:PRK14258 96 kpnlfpmSVYDNVAYGVKIvGWRPKLEIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 463 EPTNDLDIVTLNVLEEYLRNFK----GCVIVVSHDRYFMDKVVDHLLVFNG 509
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
345-498 |
3.87e-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: 47.70 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 345 GIVGNNGTGKSTFikilmrheqadrgALDIGETVRFGYYSQDGLQFDEQMKV-IDVVQDIaevIELGNGkRLTASQFLQh 423
Cdd:cd03238 25 VVTGVSGSGKSTL-------------VNEGLYASGKARLISFLPKFSRNKLIfIDQLQFL---IDVGLG-YLTLGQKLS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 424 flftpetqhsyvyKLSGGERRRLYLCTVLMRNP--NFLVLDEPTNDLDIVTLNVLEEYLRNFKGC---VIVVSHDRYFMD 498
Cdd:cd03238 87 -------------TLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLgntVILIEHNLDVLS 153
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-209 |
3.87e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.87e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 153 KSLSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLE----DYLRRTNLTLLMVTH 209
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1417
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
331-493 |
4.09e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKIL---------------MR-HEQADRGALDIGetVRFGYYSQdgLQFDeqM 394
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvptsgevrvlgYVpFKRRKEFARRIG--VVFGQRSQ--LWWD--L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQDIAEVIELGNG---KRLT--ASQF-LQHFLFTPetqhsyVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDL 468
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAeykKRLDelVELLdLGELLDTP------VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180
....*....|....*....|....*....
gi 2524717128 469 DIVT----LNVLEEYLRNFKGCVIVVSHD 493
Cdd:COG4586 186 DVVSkeaiREFLKEYNRERGTTILLTSHD 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
298-492 |
4.84e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 298 NNDNVKL-DVKASYIGSKIFEadhlYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGE 376
Cdd:PTZ00265 371 NDDGKKLkDIKKIQFKNVRFH----YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 T------------VRFGYYSQDGLQFDEQMK--------------------------------------------VIDVV 400
Cdd:PTZ00265 447 ShnlkdinlkwwrSKIGVVSQDPLLFSNSIKnnikyslyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMS 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 Q--DIAEVIELGN-------------GKRLTASQFLQHFLFTPETQ-HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEP 464
Cdd:PTZ00265 527 NttDSNELIEMRKnyqtikdsevvdvSKKVLIHDFVSALPDKYETLvGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
|
250 260 270
....*....|....*....|....*....|..
gi 2524717128 465 TNDLDIVTLNVLEEYLRNFKG----CVIVVSH 492
Cdd:PTZ00265 607 TSSLDNKSEYLVQKTINNLKGnenrITIIIAH 638
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-512 |
4.93e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.42 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKIL-----------MRHEQAD---------------RGALdigetvrfgYY 383
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriARPAGARvlflpqrpylplgtlREAL---------LY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 384 SQDGLQFDEQmkvidvvqDIAEVIELGNgkrltasqfLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDE 463
Cdd:COG4178 449 PATAEAFSDA--------ELREALEAVG---------LGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524717128 464 PTNDLDIVTLNVLEEYLRN-FKGC-VIVVSH----DRYFmdkvvDHLLVFNGQGD 512
Cdd:COG4178 512 ATSALDEENEAALYQLLREeLPGTtVISVGHrstlAAFH-----DRVLELTGDGS 561
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
315-515 |
4.98e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKIL------------MRHEQADRGALDIGETVRFGY 382
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgvyphgtwdgeIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 383 ysqdGLQFDEQMKVIDVvqDIAEVIELGN-----GKR-------LTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCT 450
Cdd:TIGR02633 81 ----VIIHQELTLVPEL--SVAENIFLGNeitlpGGRmaynamyLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 451 VLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK----GCvIVVSHDRYFMDKVVDHLLVfngqgdIRD 515
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKahgvAC-VYISHKLNEVKAVCDTICV------IRD 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-180 |
5.10e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTIsfrrdirvgyleqDPQYPEELTVLEACFHHGNSTVELIKe 104
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-------------DIKGSAALIAISSGLNGQLTGIENIE- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 105 yercmetdghpgLDGILARMDHEKAWEYeqkAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDE 180
Cdd:PRK13545 108 ------------LKGLMMGLTKEKIKEI---IPEIIEFADIGKFiYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
151-222 |
5.77e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 5.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRVCSEII 222
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
313-501 |
5.78e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGaldigeTVRFgyYSQDGLQFD- 391
Cdd:PRK10419 10 SHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG------NVSW--RGEPLAKLNr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 392 EQMK-----VIDVVQD--------------IAE----VIELGNGKRLT-ASQFLQHFLFTPETQHSYVYKLSGGERRRLY 447
Cdd:PRK10419 82 AQRKafrrdIQMVFQDsisavnprktvreiIREplrhLLSLDKAERLArASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 448 LCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHD----RYFMDKVV 501
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVM 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
432-493 |
5.90e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 5.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 432 HSYVYKLSGGERRRLYLCTVLMR-----NPN--FLVLDEPTNDLDIVTLNVLEEYLRNF---KGCVIVVSHD 493
Cdd:PRK03695 121 GRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
321-506 |
5.90e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.81 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 321 LYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALdigetvrfgYYS-QDGLQFDEQ------ 393
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGEL---------YYQgQDLLKADPEaqkllr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 394 MKVIDVVQD----------IAEVIE--------LGNGKRLT-ASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMR 454
Cdd:PRK11308 92 QKIQIVFQNpygslnprkkVGQILEepllintsLSAAERREkALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 455 NPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV 506
Cdd:PRK11308 172 DPDVVVADEPVSALDVSvqaqVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
438-493 |
7.08e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 47.91 E-value: 7.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717128 438 LSGGERRRLYLCTVLMR-----NPN--FLVLDEPTNDLDIVTLNVLEEYLRNFK---GCVIVVSHD 493
Cdd:COG4138 127 LSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
345-510 |
7.34e-06 |
|
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: 48.56 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 345 GIVGNNGTGKSTFIKILMRHEQADRGALDIGETV---------------RFGYYSQDGLQFDEQ---------MKVIDVV 400
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQEARLFPHLsvrgnllygRKRAPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 401 Q---DIAEVIE-LGngkrltasqfLQHFLftpetqHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT---- 472
Cdd:COG4148 109 ErriSFDEVVElLG----------IGHLL------DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaei 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524717128 473 LNVLEEYLRNFKGCVIVVSHDryfMDKVV---DHLLVF-NGQ 510
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHS---LDEVArlaDHVVLLeQGR 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-516 |
1.01e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 47.32 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 319 DHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDI-GETVRFGYYSQD----------G 387
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIaGNHFDFSKTPSDkairelrrnvG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFDE----------------QMKVIDVVQDIA--EVIELGNGKRLT--ASQFLQHflftpetqhsyvykLSGGERRRLY 447
Cdd:PRK11124 86 MVFQQynlwphltvqqnlieaPCRVLGLSKDQAlaRAEKLLERLRLKpyADRFPLH--------------LSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 448 LCTVLMRNPNFLVLDEPTNDLD------IVtlNVLEEyLRNFKGCVIVVSHDRYFMDKVVDHLLVF-NG----QGDIRDF 516
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDpeitaqIV--SIIRE-LAETGITQVIVTHEVEVARKTASRVVYMeNGhiveQGDASCF 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-230 |
1.08e-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: 45.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 33 GQRVGLIAKNGSGKSTLLNILSGkegydsgtisfrrdirvgyleqdpqypeeltvleacfhhgnstvELIKEYERCMETD 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR--------------------------------------------ELGPPGGGVIYID 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 113 GhpgldgilarmdhekaweyEQKAKQILSQLKIRDFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD------ 186
Cdd:smart00382 38 G-------------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeal 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524717128 187 ---LDMTEWLEDYLRRTNLTLLMVTHDRYFLDRvcSEIIEIDNRRIY 230
Cdd:smart00382 99 lllLEELRLLLLLKSEKNLTVILTTNDEKDLGP--ALLRRRFDRRIV 143
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
330-469 |
1.10e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.50 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMrheQADRGALDIGETV--------------RFGYYSQDGLqFDEQMK 395
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA---FRSPKGVKGSGSVllngmpidakemraISAYVQQDDL-FIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 396 VIDVVQDIAEViELGN-----GKRLTASQFLQHFLFTP--ET---QHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:TIGR00955 116 VREHLMFQAHL-RMPRrvtkkEKRERVDEVLQALGLRKcaNTrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
....
gi 2524717128 466 NDLD 469
Cdd:TIGR00955 195 SGLD 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-186 |
1.24e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.31 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSG----KEG----------YDS-GTISFRRdiR 71
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrpQKGavlwqgkpldYSKrGLLALRQ--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 72 VGYLEQDPQypeeltvleacfhhgnstvelikeyERCMETDGHPGLDGILARMDHEKAwEYEQKAKQILSQLKIRDFNQQ 151
Cdd:PRK13638 79 VATVFQDPE-------------------------QQIFYTDIDSDIAFSLRNLGVPEA-EITRRVDEALTLVDAQHFRHQ 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 2524717128 152 -VKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD 186
Cdd:PRK13638 133 pIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-186 |
1.32e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 1.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2524717128 141 SQLKIR--DFNQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD 186
Cdd:NF040905 389 KKMNIKtpSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
433-506 |
1.63e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 1.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 433 SYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV 506
Cdd:PRK10418 136 LYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVAV 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
312-492 |
1.82e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 312 GSKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRF----GYYSQDG 387
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFDEQMKVIDVVQDIAEVIELGNGKRLTASQFLQHFL------FTPETQHSyvyKLSGGERRRLYLCTVLMRNPNFLVL 461
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLaalgcqLDLDSSAG---SLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190
....*....|....*....|....*....|....
gi 2524717128 462 DEPTNDLDIVTLNVLEEYLRNF--KGCVIV-VSH 492
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELlaQGVGIVfISH 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-191 |
1.91e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 22 LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGK----EG--YDSGTISF------------RRDIRVGYLEQDPQYPe 83
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElepsEGkiKHSGRISFspqtswimpgtiKDNIIFGLSYDEYRYT- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 84 elTVLEACfhhgnstvELIKEYERCMETDGHPGLDGILarmdhekaweyeqkakqilsqlkirdfnqqvkSLSGGQLKRV 163
Cdd:TIGR01271 520 --SVIKAC--------QLEEDIALFPEKDKTVLGEGGI--------------------------------TLSGGQRARI 557
|
170 180
....*....|....*....|....*...
gi 2524717128 164 ALANTLITEPDLLILDEPTNHLDLdMTE 191
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLDV-VTE 584
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-181 |
1.93e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 4 VNSILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRD-------------- 69
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 70 IRVGYLEQDPQYPEELTVLEACF----HHGNSTVELIKeyERCMETDGHPGLDGILARMDHEkaweyeqkakqilsqlki 145
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAyplrEHTQLPAPLLH--STVMMKLEAVGLRGAAKLMPSE------------------ 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 2524717128 146 rdfnqqvksLSGGQLKRVALANTLITEPDLLILDEP 181
Cdd:PRK11831 144 ---------LSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
331-503 |
2.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 46.75 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTfikiLMRHEQA----DRGALDI-GETVRFGYYSQD--------GL--QFDE-QM 394
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKST----LMQHFNAllkpSSGTITIaGYHITPETGNKNlkklrkkvSLvfQFPEaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQDIaeviELG--------NGKRLTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:PRK13641 99 FENTVLKDV----EFGpknfgfseDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524717128 467 DLDIVTLNVLEEYLRNFKGC---VIVVSHDryfMDKVVDH 503
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAghtVILVTHN---MDDVAEY 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
156-187 |
2.23e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 2.23e-05
10 20 30
....*....|....*....|....*....|..
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLDL 187
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-186 |
2.69e-05 |
|
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: 47.12 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 25 NISFGLSEGQRVGLIAKNGSGKSTLLNILSGKegYD--SGTI-------------SFRRDIrvGYLEQDpqypeelTVLe 89
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YDvtSGRIlidgqdirdvtqaSLRAAI--GIVPQD-------TVL- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 90 acFhhgNSTVELIKEYercmetdGHPGldgilARMDhekawEYEQKAKqiLSQlkIRDFnqqVKS--------------- 154
Cdd:COG5265 444 --F---NDTIAYNIAY-------GRPD-----ASEE-----EVEAAAR--AAQ--IHDF---IESlpdgydtrvgerglk 494
|
170 180 190
....*....|....*....|....*....|..
gi 2524717128 155 LSGGQLKRVALANTLITEPDLLILDEPTNHLD 186
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
331-526 |
2.73e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGEtVRFGYYSQDG------------LQFDEQMKVID 398
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD-ITITHKTKDKyirpvrkrigmvFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 399 VVQ------------DIAEVIElgngkrlTASQFLQHFLFTPETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTN 466
Cdd:PRK13646 102 TVEreiifgpknfkmNLDEVKN-------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 467 DLDIVTLNVLEEYLRNFK----GCVIVVSHDRYFMDKVVDHLLVFNgQGDI------RDFPGNYTRYRDW 526
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMK-EGSIvsqtspKELFKDKKKLADW 243
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-209 |
3.02e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 12 NLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGK--EGYDSGTISFRR---------DIR--VGY---- 74
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGYSNDLTLFGRrrgsgetiwDIKkhIGYvsss 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 75 LEQDpqYPEELTVLEAcfhhgnstveLIKEYercmetdghpgLDGI---LARMDHEKaweyeQKAKQILSQLKIRDF--N 149
Cdd:PRK10938 345 LHLD--YRVSTSVRNV----------ILSGF-----------FDSIgiyQAVSDRQQ-----KLAQQWLDILGIDKRtaD 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 150 QQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTH 209
Cdd:PRK10938 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-210 |
3.03e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 1 MAAvnsiLQVENLTKSF-GDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRrDIRVGYLEqdP 79
Cdd:PRK11650 1 MAG----LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIG-GRVVNELE--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 80 Q-------------YPeeltvleacfhHgnSTVELIKEYercmetdghpGLDgiLARMDHEKAWEYEQKAKQILsqlKIR 146
Cdd:PRK11650 74 AdrdiamvfqnyalYP-----------H--MSVRENMAY----------GLK--IRGMPKAEIEERVAEAARIL---ELE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 147 DF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLTLLMVTHD 210
Cdd:PRK11650 126 PLlDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
330-516 |
3.22e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.84 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGA----------LDIG----------ETVRFG--YYsqdG 387
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngrvsalLELGagfhpeltgrENIYLNgrLL---G 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 388 LQFDEQMKVIDvvqDIAEVIELGNgkrltasqflqhFLFTPetqhsyVYKLSGGERRRLYLCTVLMRNPNFLVLDEptnd 467
Cdd:COG1134 118 LSRKEIDEKFD---EIVEFAELGD------------FIDQP------VKTYSSGMRARLAFAVATAVDPDILLVDE---- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 468 ldivtlnVL-----------EEYLRNFK---GCVIVVSHDRYFMDKVVDHLLVFNgQGDIRDF 516
Cdd:COG1134 173 -------VLavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLE-KGRLVMD 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-504 |
3.37e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 3.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 434 YVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG--CVIVVSHDRYFMDKVVDHL 504
Cdd:PRK14267 146 YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
346-501 |
3.69e-05 |
|
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: 46.71 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 346 IVGNNGTGKSTFIKILMRHEQADRGA--LDiGETV---RFGYYSQ-------DGLQFDEQMKVIDVVQD----------- 402
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEilLD-GQPVtadNREAYRQlfsavfsDFHLFDRLLGLDGEADPararellerle 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 403 IAEVIELGNGKRLTAsqflqhflftpetqhsyvyKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDivtlnvlEEYLRN 482
Cdd:COG4615 442 LDHKVSVEDGRFSTT-------------------DLSQGQRKRLALLVALLEDRPILVFDEWAADQD-------PEFRRV 495
|
170 180 190
....*....|....*....|....*....|...
gi 2524717128 483 F----------KG-CVIVVSHD-RYF--MDKVV 501
Cdd:COG4615 496 FytellpelkaRGkTVIAISHDdRYFdlADRVL 528
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
313-493 |
3.90e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.99 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEADHLYKSFGD-LKILDDFSYIFARYEKMGIVGNNGTGKSTFI------------KILMRHEQAD---RGALDIGE 376
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFqnlngilkpssgRILFDGKPIDysrKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 377 TVrfGYYSQDGlqfDEQMKVIDVVQDIA-EVIELGNGK--------RLTASQFLQHFlftpetQHSYVYKLSGGERRRLY 447
Cdd:PRK13636 83 SV--GMVFQDP---DNQLFSASVYQDVSfGAVNLKLPEdevrkrvdNALKRTGIEHL------KDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524717128 448 LCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHD 493
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMgvseIMKLLVEMQKELGLTIIIATHD 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
314-508 |
4.47e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 314 KIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMR----------------------------HE 365
Cdd:PTZ00265 1167 EIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgDE 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 366 QADRGALDIGE--TVRFGYYSQDGLQFDEQMKV----IDVVQ----------------------DIAEVIELG------- 410
Cdd:PTZ00265 1247 EQNVGMKNVNEfsLTKEGGSGEDSTVFKNSGKIlldgVDICDynlkdlrnlfsivsqepmlfnmSIYENIKFGkedatre 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 411 NGKRLTASQFLQHFLFTPETQHS-----YVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG 485
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
250 260
....*....|....*....|....*..
gi 2524717128 486 ----CVIVVSHdRYFMDKVVDHLLVFN 508
Cdd:PTZ00265 1407 kadkTIITIAH-RIASIKRSDKIVVFN 1432
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-232 |
5.67e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVgyleqdpqypeelTVLEACFHHGNSTVELIK 103
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV-------------IAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 104 EYERCMETdghpgldgilarmdheKAWEYEQKAKQILSQLKIRDF-NQQVKSLSGGQLKRVALANTLITEPDLLILDEPT 182
Cdd:PRK13546 108 FKMLCMGF----------------KRKEIKAMTPKIIEFSELGEFiYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 183 NHLDLDMTEWLEDYL---RRTNLTLLMVTHDRYFLDRVCSEIIEIDNRRIYQY 232
Cdd:PRK13546 172 SVGDQTFAQKCLDKIyefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-71 |
5.85e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 7 ILQVENLTKSFGDLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDS--GTISFR------RDIR 71
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDgevcrfKDIR 73
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
313-510 |
7.30e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 313 SKIFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRH--------------------EQADRGAL 372
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaykilegdilfkgesildlEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 373 DI---------------GETVRFGYYSQDGLQFDEQMKVIDVVQDIAEVIELGNGKrltasqflQHFLftpetqHSYVYK 437
Cdd:CHL00131 85 GIflafqypieipgvsnADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMD--------PSFL------SRNVNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 438 -LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG---CVIVVSHDRYFMDKVV-DHLLVF-NGQ 510
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITHYQRLLDYIKpDYVHVMqNGK 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
432-492 |
7.98e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.77 E-value: 7.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 432 HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG--CVIVVSH 492
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
330-494 |
8.18e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.06 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 330 ILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADrGALDIG---------ETVR--FGYYSQDGLQF-------- 390
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDgvswnsvtlQTWRkaFGVIPQKVFIFsgtfrknl 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 391 -------DEQM-KVIDVVqDIAEVIElgngkrltasQFLQHFLFTPETQHsyvYKLSGGERRRLYLCTVLMRNPNFLVLD 462
Cdd:TIGR01271 1313 dpyeqwsDEEIwKVAEEV-GLKSVIE----------QFPDKLDFVLVDGG---YVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|...
gi 2524717128 463 EPTNDLDIVTLNVLEEYLRN-FKGCVIVVSHDR 494
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
315-493 |
9.99e-05 |
|
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: 44.35 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGD----LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRG--ALDiGEtvRFGYYSQDGL 388
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGtvRLA-GQ--DLFALDEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 389 ------------QfDEQ----MKVIDVV------------QDIAEVI--ELGNGKRLTAsqflqhflftpetqhsYVYKL 438
Cdd:COG4181 85 arlrarhvgfvfQ-SFQllptLTALENVmlplelagrrdaRARARALleRVGLGHRLDH----------------YPAQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 439 SGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHD 493
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHD 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
315-492 |
1.03e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKIL------------MRHEQADRGALDIGETVRFG- 381
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphgtyegeIIFEGEELQASNIRDTERAGi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 382 -YYSQDgLQFDEQMKVidvvqdiAEVIELGN----GKR-------LTASQFLQ--HFLFTPETQhsyVYKLSGGERRRLY 447
Cdd:PRK13549 85 aIIHQE-LALVKELSV-------LENIFLGNeitpGGImdydamyLRAQKLLAqlKLDINPATP---VGNLGLGQQQLVE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2524717128 448 LCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFK----GCvIVVSH 492
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKahgiAC-IYISH 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-492 |
1.32e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.13 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFG--YYSQDGLQFDEQM 394
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGqdIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 395 KVIDVVQD------IAEVIELG--------NGKRLTA--SQFLQHFLFTPETQH---SYVYKLSGGERRRLYLCTVLMRN 455
Cdd:PRK14247 85 QMVFQIPNpipnlsIFENVALGlklnrlvkSKKELQErvRWALEKAQLWDEVKDrldAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524717128 456 PNFLVLDEPTNDLDIVTLNVLEEYLRNFKG--CVIVVSH 492
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
317-513 |
1.34e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.97 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 317 EADHLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALDIGETVRFGYYS---QDGLQFDEQ 393
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 394 MKVIDVVQD---------IAEVIE-------------LGNGKRLTASQFLQHflftpeTQHSYVYKLSGGERRRLYLCTV 451
Cdd:PRK11264 85 QHVGFVFQNfnlfphrtvLENIIEgpvivkgepkeeaTARARELLAKVGLAG------KETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 452 LMRNPNFLVLDEPTNDLD-------IVTLNVLEEYLRNfkgcVIVVSHDRYFMDKVVDHlLVFNGQGDI 513
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDpelvgevLNTIRQLAQEKRT----MVIVTHEMSFARDVADR-AIFMDQGRI 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
331-493 |
1.38e-04 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 43.61 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRGALdigetvrfgyySQDGLQFDE----QMKV---------I 397
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-----------ILEGKQITEpgpdRMVVfqnysllpwL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 DVVQDIAEVIELGNGKRLTASQ---FLQHFLFT--PETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT 472
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERraiVEEHIALVglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180
....*....|....*....|....*
gi 2524717128 473 LNVLEEYLRNF---KGC-VIVVSHD 493
Cdd:TIGR01184 150 RGNLQEELMQIweeHRVtVLMVTHD 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
432-491 |
1.58e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 432 HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD-------IVTLNVLEEylrnfKGCVIVVS 491
Cdd:PLN03211 201 NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDataayrlVLTLGSLAQ-----KGKTIVTS 262
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
432-510 |
1.94e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 432 HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV- 506
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVl 232
|
....
gi 2524717128 507 FNGQ 510
Cdd:PRK15093 233 YCGQ 236
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-214 |
2.31e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.09 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 8 LQVENLTKSFG-DLVLFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVGYLEQDPQYPEELT 86
Cdd:cd03290 1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 87 VLEACFHHG--NSTVElikeyERCmeTDGHPGldgilarmdHEKAWEYEQKAKQILSQLKIRDFNQQVK------SLSGG 158
Cdd:cd03290 81 VAYAAQKPWllNATVE-----ENI--TFGSPF---------NKQRYKAVTDACSLQPDIDLLPFGDQTEigergiNLSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 159 QLKRVALANTLITEPDLLILDEPTNHLDLD-----MTEWLEDYLRRTNLTLLMVTHDRYFL 214
Cdd:cd03290 145 QRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
432-510 |
2.61e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 432 HSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLVF 507
Cdd:PRK15134 151 TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqiLQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
....
gi 2524717128 508 -NGQ 510
Cdd:PRK15134 231 qNGR 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
302-606 |
3.89e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 302 VKLDVKASYigsKIFeADHLYKSFGDLK-------ILD---------DFSYIFARYEKMGIVGNNGTGKSTFIKILMRHE 365
Cdd:PRK10070 3 IKLEIKNLY---KIF-GEHPQRAFKYIEqglskeqILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 366 QADRGALDIgETVRFGYYSQDGLQFDEQMKVIDVVQDIA---------------EVIELGNGKRLTASQFLQHFLFTPET 430
Cdd:PRK10070 79 EPTRGQVLI-DGVDIAKISDAELREVRRKKIAMVFQSFAlmphmtvldntafgmELAGINAEERREKALDALRQVGLENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 431 QHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKG----CVIVVSHDRYFMDKVVDHLLV 506
Cdd:PRK10070 158 AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 507 F-NGQ-------GDIRDFPGN-YTR--YRDWKDAKAAQEREKEKEAAKAQEEKTAKVRLNEKRRMSFKEKREFEQLEQ-- 573
Cdd:PRK10070 238 MqNGEvvqvgtpDEILNNPANdYVRtfFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIErg 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2524717128 574 -------DIAALEA---EKQSIEEALCSGALSVDELTEKSKRL 606
Cdd:PRK10070 318 nkfvgavSIDSLKTaltQQQGLDAALIDAPLAVDAQTPLSELL 360
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
414-482 |
3.96e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 3.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 414 RLTASQFLQHFLFTpETQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRN 482
Cdd:NF000106 122 RARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
315-510 |
4.23e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGD----LKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMrheqadrGALD-----IGETVRFGyySQ 385
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIM-------GLIDypgrvMAEKLEFN--GQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 386 DGLQFDEQMK-------VIDVVQD--------------IAEVIELGNG-----KRLTASQFL-QHFLFTPETQHS-YVYK 437
Cdd:PRK11022 74 DLQRISEKERrnlvgaeVAMIFQDpmtslnpcytvgfqIMEAIKVHQGgnkktRRQRAIDLLnQVGIPDPASRLDvYPHQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHDRYFMDKVVDHLLV-FNGQ 510
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiqaqIIELLLELQQKENMALVLITHDLALVAEAAHKIIVmYAGQ 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
437-465 |
4.40e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 4.40e-04
10 20
....*....|....*....|....*....
gi 2524717128 437 KLSGGERRRLYLCTVLMRNPNFLVLDEPT 465
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
315-493 |
5.62e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 315 IFEADHLYKSFGD-LKILDDFSYIFARYEKMGIVGNNGTGKST----FIKILmrheQADRGALDI-GETVRFGYYS---- 384
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTlflhFNGIL----KPTSGEVLIkGEPIKYDKKSllev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 385 --QDGLQF---DEQMKVIDVVQDIA----------EVIElgngKRLT-ASQFLQHFLFTPETQHsyvyKLSGGERRRLYL 448
Cdd:PRK13639 77 rkTVGIVFqnpDDQLFAPTVEEDVAfgplnlglskEEVE----KRVKeALKAVGMEGFENKPPH----HLSGGQKKRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524717128 449 CTVLMRNPNFLVLDEPTNDLD----IVTLNVLEEYlrNFKGCVIVVS-HD 493
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDL--NKEGITIIIStHD 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
148-210 |
7.63e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 7.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 148 FNQQVKSLSGGQLKRVALANTL----ITEPDLLILDEPTNHLDLDMTEWLEDYLRRTNL---TLLMVTHD 210
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkgaQVIVITHL 140
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
421-472 |
1.08e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 41.39 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 421 LQHFlftpetQHSYVYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT 472
Cdd:COG4525 124 LADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
436-503 |
1.54e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.88 E-value: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717128 436 YKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNF--KGCVIV-VSHdryFMDKVVDH 503
Cdd:PRK13649 144 FELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhqSGMTIVlVTH---LMDDVANY 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
156-229 |
1.59e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 156 SGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLR---RTNLTLLMVTHDRYFLDRVCSEIIEIDNRRI 229
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRsmvRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
438-493 |
1.74e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.16 E-value: 1.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDiVTLN------VLEEyLRNFKGCVIVVSHD 493
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLD-AALRaqfrefVFEQ-IRQRGIPALLVTHD 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
340-409 |
1.77e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 340 RYEKMGIVGNNGTGKSTFIKILMRHEQADRG---ALDIGETVRFGYYSQDGLQFDEQMKVIDVVQDIAEVIEL 409
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
30-61 |
2.03e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 41.14 E-value: 2.03e-03
10 20 30
....*....|....*....|....*....|..
gi 2524717128 30 LSEGQRVGLIAKNGSGKSTLLNILSGKEGYDS 61
Cdd:PRK06002 162 LCAGQRIGIFAGSGVGKSTLLAMLARADAFDT 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
438-492 |
2.04e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.01 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI-VTLNVLEE----YLRNFKGCVIVVSH 492
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEgilkFLQDDKRTLVLVTH 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
129-231 |
2.21e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.79 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 129 AWEYEQKAKQILSQLKIRDFNQQV-KSLSGGQLKRVALANTLITEPDLLILDEPTNHLD----LDMTEWLEDYLRRTNLT 203
Cdd:PRK10070 138 AEERREKALDALRQVGLENYAHSYpDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRT 217
|
90 100
....*....|....*....|....*...
gi 2524717128 204 LLMVTHDRYFLDRVCSEIIEIDNRRIYQ 231
Cdd:PRK10070 218 IVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
331-502 |
2.27e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.46 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 331 LDDFSYIFARYEKMGIVGNNGTGKSTFIK----ILMRHEQA----DRGALDIGET--VRfgyySQDGLQF---DEQMKVI 397
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnaLLIPSEGKvyvdGLDTSDEENLwdIR----NKAGMVFqnpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 398 DVVQDIAEVIE-LG------------NGKRLTASQFLQHflfTPetqhsyvYKLSGGERRRLYLCTVLMRNPNFLVLDEP 464
Cdd:PRK13633 102 IVEEDVAFGPEnLGippeeirervdeSLKKVGMYEYRRH---AP-------HLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524717128 465 TNDLDIV----TLNVLEEYLRNFKGCVIVVSHdryFMDKVVD 502
Cdd:PRK13633 172 TAMLDPSgrreVVNTIKELNKKYGITIILITH---YMEEAVE 210
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-186 |
2.32e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.85 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 24 ENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFrRDIRVGYLEQDPQYPEELTVLEACFHHGNSTVELIK 103
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 104 eyercmetdghpgldgiLARMDHEKAwEYEQKAK------QILsQLKiRDFNQQVKS----LSGGQLKRVALANTLITEP 173
Cdd:PRK10789 411 -----------------LGRPDATQQ-EIEHVARlasvhdDIL-RLP-QGYDTEVGErgvmLSGGQKQRISIARALLLNA 470
|
170
....*....|...
gi 2524717128 174 DLLILDEPTNHLD 186
Cdd:PRK10789 471 EILILDDALSAVD 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-187 |
2.75e-03 |
|
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: 40.23 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 22 LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGK----EGY--DSGTISF------------RRDIRVGYLEQDPQYpe 83
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGElepsEGKikHSGRISFssqfswimpgtiKENIIFGVSYDEYRY-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 84 eLTVLEACfhhgnstvELIKEYERCMETDGHPGLDGILarmdhekaweyeqkakqilsqlkirdfnqqvkSLSGGQLKRV 163
Cdd:cd03291 130 -KSVVKAC--------QLEEDITKFPEKDNTVLGEGGI--------------------------------TLSGGQRARI 168
|
170 180
....*....|....*....|....
gi 2524717128 164 ALANTLITEPDLLILDEPTNHLDL 187
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
435-493 |
2.78e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 39.97 E-value: 2.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717128 435 VYKLSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHD 493
Cdd:PRK10253 141 VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShqidLLELLSELNREKGYTLAAVLHD 203
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
438-510 |
3.13e-03 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 39.74 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHD----RYFMDKVvdhLLVFNG 509
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGLTVLMVTHDpedaARIADRV---LLVADG 206
|
.
gi 2524717128 510 Q 510
Cdd:COG3840 207 R 207
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
438-511 |
3.28e-03 |
|
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: 40.50 E-value: 3.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLRNFKGCVIVVSHdRYFMDKVVDHLLVFNGQG 511
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDGRG 655
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
438-516 |
3.57e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.86 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIV----TLNVLEEYLRNFKGCVIVVSHDryfMDKVV---DHLLVFNgQ 510
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPrkreLLPYLERLAREINIPILYVSHS---LDEILrlaDRVVVLE-Q 204
|
....*.
gi 2524717128 511 GDIRDF 516
Cdd:PRK11144 205 GKVKAF 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
438-508 |
3.85e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 3.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLD-IVTLNVlEEYLRNFKG--CVIVVSHDRYFMDKVVDHLLVFN 508
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLRI-EELMHELKEqyTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
320-513 |
4.02e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 39.70 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 320 HLYKSFGDLKILDDFSYIFARYEKMGIVGNNGTGKSTFIKILMRHEQADRG--------------------------AL- 372
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvthrsiqqrdicmvfqsyALf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 373 ---DIGETVRFGYYSQdGLQFDEqmkvidVVQDIAEVIEL----GNGKRltasqflqhflftpetqhsYVYKLSGGERRR 445
Cdd:PRK11432 91 phmSLGENVGYGLKML-GVPKEE------RKQRVKEALELvdlaGFEDR-------------------YVDQISGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524717128 446 LYLCTVLMRNPNFLVLDEPTNDLDIVTLNVLEEYLR----NFKGCVIVVSHDRYFMDKVVDHLLVFNgQGDI 513
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqqQFNITSLYVTHDQSEAFAVSDTVIVMN-KGKI 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
438-509 |
4.61e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 38.57 E-value: 4.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDIVT----LNVLEEYLRNFKGcVIVVSHDryfMDKVV---DHLLVFNG 509
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAkaeiYRLIRELADAGKA-VLLISSE---LDELLglcDRILVMYE 179
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
435-511 |
6.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 435 VYKLSGGERRRLYLCTVLM---RNPNFLVLDEPTNDL---DIVTLNVLEEYLRNFKGCVIVVSHDRYFMdKVVDHLLVFN 508
Cdd:PRK00635 807 LSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELG 885
|
...
gi 2524717128 509 GQG 511
Cdd:PRK00635 886 PEG 888
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
438-511 |
6.64e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 38.82 E-value: 6.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPT---NDLDIVTLNVLEEYLRN-FKGCVIVVSHDRYFMDKVVDHLLVFNgQG 511
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVN-QG 230
|
|
| DUF6033 |
pfam19498 |
Protein of unknown function (DUF6033); This family of proteins is functionally uncharacterized. ... |
529-604 |
6.73e-03 |
|
Protein of unknown function (DUF6033); This family of proteins is functionally uncharacterized. This family of proteins is primarily found in Clostridia. Proteins in this family are typically between 212 and 271 amino acids in length.
Pssm-ID: 437330 Cd Length: 204 Bit Score: 38.42 E-value: 6.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524717128 529 AKAAQEREKEKEAAKAQEEKTAKVRLNEKRRMSFKEKREFEQLEQDiaALEAEKQSIEEALCSGAL-SVDELTEKSK 604
Cdd:pfam19498 122 ERIEKKRAKKKEEKKAEEKKAEKKKREERLEKAKEEKEETVTVTAS--SIEELLKKIKDYYYNVKSdSVLTEEEKGV 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
151-187 |
7.11e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 7.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2524717128 151 QVKSLSGGQLKRVALANTLITEPDLLILDEPTNHLDL 187
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
22-215 |
7.39e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 22 LFENISFGLSEGQRVGLIAKNGSGKSTLLNILSGKEGYDSGTISFRRDIRVgYLEQDPQYPEELTVLE--ACFHHGNSTV 99
Cdd:pfam13304 104 SEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFL-LLLDEGLLLEDWAVLDlaADLALFPDLK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 100 ELIKEYERCMETDGHPGLDGILARMDHEKAWEYEQKAKQILSQLKiRDFNQQVKSLSGGQLKRVALANTLI---TEPDLL 176
Cdd:pfam13304 183 ELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENG-GGGELPAFELSDGTKRLLALLAALLsalPKGGLL 261
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524717128 177 ILDEPTNHLDLDMTEWL-E--DYLRRTNLTLLMVTHDRYFLD 215
Cdd:pfam13304 262 LIDEPESGLHPKLLRRLlEllKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
438-470 |
8.08e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 39.23 E-value: 8.08e-03
10 20 30
....*....|....*....|....*....|...
gi 2524717128 438 LSGGERRRLYLCTVLMRNPNFLVLDEPTNDLDI 470
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
134-210 |
9.38e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.73 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717128 134 QKAKQILSQLKIRDFNQQVKS----LSGGQLKRVALANTLITEPDLLILDEPTNHLDLDMTEWLEDYLRRTN----LTLL 205
Cdd:COG4170 134 KRAIELLHRVGIKDHKDIMNSypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqlqgTSIL 213
|
....*
gi 2524717128 206 MVTHD 210
Cdd:COG4170 214 LISHD 218
|
|
| |
