|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-533 |
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: 652.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 6 VNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIPVYPAGCTVE 85
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 86 DVLRSAFARLESLAEEMRALEARMAAGESDpaiLKRYGTLSERFEAFGGYDTDVAVNKIANGLSIPDSQRSQLFDSLSGG 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDED---LERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGNYSF 245
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 246 YAVEKERRYQERMKQYEKEQAKIAQLEKAAEQLRVWAfmgmdKTYRRAISMERRIERMRTTAKPTKARKMDARFSSAEFH 325
Cdd:COG0488 237 YLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKA-----RKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 326 GDEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIRFDH 405
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 PDWNLVENMMAAKKGLSAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWI 485
Cdd:COG0488 392 PDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2526491659 486 EEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDYPCGFAQYRQ 533
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-524 |
5.34e-106 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 331.51 E-value: 5.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGeLDYD-EGTVVVGQGRRVGLISQIPVYPAGCT 83
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDfNGEARPQPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRSAFARLESLAEEMRALEARMAAGESD-PAILKRYGTLSERFEAFGGYDTDVAVNKIANGLSIPDSQrsQLFDSL 162
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEISAKYAEPDADfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWD--ADVTKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 163 SGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGN 242
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 243 YSFYAVEKerryQERMKQYEKEQAKIA-QLEKAAEQLRvwafmgMDKTYRRAISMER--RIERMRTTAKPTKARKMDARF 319
Cdd:TIGR03719 243 YSSWLEQK----QKRLEQEEKEESARQkTLKRELEWVR------QSPKGRQAKSKARlaRYEELLSQEFQKRNETAEIYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 320 SSAEFHGDEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQ 399
Cdd:TIGR03719 313 PPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 iIRfDHPD-----WNLVEN----MMAAKKGLsaqSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLIL 470
Cdd:TIGR03719 393 -SR-DALDpnktvWEEISGgldiIKLGKREI---PSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 471 DEPTNHLDIDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRI--------WELADGTITDY 524
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHIlafegdshVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-524 |
1.36e-100 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 317.45 E-value: 1.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 7 NNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGeLDYD-EGTVVVGQGRRVGLISQIPVYPAGCTVE 85
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEfEGEARPAPGIKVGYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 86 DVLRSAFARLESLAEEMRALEARMAAGESDP-AILKRYGTLSERFEAFGGYDTDVAVNKIANGLSIPDSQrsQLFDSLSG 164
Cdd:PRK11819 89 ENVEEGVAEVKAALDRFNEIYAAYAEPDADFdALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWD--AKVTKLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 165 GEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGNYS 244
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 245 FYAVEKerryQERMKQYEKEQAKiaqLEKAAEQLRVWAFMGmDKTyRRAISMER--RIERMRTTAKPTKARKMDARFSSA 322
Cdd:PRK11819 247 SWLEQK----AKRLAQEEKQEAA---RQKALKRELEWVRQS-PKA-RQAKSKARlaRYEELLSEEYQKRNETNEIFIPPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 323 EFHGDEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQiIR 402
Cdd:PRK11819 318 PRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ-SR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 fDHPD-----WNLV----ENMMAAKKGLsaqSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEP 473
Cdd:PRK11819 397 -DALDpnktvWEEIsgglDIIKVGNREI---PSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 474 TNHLDIDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRI--------WELADGTITDY 524
Cdd:PRK11819 473 TNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHIlafegdsqVEWFEGNFQEY 531
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-629 |
4.83e-99 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 315.74 E-value: 4.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIPVYPAGCTVEDVLRSAFARLESLA 99
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 100 EEMRALEARMAAGESDpAILKRYGTLSERFEAFGGYDTDVAVNKIANGLSI-PDSQRSqlfdSLSGGEKTRVNLGRLILE 178
Cdd:PRK11147 99 KRYHDISHLVETDPSE-KNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLdPDAALS----SLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 179 DTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGNYSFYAVEKerryqERM 258
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEK-----EEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 259 KQYEKEQAkiAQLEKAAEQLRVWAFMGMdKTYR----------RAISMER--RIERMRTTakptkarKMdaRFSSAEFHG 326
Cdd:PRK11147 249 LRVEELQN--AEFDRKLAQEEVWIRQGI-KARRtrnegrvralKALRRERseRREVMGTA-------KM--QVEEASRSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIRFDHP 406
Cdd:PRK11147 317 KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 407 DWNLVENMMAAKKGLSAQSARNRLAAY--DFrgedVF------KPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD 478
Cdd:PRK11147 397 EKTVMDNLAEGKQEVMVNGRPRHVLGYlqDF----LFhpkramTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 479 IDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELA-DGTITDYPCGFAQYRQMKAQEEAEKAAAPKPEKEREKPAA 557
Cdd:PRK11147 473 VETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKA 552
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 558 ERPQR-GNKAQQAARRQLTICERDIARAEERIAALEADMEAA---ACDYEKLNELVGQKDAAQAELDALYERWEQL 629
Cdd:PRK11147 553 ETVKRsSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADAdffSQPHEQTQKVLADLADAEQELEVAFERWEEL 628
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
30-531 |
3.89e-94 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 299.88 E-value: 3.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 30 GERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIPVYPAGCTVEDVLRSAFARLESLAEEMRALEARM 109
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTELWEVKQERDRIYALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 110 AAGESDPAilkRYGTLSERFEAFGGYDTDVAVNKIANGLSIPDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPT 189
Cdd:PRK15064 107 EMSEEDGM---KVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 190 NHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGNYSFYaVEKERRYQER-MKQYEKEQAKI 268
Cdd:PRK15064 184 NNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY-MTAATQARERlLADNAKKKAQI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 269 AQLekaaeQLRVWAFMGMDKTYRRAISMERRIERMRTT-AKPTKARKMDARFSSAEFHGDEVLGIRNVSKSYGDKHLFEG 347
Cdd:PRK15064 263 AEL-----QSFVSRFSANASKAKQATSRAKQIDKIKLEeVKPSSRQNPFIRFEQDKKLHRNALEVENLTKGFDNGPLFKN 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQiirfDHP-----DWNLVENMMAAKK-GL 421
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ----DHAydfenDLTLFDWMSQWRQeGD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 422 SAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSH 501
Cdd:PRK15064 414 DEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSH 493
|
490 500 510
....*....|....*....|....*....|
gi 2526491659 502 DRYFINRFATRIWELADGTITDYPCGFAQY 531
Cdd:PRK15064 494 DREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-634 |
3.33e-85 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 279.36 E-value: 3.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQipVYPAgctvedVLRSAFARLESL 98
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQ--ETPA------LPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 99 AEEMRALEARMA-AGESDP--AIlkryGTLSERFEAFGGYDTDVAVNKIANGLSIPDSQRSQLFDSLSGGEKTRVNLGRL 175
Cdd:PRK10636 88 DREYRQLEAQLHdANERNDghAI----ATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 176 ILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGNYSFYAVEKERRYQ 255
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 256 ERMKQYEKEQAKIAQLEKAAEQLRVWAfmgmdKTYRRAISMERRIERMRTTAKPTKARKMDARFSSAEFHGDEVLGIRNV 335
Cdd:PRK10636 244 QQQAMYESQQERVAHLQSYIDRFRAKA-----TKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 336 SKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQ-IIRFDHPDWNLVENM 414
Cdd:PRK10636 319 SAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhQLEFLRADESPLQHL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 415 MAAKKGLSAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDG 494
Cdd:PRK10636 399 ARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 495 TLLFVSHDRYFINRFATRIWELADGTITDYPCGFAQYRQMKAQEEAEKAaapkpekerEKPAAERPQRGNKAQ------- 567
Cdd:PRK10636 479 ALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQEN---------QTDEAPKENNANSAQarkdqkr 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 568 ---------QAARRQLTICERDIARAEERIAALEADMEAAACdYE-----KLNELVGQKDAAQAELDALYERWEQLSEEA 633
Cdd:PRK10636 550 reaelrtqtQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSEL-YDqsrkaELTACLQQQASAKSGLEECEMAWLEAQEQL 628
|
.
gi 2526491659 634 E 634
Cdd:PRK10636 629 E 629
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
332-599 |
2.74e-64 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 220.71 E-value: 2.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIRFDhPDWNLV 411
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLD-DDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 412 ENMMAAKKGLSAQSAR----------------------NRLAAYD----------------FRGEDVFKPVSVLSGGEQS 453
Cdd:COG0488 80 DTVLDGDAELRALEAEleeleaklaepdedlerlaelqEEFEALGgweaearaeeilsglgFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 454 RLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDYPCGFAQYRQ 533
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 534 MkaqeeaekaaapkpekeREKpAAERPQRGNKAQQAARRQLticERDIAR----------AEERIAALEAdMEAAA 599
Cdd:COG0488 240 Q-----------------RAE-RLEQEAAAYAKQQKKIAKE---EEFIRRfrakarkakqAQSRIKALEK-LEREE 293
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
332-520 |
2.37e-63 |
|
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: 205.76 E-value: 2.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQiirfdhpdwnlv 411
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 412 enmmaakkglsaqsarnrlaaydfrgedvfkpvsvLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEA 491
Cdd:cd03221 71 -----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
170 180
....*....|....*....|....*....
gi 2526491659 492 YDGTLLFVSHDRYFINRFATRIWELADGT 520
Cdd:cd03221 116 YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-534 |
4.09e-61 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 216.26 E-value: 4.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTgeLDYDEGtvvVGQGRRVGLISQIPVYPAGCTVEDVLRSAFARL 95
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG---IPKNCQILHVEQEVVGDDTTALQCVLNTDIERT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 96 ESLAEEMRALEARMA---------------AGESDPAILKRYGTLSERFEAFGGYDTDVAVNKIANGLSI-PDSQRSQLf 159
Cdd:PLN03073 264 QLLEEEAQLVAQQRElefetetgkgkgankDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFtPEMQVKAT- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 160 DSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFY 239
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTY 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 240 SGNYSFYAVEKERRYQERMKQYEKEQAKIAQLEKAAEQLRVWAfmgmdktyRRAISMERRIERMRTTAkptkarKMDARF 319
Cdd:PLN03073 423 KGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNA--------KRASLVQSRIKALDRLG------HVDAVV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 320 SSAEFH----------GDEVLGIRNVSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT 388
Cdd:PLN03073 489 NDPDYKfefptpddrpGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 389 GPQVKEAYLPQiirfDHPD-WNLVEN----MMAAKKGLSAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDD 463
Cdd:PLN03073 569 SAKVRMAVFSQ----HHVDgLDLSSNpllyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 464 EINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDYPCGFAQYRQM 534
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKT 715
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-235 |
1.29e-51 |
|
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: 174.56 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQipvypagct 83
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlrsafarleslaeemralearmaagesdpailkrygtlserfeafggydtdvavnkianglsipdsqrsqlfdsLS 163
Cdd:cd03221 71 ------------------------------------------------------------------------------LS 72
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd03221 73 GGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-235 |
3.24e-37 |
|
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: 138.84 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG---------RRVGLIS 73
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDvrkeprearRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIPVYPAGCTVEDVLRSaFARLeslaeemralearmaAGESDPAILKRYGTLSERFEAFGGYDtdvavnkianglsipds 153
Cdd:COG4555 81 DERGLYDRLTVRENIRY-FAEL---------------YGLFDEELKKRIEELIELLGLEEFLD----------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 154 qrsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVTRVIE 230
Cdd:COG4555 128 ---RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVI 204
|
....*
gi 2526491659 231 IQDGK 235
Cdd:COG4555 205 LHKGK 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-521 |
5.34e-37 |
|
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: 144.66 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYD---EGTVVVG-----------QGRR 68
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgrdllelsealRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 69 VGLISQIPVY---PAgcTVEDVLRSAFARLESLAEEMRALEARMAAGESDPAILKRYGtlserfeafggydtdvavnkia 145
Cdd:COG1123 85 IGMVFQDPMTqlnPV--TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP---------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 146 nglsipdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVTISHDRYFL 221
Cdd:COG1123 141 --------------HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQaeilDLLRELQRERGTTVLLITHDLGVV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 222 DRTVTRVIEIQDGKAEfysgnysfyavekerryqermkqyekEQAKIAQLEKAAEQLRvwafmgmdktyrraismerrie 301
Cdd:COG1123 207 AEIADRVVVMDDGRIV--------------------------EDGPPEEILAAPQALA---------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 302 rmrttAKPTKARKMDARFSSAEfHGDEVLGIRNVSKSY-----GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIV 376
Cdd:COG1123 239 -----AVPRLGAARGRAAPAAA-AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 377 GELYPDDGRI---------KTGPQVKEAY-LPQIIrFDHPDWNLVENM---------MAAKKGLSAQSARNRLAA----- 432
Cdd:COG1123 313 GLLRPTSGSIlfdgkdltkLSRRSLRELRrRVQMV-FQDPYSSLNPRMtvgdiiaepLRLHGLLSRAERRERVAEllerv 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 433 ---YDFRGedvfKPVSVLSGGEQSRLRLC--MLMDDEInfLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDR 503
Cdd:COG1123 392 glpPDLAD----RYPHELSGGQRQRVAIAraLALEPKL--LILDEPTSALDVSVQaqilNLLRDLQRELGLTYLFISHDL 465
|
570
....*....|....*...
gi 2526491659 504 YFINRFATRIWELADGTI 521
Cdd:COG1123 466 AVVRYIADRVAVMYDGRI 483
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-235 |
5.37e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.19 E-value: 5.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqG-----------RRVGLI 72
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-GedvardpaevrRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIPVYPAGCTVEDVLRsAFARLeslaeemralearmaAGESDPAILKRYGTLSERFeafggydtdvavnkianGLsipD 152
Cdd:COG1131 79 PQEPALYPDLTVRENLR-FFARL---------------YGLPRKEARERIDELLELF-----------------GL---T 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 153 SQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTI---SHDRYFLDRTVTRVI 229
Cdd:COG1131 123 DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVllsTHYLEEAERLCDRVA 202
|
....*.
gi 2526491659 230 EIQDGK 235
Cdd:COG1131 203 IIDKGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
332-521 |
2.19e-35 |
|
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: 131.37 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQVKE--AYLPQII 401
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikKEPEEVKRriGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 RFDhpdwnlvenmmaakkglsaqsarnrlaaYDFRGEDVFKpvsvLSGGEQSRLRL-CMLMDD-EInfLILDEPTNHLDI 479
Cdd:cd03230 83 SLY----------------------------ENLTVRENLK----LSGGMKQRLALaQALLHDpEL--LILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526491659 480 DSREWIEEAVEAY---DGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03230 129 ESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-235 |
2.75e-34 |
|
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: 128.28 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG---------RRVGLIS 73
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDikkepeevkRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIPVYPAGCTVEDVLRsafarleslaeemralearmaagesdpailkrygtlserfeafggydtdvavnkianglsipds 153
Cdd:cd03230 80 EEPSLYENLTVRENLK---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 154 qrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISHDRYFLDRTVTRVIE 230
Cdd:cd03230 96 --------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAI 167
|
....*
gi 2526491659 231 IQDGK 235
Cdd:cd03230 168 LNNGR 172
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-235 |
1.13e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 129.01 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ----------GRRVGLI 72
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRdlaslsrrelARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIPVYPAGCTVEDVL-------RSAFARLEslAEEMRALEARMAAgesdpailkrygtlserfeafggydTDVAvnkia 145
Cdd:COG1120 81 PQEPPAPFGLTVRELValgryphLGLFGRPS--AEDREAVEEALER-------------------------TGLE----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 146 nGLsipdsqRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL-HATEWLE---EYIRSFHGTVVTISHD---- 217
Cdd:COG1120 129 -HL------ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLEllrRLARERGRTVVMVLHDlnla 201
|
250
....*....|....*....
gi 2526491659 218 -RYFldrtvTRVIEIQDGK 235
Cdd:COG1120 202 aRYA-----DRLVLLKDGR 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-253 |
1.54e-33 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 135.25 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFevGKNVL-DGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIpvypagc 82
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 83 tvedvlRSAFARLESLAEEMralearmaAGESDPAILKRYGTLSE----RFeAFGGydtdvavnkianglsiPDSQrsQL 158
Cdd:PRK11819 396 ------RDALDPNKTVWEEI--------SGGLDIIKVGNREIPSRayvgRF-NFKG----------------GDQQ--KK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 159 FDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQ-DGKAE 237
Cdd:PRK11819 443 VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVE 522
|
250
....*....|....*.
gi 2526491659 238 FYSGNYSFYAVEKERR 253
Cdd:PRK11819 523 WFEGNFQEYEEDKKRR 538
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
332-520 |
3.01e-33 |
|
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: 124.66 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIktgpqvkeaylpqiiRFDHPDWNLV 411
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------------LIDGKDIAKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 412 ENmmaakkglsaQSARNRLAAydfrgedvfkpVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEA 491
Cdd:cd00267 67 PL----------EELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|..
gi 2526491659 492 Y---DGTLLFVSHDRYFINRFATRIWELADGT 520
Cdd:cd00267 126 LaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-235 |
5.81e-33 |
|
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: 126.29 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqG------------RRVGL 71
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GkditkknlrelrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 I-----SQIpVYPagcTV-EDVlrsAFArLESL---AEEM--RALEArmaagesdpaiLKRYGtlserFEAFGGYDTdva 140
Cdd:COG1122 80 VfqnpdDQL-FAP---TVeEDV---AFG-PENLglpREEIreRVEEA-----------LELVG-----LEHLADRPP--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsipdsqrsqlfDSLSGGEKTRVNL-GRLILEdTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISH 216
Cdd:COG1122 133 -------------------HELSGGQKQRVAIaGVLAME-PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTH 192
|
250
....*....|....*....
gi 2526491659 217 DRYFLDRTVTRVIEIQDGK 235
Cdd:COG1122 193 DLDLVAELADRVIVLDDGR 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-246 |
8.63e-33 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 132.71 E-value: 8.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGlisqipvYPAGCT 83
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIG-------YYAQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDvlrsaFARLESLAEEMRALearMAAGESDPAILKRYGTLserfeAFGGYDtdvaVNKIANglsipdsqrsqlfdSLS 163
Cdd:PRK15064 392 AYD-----FENDLTLFDWMSQW---RQEGDDEQAVRGTLGRL-----LFSQDD----IKKSVK--------------VLS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGNY 243
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTY 520
|
...
gi 2526491659 244 SFY 246
Cdd:PRK15064 521 EEY 523
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
332-521 |
6.31e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.64 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQVKE--AYLPQII 401
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvaRDPAEVRRriGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 RFdHPDWNLVEN--MMAAKKGLSAQSARNRLAAY-------DFRGedvfKPVSVLSGGEQSRLRLCM-LMDD-EInfLIL 470
Cdd:COG1131 83 AL-YPDLTVRENlrFFARLYGLPRKEARERIDELlelfgltDAAD----RKVGTLSGGMKQRLGLALaLLHDpEL--LIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 471 DEPTNHLDIDSREWIEEAVEAY---DGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-235 |
1.00e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQG------------RRVGL 71
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL-DGkplsampppewrRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIPVYPAGcTVEDVLRSAFARLESLAEEMRALEArmaagesdpailkrygtlserFEAFGgydtdvavnkianglsIP 151
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRERKFDRERALEL---------------------LERLG----------------LP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 152 DSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF----HGTVVTISHDRYFLDRTVTR 227
Cdd:COG4619 121 PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADR 200
|
....*...
gi 2526491659 228 VIEIQDGK 235
Cdd:COG4619 201 VLTLEAGR 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-235 |
3.08e-31 |
|
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: 121.03 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFEVG-KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ----------GRRVGLI 72
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQipvYPA----GCTVEDVLrsAFArLESLaeemralearmaaGESDPAILKRygtLSERFEAFGgydtdvavnkiangl 148
Cdd:cd03225 81 FQ---NPDdqffGPTVEEEV--AFG-LENL-------------GLPEEEIEER---VEEALELVG--------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 siPDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTV 225
Cdd:cd03225 124 --LEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELA 201
|
250
....*....|
gi 2526491659 226 TRVIEIQDGK 235
Cdd:cd03225 202 DRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
8.27e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV------VVGQGRRVGLISQ 74
Cdd:COG1121 4 MPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 I----PVYPAgcTVEDVL-------RSAFARLeSLAEEMRALEArmaagesdpaiLKRYGtLSERfeafggydtdvavnk 143
Cdd:COG1121 83 RaevdWDFPI--TVRDVVlmgrygrRGLFRRP-SRADREAVDEA-----------LERVG-LEDL--------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 144 ianglsipdsqRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYF 220
Cdd:COG1121 133 -----------ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGA 201
|
250
....*....|....
gi 2526491659 221 LDRTVTRVIEIQDG 234
Cdd:COG1121 202 VREYFDRVLLLNRG 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
332-521 |
1.61e-30 |
|
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: 119.36 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQIIR-----FD 404
Cdd:COG1122 3 LENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRkvglvFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 HPDWNLV------------ENMmaakkGLSAQSARNR----LAA---YDFRGedvfKPVSVLSGGEQSRLRL-CML-MDD 463
Cdd:COG1122 83 NPDDQLFaptveedvafgpENL-----GLPREEIRERveeaLELvglEHLAD----RPPHELSGGQKQRVAIaGVLaMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 464 EInfLILDEPTNHLDIDSREWIEEAVEAYDG---TLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:COG1122 154 EV--LVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
332-520 |
4.66e-30 |
|
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: 117.57 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQIIR-----F 403
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRkvglvF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DHPDWNLV------------ENMmaakkGLSAQSARNRLAA-------YDFRGEDVFKpvsvLSGGEQSRLRL-CML-MD 462
Cdd:cd03225 82 QNPDDQFFgptveeevafglENL-----GLPEEEIEERVEEalelvglEGLRDRSPFT----LSGGQKQRVAIaGVLaMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 463 DEInfLILDEPTNHLDIDSREWIEEAVEAY--DG-TLLFVSHDRYFINRFATRIWELADGT 520
Cdd:cd03225 153 PDI--LLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
332-522 |
4.74e-30 |
|
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: 116.38 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGPQVKE-----AYLPQI 400
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlASLSPKElarkiAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRfdhpdwnlvenmmaakkglsaqsarnRLAAYDFRGedvfKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDID 480
Cdd:cd03214 82 LE--------------------------LLGLAHLAD----RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526491659 481 SR----EWIEEAVEAYDGTLLFVSHDryfIN---RFATRIWELADGTIT 522
Cdd:cd03214 132 HQiellELLRRLARERGKTVVMVLHD---LNlaaRYADRVILLKDGRIV 177
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-235 |
2.53e-29 |
|
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: 114.45 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLvkSFEVGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgrrvglisqipvypaGCT 83
Cdd:cd03214 1 EVENL--SVGYGGRtVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD----------------GKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRSAFARLESLAeemralearmaagesdPAILKRYGT--LSERFeafggydtdvavnkianglsipdsqrsqlFDS 161
Cdd:cd03214 63 LASLSPKELARKIAYV----------------PQALELLGLahLADRP-----------------------------FNE 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVTISHD-----RYFldrtvTRVIEIQ 232
Cdd:cd03214 98 LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQiellELLRRLARERGKTVVMVLHDlnlaaRYA-----DRVILLK 172
|
...
gi 2526491659 233 DGK 235
Cdd:cd03214 173 DGR 175
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
329-521 |
4.10e-29 |
|
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: 116.30 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPqvKE-----A 395
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSR--RElarriA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 396 YLPQIIrfdHPDWNL-VENMMAA-----KKGLSAQSARNRLAAY---------DFRGedvfKPVSVLSGGEQSRLRLCML 460
Cdd:COG1120 79 YVPQEP---PAPFGLtVRELVALgryphLGLFGRPSAEDREAVEealertgleHLAD----RPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 461 M--DDEInfLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDryfIN---RFATRIWELADGTI 521
Cdd:COG1120 152 LaqEPPL--LLLDEPTSHLDLAHQlevlELLRRLARERGRTVVMVLHD---LNlaaRYADRLVLLKDGRI 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
332-531 |
8.27e-29 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 121.60 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQ------------ 399
Cdd:PRK11147 6 IHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvyd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 ---------------------IIRFDHPDWNLveNMMAAkkgLSAQSARNRLAAYDFRGEDVFK--------PVSVLSGG 450
Cdd:PRK11147 86 fvaegieeqaeylkryhdishLVETDPSEKNL--NELAK---LQEQLDHHNLWQLENRINEVLAqlgldpdaALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 451 EQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDYPCGFAQ 530
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
.
gi 2526491659 531 Y 531
Cdd:PRK11147 241 Y 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-235 |
9.19e-29 |
|
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: 121.02 E-value: 9.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 2 IEIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRVG 70
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYPAGcTVEDVLRsaFARLESLAEEM-RALEarmAAGesdpailkrygtLSERFEAF-GGYDTDVAvnkiANGL 148
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLR--LGRPDASDEELeAALE---AAG------------LDEFVAALpDGLDTPLG----EGGR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 sipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS-FHG-TVVTISHDRYFLDRtVT 226
Cdd:COG4988 473 ------------GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQ-AD 539
|
....*....
gi 2526491659 227 RVIEIQDGK 235
Cdd:COG4988 540 RILVLDDGR 548
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
329-518 |
1.27e-28 |
|
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: 113.34 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQVKE--AYLP 398
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirDAREDYRRrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QIIRFdHPDWNLVEN--MMAAKKGL--SAQSARNRLAAYDFRG-EDvfKPVSVLSGGEQSRLRLCMLMDDEINFLILDEP 473
Cdd:COG4133 82 HADGL-KPELTVRENlrFWAALYGLraDREAIDEALEAVGLAGlAD--LPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526491659 474 TNHLDIDSREWIEEAVEAY---DGTLLFVSHDRYFINrfATRIWELAD 518
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-523 |
3.73e-28 |
|
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: 118.75 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDY--DEGTVVVGQGR-----RVGLISQIP 76
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHVALcekcgYVERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 VYPAGCtvEDVLRSAFARLESLAEEMRAlearmaagesdpAILKRYGTLSER-FEAFG---------------GYDTDVA 140
Cdd:TIGR03269 80 EPCPVC--GGTLEPEEVDFWNLSDKLRR------------RIRKRIAIMLQRtFALYGddtvldnvlealeeiGYEGKEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 VNKIANGLSIPD-SQR-SQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD------LHatEWLEEYIRSFHGTVV 212
Cdd:TIGR03269 146 VGRAVDLIEMVQlSHRiTHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtaklVH--NALEEAVKASGISMV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 213 TISHDRYFLDRTVTRVIEIQDGkaefysgnysfyAVEKERRYQERMKQYekeqakiaqlekaaeqlrvwafmgmdktyrr 292
Cdd:TIGR03269 224 LTSHWPEVIEDLSDKAIWLENG------------EIKEEGTPDEVVAVF------------------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 293 aismerrierMRTTAKPTKARKMDArfssaefhGDEVLGIRNVSKSY-----GDKHLFEGISLKVEGGERIALIGDNGTG 367
Cdd:TIGR03269 261 ----------MEGVSEVEKECEVEV--------GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 368 KSTLIKMIVGELYPDDGRI------------KTGPQVKeAYLPQIIRFDHPDWNL------VENMMAA-----KKGLSAQ 424
Cdd:TIGR03269 323 KTTLSKIIAGVLEPTSGEVnvrvgdewvdmtKPGPDGR-GRAKRYIGILHQEYDLyphrtvLDNLTEAiglelPDELARM 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 425 SARNRLAAYDF---RGEDVF-KPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD----IDSREWIEEAVEAYDGTL 496
Cdd:TIGR03269 402 KAVITLKMVGFdeeKAEEILdKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTF 481
|
570 580
....*....|....*....|....*..
gi 2526491659 497 LFVSHDRYFINRFATRIWELADGTITD 523
Cdd:TIGR03269 482 IIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-235 |
4.31e-28 |
|
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: 119.10 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSF-EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG-----------QGRRVGL 71
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeddLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQ-IPVYPAgcTVEDVLRsaFARLESLAEEMR-ALEArmaAGesdpailkrygtLSERFEAF-GGYDTDVAvnkiANGL 148
Cdd:COG4987 414 VPQrPHLFDT--TLRENLR--LARPDATDEELWaALER---VG------------LGDWLAALpDGLDTWLG----EGGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 SipdsqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDlHATE--WLEEYIRSFHG-TVVTISHDRYFLDRtV 225
Cdd:COG4987 471 R------------LSGGERRRLALARALLRDAPILLLDEPTEGLD-AATEqaLLADLLEALAGrTVLLITHRLAGLER-M 536
|
250
....*....|
gi 2526491659 226 TRVIEIQDGK 235
Cdd:COG4987 537 DRILVLEDGR 546
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-513 |
6.52e-28 |
|
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: 111.47 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 334 NVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKE------AYLPQIIRFdhpD 407
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEkerkriGYVPQRRSI---D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 408 WNL---VENMMA----AKKGLS----------AQSARNRLAAYDFRGedvfKPVSVLSGGEQSRLRL--CMLMDDEInfL 468
Cdd:cd03235 81 RDFpisVRDVVLmglyGHKGLFrrlskadkakVDEALERVGLSELAD----RQIGELSGGQQQRVLLarALVQDPDL--L 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526491659 469 ILDEPTNHLDIDSREWIEEAVE---AYDGTLLFVSHDRYFINRFATRI 513
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRelrREGMTILVVTHDLGLVLEYFDRV 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-235 |
6.68e-28 |
|
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: 111.42 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG----------RRVGLIS 73
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIPVYPAGCTVEDVLRSAFARLESLAEEMRALEArmaagesdpailkrygtlserFEAFGgydtdvavnkianglsiPDS 153
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEA---------------------LEAVG-----------------LAG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 154 QRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH---GTVVTISHDRYFLDRtvTRVIE 230
Cdd:COG4133 124 LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA--ARVLD 201
|
....*
gi 2526491659 231 IQDGK 235
Cdd:COG4133 202 LGDFK 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
16-513 |
1.48e-27 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 117.60 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKN--VLDGLTfQVDQGERVGLLGRNGAGKTTLFKILTGEL-----DYDEGTvvvgqgrrvglisqipvypagcTVEDVL 88
Cdd:PRK13409 84 GVNgfKLYGLP-IPKEGKVTGILGPNGIGKTTAVKILSGELipnlgDYEEEP----------------------SWDEVL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 89 RsAFARleslaEEMRALEARMAAGESDPAILKRY---------GTLSERFEafgGYDTDVAVNKIANGLSIpDSQRSQLF 159
Cdd:PRK13409 141 K-RFRG-----TELQNYFKKLYNGEIKVVHKPQYvdlipkvfkGKVRELLK---KVDERGKLDEVVERLGL-ENILDRDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 160 DSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSfhGTVVTISHDRYFLDrTVTRVIEIQDGK 235
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRELAEG--KYVLVVEHDLAVLD-YLADNVHIAYGE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 236 aefySGNYSFYAVEKERR--YQERMKQYEKEqakiaqlekaaEQLRVwafmgmdktYRRAISMERRIERmrttakptkar 313
Cdd:PRK13409 288 ----PGAYGVVSKPKGVRvgINEYLKGYLPE-----------ENMRI---------RPEPIEFEERPPR----------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 314 kmdarfssAEFHGDEVLGIRNVSKSYGDkhlFegiSLKVEGG-----ERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT 388
Cdd:PRK13409 333 --------DESERETLVEYPDLTKKLGD---F---SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 389 gpQVKEAYLPQIIRFDhPDWNLVENMMAAKKGLSAQSARNRLAAyDFRGEDVF-KPVSVLSGGEQSRLRL--CMLMDDEI 465
Cdd:PRK13409 399 --ELKISYKPQYIKPD-YDGTVEDLLRSITDDLGSSYYKSEIIK-PLQLERLLdKNVKDLSGGELQRVAIaaCLSRDADL 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 466 nfLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRI 513
Cdd:PRK13409 475 --YLLDEPSAHLDVEQRlavaKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
332-521 |
1.50e-27 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 111.49 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQVKE--AYLPQII 401
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREARRqiGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 RFdHPDWNLVEN--MMAAKKGLSAQSARNRLAAYDFR---GEDVFKPVSVLSGGEQSRLRL-CMLMDDEINfLILDEPTN 475
Cdd:COG4555 84 GL-YDRLTVRENirYFAELYGLFDEELKKRIEELIELlglEEFLDRRVGELSTGMKKKVALaRALVHDPKV-LLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526491659 476 HLDIDSREWIEEAVEAY---DGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:COG4555 162 GLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-235 |
2.96e-27 |
|
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: 109.89 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ-------------- 65
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTdisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 66 GRRVGLISQ----IPVYPAgctVEDVLRSA-FARLESLAEEMRALEArmaagesdpaiLKRYGtLSERFEAFggydtdva 140
Cdd:cd03255 81 RRHIGFVFQsfnlLPDLTA---LENVELPLlLAGVPKKERRERAEEL-----------LERVG-LGDRLNHY-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsiPdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISH 216
Cdd:cd03255 138 ----------P--------SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTH 199
|
250
....*....|....*....
gi 2526491659 217 DRyFLDRTVTRVIEIQDGK 235
Cdd:cd03255 200 DP-ELAEYADRIIELRDGK 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-190 |
5.11e-27 |
|
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: 106.96 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ----------GRRVGLISQIPVYPAGCTVEDVL 88
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQdltdderkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 89 RSAfARLESLAEemRALEARMAagesdpAILKRYGtlserfeafggyDTDVAVNKIANGLSipdsqrsqlfdSLSGGEKT 168
Cdd:pfam00005 81 RLG-LLLKGLSK--REKDARAE------EALEKLG------------LGDLADRPVGERPG-----------TLSGGQRQ 128
|
170 180
....*....|....*....|..
gi 2526491659 169 RVNLGRLILEDTDILLLDEPTN 190
Cdd:pfam00005 129 RVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-235 |
8.11e-27 |
|
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: 106.56 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGLISqipvypagctv 84
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 edvlrsafarleslaeemralearmaagesDPAILKRYGTLSErfeafggydtdvavnkianglsipdsqrsqlfdsLSG 164
Cdd:cd00267 68 ------------------------------LEELRRRIGYVPQ----------------------------------LSG 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 165 GEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd00267 84 GQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-225 |
1.30e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 108.00 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV-VVGQ-----GRRVGLISQIPV- 77
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKplekeRKRIGYVPQRRSi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 78 ---YPAgcTVEDVLRSA------FARLESLAEEMRALEArmaagesdpaiLKRygtlserfeafggydtdVAVNKIANgl 148
Cdd:cd03235 80 drdFPI--SVRDVVLMGlyghkgLFRRLSKADKAKVDEA-----------LER-----------------VGLSELAD-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 sipdsqrsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHD----RYFL 221
Cdd:cd03235 128 --------RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDlglvLEYF 199
|
....
gi 2526491659 222 DRTV 225
Cdd:cd03235 200 DRVL 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-513 |
1.57e-26 |
|
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: 114.50 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 29 QGERVGLLGRNGAGKTTLFKILTGEL-----DYDEGTvvvgqgrrvglisqipvypagcTVEDVLRsAFARLEsLAEEMR 103
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgDYDEEP----------------------SWDEVLK-RFRGTE-LQDYFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 104 ALearmAAGESDPAILKRY---------GTLSERFEafgGYDTDVAVNKIANGLSIpDSQRSQLFDSLSGGEKTRVNLGR 174
Cdd:COG1245 154 KL----ANGEIKVAHKPQYvdlipkvfkGTVRELLE---KVDERGKLDELAEKLGL-ENILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 175 LILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISHDRYFLDrTVTRVIEIQDGKaefySGNYSFyaVEKE 251
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaeeGKYVLVVEHDLAILD-YLADYVHILYGE----PGVYGV--VSKP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 252 RRYQERMKQYekeqakiaqLEkaaeqlrvwafmGmdktYRRAISMerrieRMRTtakptKARKMDARFSSAEFHGDEVLG 331
Cdd:COG1245 299 KSVRVGINQY---------LD------------G----YLPEENV-----RIRD-----EPIEFEVHAPRREKEEETLVE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDkhlFegiSLKVEGG-----ERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTgpQVKEAYLPQIIRFDHP 406
Cdd:COG1245 344 YPDLTKSYGG---F---SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQYISPDYD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 407 DwnLVENMM--AAKKGLSAQSARNRLAAyDFRGEDVF-KPVSVLSGGEQSRL--RLCMLMDDEInfLILDEPTNHLDIDS 481
Cdd:COG1245 416 G--TVEEFLrsANTDDFGSSYYKTEIIK-PLGLEKLLdKNVKDLSGGELQRVaiAACLSRDADL--YLLDEPSAHLDVEQ 490
|
490 500 510
....*....|....*....|....*....|....*.
gi 2526491659 482 R----EWIEEAVEAYDGTLLFVSHDRYFINRFATRI 513
Cdd:COG1245 491 RlavaKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-235 |
1.47e-25 |
|
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: 105.94 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGR------------RVGLISQ--IPVYPAG 81
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGErrggedvwelrkRIGLVSPalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 CTVEDVLRSAF----ARLESLAEEMRALeARmaagesdpAILKRYGtLSERfeafggydtdvavnkianglsipdsqRSQ 157
Cdd:COG1119 95 ETVLDVVLSGFfdsiGLYREPTDEQRER-AR--------ELLELLG-LAHL--------------------------ADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 158 LFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDRYFLDRTVTRVIEIQD 233
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTHHVEEIPPGITHVLLLKD 218
|
..
gi 2526491659 234 GK 235
Cdd:COG1119 219 GR 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-226 |
1.50e-25 |
|
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: 110.84 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 2 IEIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG-----------QGRRVG 70
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvpladadadsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYPAGCTVEDVlrsAFARLESLAEEMRALEARMAAGESDPAILkrygtlserfeafGGYDTDVAvnkianglsi 150
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENI---RLARPDASDAEIREALERAGLDEFVAALP-------------QGLDTPIG---------- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 151 PDSQRsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHDR---YFLDRTV 225
Cdd:TIGR02857 454 EGGAG------LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLalaALADRIV 527
|
.
gi 2526491659 226 T 226
Cdd:TIGR02857 528 V 528
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-235 |
2.09e-25 |
|
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: 104.22 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG---------RRVGLISQ 74
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 IP-VYPAGCTVEDVLRSAFARLESLAEEMRALEarmaagesdpailkrYGTLSERfeafggydtdvavnkianglsipds 153
Cdd:cd03268 80 APgFYPNLTARENLRLLARLLGIRKKRIDEVLD---------------VVGLKDS------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 154 qRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTI---SHDRYFLDRTVTRVIE 230
Cdd:cd03268 120 -AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVlisSHLLSEIQKVADRIGI 198
|
....*
gi 2526491659 231 IQDGK 235
Cdd:cd03268 199 INKGK 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-235 |
8.43e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 102.34 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG--------QGRRVGLISQIP 76
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakeRRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 VYPA-GCTVEDVLRsafarleslaEEMRALEARMAAGEsdpAILKRYgtlserfeafggydtdvavnkianGLSIPDSQR 155
Cdd:cd03226 81 DYQLfTDSVREELL----------LGLKELDAGNEQAE---TVLKDL------------------------DLYALKERH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 156 SQlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVTRVIEIQ 232
Cdd:cd03226 124 PL---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLA 200
|
...
gi 2526491659 233 DGK 235
Cdd:cd03226 201 NGA 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-237 |
1.09e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 103.34 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG---------- 66
Cdd:COG1124 1 MLEVR--NLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPvtrrrrkafr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 RRVGLISQIPvypagctvedvlrsafarleslaeeMRALEARMAAGEsdpailkrygTLSERFEAFGGYDTDVAVNKIAN 146
Cdd:COG1124 79 RRVQMVFQDP-------------------------YASLHPRHTVDR----------ILAEPLRIHGLPDREERIAELLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 147 GLSIPDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVTISHDRYFLD 222
Cdd:COG1124 124 QVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQaeilNLLKDLREERGLTYLFVSHDLAVVA 203
|
250
....*....|....*
gi 2526491659 223 RTVTRVIEIQDGKAE 237
Cdd:COG1124 204 HLCDRVAVMQNGRIV 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
332-519 |
1.11e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 100.92 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKH--LFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRiktgpqvkeaylpqiIRFDHPDWn 409
Cdd:cd03228 3 FKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE---------------ILIDGVDL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 410 lvenmmaakKGLSAQSARNRLA-----AYDFRGedvfkpvSV----LSGGEQSRLRLC--MLMDDEInfLILDEPTNHLD 478
Cdd:cd03228 67 ---------RDLDLESLRKNIAyvpqdPFLFSG-------TIreniLSGGQRQRIAIAraLLRDPPI--LILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526491659 479 IDSREWIEEAVEAYDG--TLLFVSHdRYFINRFATRIWELADG 519
Cdd:cd03228 129 PETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-276 |
1.32e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 108.88 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKS----FEV--------GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGL 71
Cdd:PRK11147 307 MQVEEASRSgkivFEMenvnyqidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQipvYPAGC----TVEDvlrsafarleSLAEEMRALearMAAGESDPAIlkrygtlserfeafgGYDTDVavnkiang 147
Cdd:PRK11147 387 FDQ---HRAELdpekTVMD----------NLAEGKQEV---MVNGRPRHVL---------------GYLQDF-------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 148 LSIPDSQRSQLfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTR 227
Cdd:PRK11147 428 LFHPKRAMTPV-KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTE 506
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2526491659 228 V-IEIQDGKAEFYSGNYsFYAVEKERRYQErMKQYEKEQAKIAQLEKAAE 276
Cdd:PRK11147 507 CwIFEGNGKIGRYVGGY-HDARQQQAQYLA-LKQPAVKKKEEAAAPKAET 554
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-235 |
2.44e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.67 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqG-------------- 66
Cdd:COG2884 1 MIRFE--NVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-Gqdlsrlkrreipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 -RRVGLISQ----IP---VYpagctvEDVlrsAFArLESLAEEMRALEARMaagesdPAILKRYGtLSERFEAFggydtd 138
Cdd:COG2884 78 rRRIGVVFQdfrlLPdrtVY------ENV---ALP-LRVTGKSRKEIRRRV------REVLDLVG-LSDKAKAL------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 139 vavnkianglsiPdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH--G-TVVTIS 215
Cdd:COG2884 135 ------------P--------HELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIAT 194
|
250 260
....*....|....*....|
gi 2526491659 216 HDRYFLDRTVTRVIEIQDGK 235
Cdd:COG2884 195 HDLELVDRMPKRVLELEDGR 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-235 |
2.69e-24 |
|
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: 101.51 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSF-EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRVG 70
Cdd:cd03245 2 RIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYPAGcTVEDVLrsAFARLEslAEEMRALEARMAAGesdpailkrygtlserfeafggydTDVAVNKIANGLSI 150
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNI--TLGAPL--ADDERILRAAELAG------------------------VTDFVNKHPNGLDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 151 PDSQRSQlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HGTVVTISHdRYFLDRTVTRV 228
Cdd:cd03245 133 QIGERGR---GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH-RPSLLDLVDRI 208
|
....*..
gi 2526491659 229 IEIQDGK 235
Cdd:cd03245 209 IVMDSGR 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-235 |
3.03e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.27 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ-------------- 65
Cdd:COG1136 5 LELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQdisslserelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 66 GRRVGLISQ----IPVYpagcTVED--VLRSAFARLESLAEEMRALEArmaagesdpaiLKRYGtLSERFEAFggydtdv 139
Cdd:COG1136 85 RRHIGFVFQffnlLPEL----TALEnvALPLLLAGVSRKERRERAREL-----------LERVG-LGDRLDHR------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 140 avnkianglsiPDSqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVTIS 215
Cdd:COG1136 142 -----------PSQ--------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNRELGTTIVMVT 202
|
250 260
....*....|....*....|
gi 2526491659 216 HDRYFLDRTvTRVIEIQDGK 235
Cdd:COG1136 203 HDPELAARA-DRVIRLRDGR 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-317 |
3.14e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 107.56 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQipvypagctvedvlrsafARLE 96
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ------------------HQLE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 97 SLAEEMRALE--ARMAAGESDPAiLKRYgtlserfeaFGGYdtdvavnkianglSIPDSQRSQLFDSLSGGEKTRVNLGR 174
Cdd:PRK10636 387 FLRADESPLQhlARLAPQELEQK-LRDY---------LGGF-------------GFQGDKVTEETRRFSGGEKARLVLAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 175 LILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSG---NYSFYAVEKE 251
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGdleDYQQWLSDVQ 523
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 252 RRYQERMKQYEKEQAKIAQLEKaaEQLRVWA-FMGMDKTYRRAI-SMERRIERMRTTAKPTKARKMDA 317
Cdd:PRK10636 524 KQENQTDEAPKENNANSAQARK--DQKRREAeLRTQTQPLRKEIaRLEKEMEKLNAQLAQAEEKLGDS 589
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
345-475 |
7.42e-24 |
|
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: 98.10 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 345 FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-----------TGPQVKEAYLPQIIRFDhPDWNLVEN 413
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQDPQLF-PRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 414 MM--AAKKGLS-------AQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTN 475
Cdd:pfam00005 80 LRlgLLLKGLSkrekdarAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-238 |
1.34e-22 |
|
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: 96.80 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGLISQIPVYPAGCT 83
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRSAfarleslaeemrALEARMAAGESDPAILKRYGTLSERFEafggydTDVAVNKIAN-GLSipdSQRSQLFDSL 162
Cdd:cd03261 79 MGMLFQSG------------ALFDSLTVFENVAFPLREHTRLSEEEI------REIVLEKLEAvGLR---GAEDLYPAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 163 SGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDRYFLDRTVTRVIEIQDGKAEF 238
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelglTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
330-519 |
1.68e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 95.81 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-------KTGPQVKEAYLPQiIR 402
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPE-ER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 FDHPDWNLVENMM--AAKKGLSAQSARNRLAAYDFR---GEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHL 477
Cdd:cd03269 80 GLYPKMKVIDQLVylAQLKGLKKEEARRRIDEWLERlelSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526491659 478 DIDSREWIEEAVEAYDG---TLLFVSHDRYFINRFATRIWELADG 519
Cdd:cd03269 160 DPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
334-531 |
1.86e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 101.51 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 334 NVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIiRFDHPDWNLVEN 413
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQD-QFAFEEFTVLDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 414 -MMAAKKGLSAQSARNRL---------------------AAYD----------------FRGEDVFKPVSVLSGGEQSRL 455
Cdd:PRK15064 85 vIMGHTELWEVKQERDRIyalpemseedgmkvadlevkfAEMDgytaearagelllgvgIPEEQHYGLMSEVAPGWKLRV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 456 RLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDYPCGFAQY 531
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
1.97e-22 |
|
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: 95.66 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG---------QGRRVGLISQ 74
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvppERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 -IPVYPAgCTVEDVLRSAFARLESLAEEMRALEARMAAGESDPAILKRYgtlserfeafggydtdvavnkianglsiPds 153
Cdd:cd03259 80 dYALFPH-LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRY----------------------------P-- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 154 qrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDR 218
Cdd:cd03259 129 ------HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
332-523 |
2.45e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.89 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHL-FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ----VKEAYLPQIIR---- 402
Cdd:COG2884 4 FENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrLKRREIPYLRRrigv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -F-DH---PDWNLVENMMAAKK--GLSAQSARNRLaaydfrgEDV----------FKPVSVLSGGEQSRL---RlCMLMD 462
Cdd:COG2884 84 vFqDFrllPDRTVYENVALPLRvtGKSRKEIRRRV-------REVldlvglsdkaKALPHELSGGEQQRVaiaR-ALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 463 DEInfLILDEPTNHLDIDSREWI----EEAVEAydG-TLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:COG2884 156 PEL--LLADEPTGNLDPETSWEImellEEINRR--GtTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
332-521 |
3.83e-22 |
|
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: 95.65 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG----PQVKEAYLPQIIR----- 402
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgediSGLSEAELYRLRRrmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ------FDhpDWNLVENMM-------AAKKGLSAQSARNRLAAYDFRGEDVFKPvSVLSGGEQSRLRLC--MLMDDEInf 467
Cdd:cd03261 83 fqsgalFD--SLTVFENVAfplrehtRLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALAraLALDPEL-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 468 LILDEPTNHLD-IDSREwIEEAV----EAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03261 158 LLYDEPTAGLDpIASGV-IDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-235 |
4.37e-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: 93.60 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSF-EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgrrvGL-ISQIPVypag 81
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-----GVdLRDLDL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 ctveDVLRSAFArleslaeemralearmaagesdpailkrygtlserfeafggydtdvAVnkianglsipdSQRSQLFDS 161
Cdd:cd03228 72 ----ESLRKNIA----------------------------------------------YV-----------PQDPFLFSG 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 162 ------LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHdRYFLDRTVTRVIEIQD 233
Cdd:cd03228 91 tireniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDD 169
|
..
gi 2526491659 234 GK 235
Cdd:cd03228 170 GR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
293-523 |
6.10e-22 |
|
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: 99.83 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 293 AISMERRIERMRTTAKPTKARKMdarfSSAEFHGDEVLGIRNVSKSYGD-KHLFEGISLKVEGGERIALIGDNGTGKSTL 371
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGT----APLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 372 IKMIVGELYPDDGRIK-TGPQVKE----------AYLPQ-----------IIRFDHPDWNLVEnMMAAkkglsAQSAR-- 427
Cdd:COG4988 380 LNLLLGFLPPYSGSILiNGVDLSDldpaswrrqiAWVPQnpylfagtireNLRLGRPDASDEE-LEAA-----LEAAGld 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 428 ---NRLAA-YDFR-GEDVFKpvsvLSGGEQSRL---RLcMLMDDEInfLILDEPTNHLDIDSREWIEEAVEAY--DGTLL 497
Cdd:COG4988 454 efvAALPDgLDTPlGEGGRG----LSGGQAQRLalaRA-LLRDAPL--LLLDEPTAHLDAETEAEILQALRRLakGRTVI 526
|
250 260
....*....|....*....|....*.
gi 2526491659 498 FVSHDRYFInRFATRIWELADGTITD 523
Cdd:COG4988 527 LITHRLALL-AQADRILVLDDGRIVE 551
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-502 |
1.35e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFevGKNV-LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV------------- 69
Cdd:COG3845 6 LELRGITKRF--GGVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DGKPVrirsprdaialgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQ----IPVYpagcTV-EDVL----RSAFARLEslaeeMRALEARMAAgesdpailkrygtLSERFeafggydtdva 140
Cdd:COG3845 83 GMVHQhfmlVPNL----TVaENIVlglePTKGGRLD-----RKAARARIRE-------------LSERY----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianGLSI-PDsqrsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISH 216
Cdd:COG3845 130 ------GLDVdPD----AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaeGKSIIFITH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 217 DryfLD--RTVT-RVIEIQDGKaefysgnysfyavekerryqermkqyekeqaKIAQLEKA---AEQLrVWAFMGmdkty 290
Cdd:COG3845 200 K---LRevMAIAdRVTVLRRGK-------------------------------VVGTVDTAetsEEEL-AELMVG----- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 291 rRAISMERRiermRTTAKPtkarkmdarfssaefhGDEVLGIRNVS-KSYGDKHLFEGISLKVEGGERIALIGDNGTGKS 369
Cdd:COG3845 240 -REVLLRVE----KAPAEP----------------GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQS 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 370 TLIKMIVGELYPDDGRIK------TGPQVKE------AYLPQIiRFDH---PDWNLVENMMA--------AKKGL----- 421
Cdd:COG3845 299 ELAEALAGLRPPASGSIRldgediTGLSPRErrrlgvAYIPED-RLGRglvPDMSVAENLILgryrrppfSRGGFldrka 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 422 SAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEA-VEAYDG--TLLF 498
Cdd:COG3845 378 IRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRlLELRDAgaAVLL 457
|
....
gi 2526491659 499 VSHD 502
Cdd:COG3845 458 ISED 461
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
330-524 |
1.36e-21 |
|
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: 93.75 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVkeAYLPQIIRFDHPDWN 409
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV--SSLLGLGGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 410 LVEN--MMAAKKGLSAQSARNRLAA-YDFR--GEDVFKPVSVLSGGEQSRLR--LCMLMDDEInfLILDEPT----NHLD 478
Cdd:cd03220 101 GRENiyLNGRLLGLSRKEIDEKIDEiIEFSelGDFIDLPVKTYSSGMKARLAfaIATALEPDI--LLIDEVLavgdAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 479 IDSREWIEEAVEAyDGTLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:cd03220 179 EKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-235 |
1.38e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 99.52 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLvkSF---EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqG------------R 67
Cdd:COG2274 473 DIELENV--SFrypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-GidlrqidpaslrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 68 RVGLISQipvypagctvEDVLRS-------AFARLE-SLAEEMRAleARMAAgesdpailkrygtLSERFEAF-GGYDTD 138
Cdd:COG2274 550 QIGVVLQ----------DVFLFSgtireniTLGDPDaTDEEIIEA--ARLAG-------------LHDFIEALpMGYDTV 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 139 VAvnkiANGlsipdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISH 216
Cdd:COG2274 605 VG----EGG------------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH 668
|
250
....*....|....*....
gi 2526491659 217 DRYFLDRtVTRVIEIQDGK 235
Cdd:COG2274 669 RLSTIRL-ADRIIVLDKGR 686
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-217 |
1.43e-21 |
|
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: 94.04 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV-GL---------IS 73
Cdd:cd03219 1 LEVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF-DGEDItGLppheiarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 ---QIP-VYPAGCTVEDVLRSAFARLESLAEEMRALEARMAAGESDPAILKRYGtLSERfeafggydtdvavnkiangls 149
Cdd:cd03219 79 rtfQIPrLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVG-LADL--------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 150 ipdsqRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPT---NHLDLHAT-EWLEEyIRSFHGTVVTISHD 217
Cdd:cd03219 137 -----ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELaELIRE-LRERGITVLLVEHD 202
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
332-521 |
1.73e-21 |
|
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: 93.89 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG----PQVKEAYLPQIIR----- 402
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqdiTGLSEKELYELRRrigml 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ------FDhpDWNLVENMMAA---KKGLSAQSARNR----LAAYDFRG-EDVFkPvSVLSGGEQSRLRL--CMLMDDEIn 466
Cdd:COG1127 88 fqggalFD--SLTVFENVAFPlreHTDLSEAEIRELvlekLELVGLPGaADKM-P-SELSGGMRKRVALarALALDPEI- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 467 fLILDEPTNHLD------IDsrEWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:COG1127 163 -LLYDEPTAGLDpitsavID--ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
332-521 |
1.87e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 92.98 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQI--IR------F 403
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRqkvgmvF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DH----PDWNLVENMMAAK---KGLSAQSARNrlaaydfRGEDVFKPV----------SVLSGGEQSRLRLC--MLMDDE 464
Cdd:cd03262 83 QQfnlfPHLTVLENITLAPikvKGMSKAEAEE-------RALELLEKVgladkadaypAQLSGGQQQRVAIAraLAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 465 InfLILDEPTNHLDidsREWIEEAVE-----AYDG-TLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03262 156 V--MLFDEPTSALD---PELVGEVLDvmkdlAEEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
332-520 |
3.16e-21 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 91.48 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRiktgpqvkeaylpqiIRFDHPDWNLV 411
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS---------------ILIDGEDLTDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 412 ENMMAAKK---GLSAQSAR--NRLAAYDFRGEdvfkpvsVLSGGEQSRLRL--CMLMDDEInfLILDEPTNHLDIDSREW 484
Cdd:cd03229 68 EDELPPLRrriGMVFQDFAlfPHLTVLENIAL-------GLSGGQQQRVALarALAMDPDV--LLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2526491659 485 IEEAVE---AYDG-TLLFVSHDRYFINRFATRIWELADGT 520
Cdd:cd03229 139 VRALLKslqAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
332-521 |
3.32e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 92.28 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQ-----IIrfDH 405
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALrrigaLI--EA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 PDW--NL--VENMMAAKKGLSAQSAR-NRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDID 480
Cdd:cd03268 81 PGFypNLtaRENLRLLARLLGIRKKRiDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526491659 481 SREWIEE---AVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03268 161 GIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-217 |
3.54e-21 |
|
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: 92.53 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVG---KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV------VVGQGRRVGLISQ 74
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 ipvypagctvEDVL---RSAfarLE--SLAEEMRALEARMAAGESDPAiLKRYGtLSERFEAFggydtdvavnkiangls 149
Cdd:cd03293 81 ----------QDALlpwLTV---LDnvALGLELQGVPKAEARERAEEL-LELVG-LSGFENAY----------------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 150 iPdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHD 217
Cdd:cd03293 129 -P--------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-217 |
4.59e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRVGLI 72
Cdd:PRK13548 3 LEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIPVYPAGCTVEDVLR-SAFARLESLAEEMRALEARMAAgesdpailkrygtlserfeafggydTDVAvnkianGLsip 151
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAmGRAPHGLSRAEDDALVAAALAQ-------------------------VDLA------HL--- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 152 dsqRSQLFDSLSGGEKTRVNLGRLIL------EDTDILLLDEPTNHLDL---HAT-EWLEEYIRSFHGTVVTISHD 217
Cdd:PRK13548 128 ---AGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqHHVlRLARQLAHERGLAVIVVLHD 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-234 |
4.74e-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: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEV----GK--NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGRRVGLisqip 76
Cdd:COG4778 5 LEVENLSKTFTLhlqgGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 vypAGCTVEDVLR---------SAFAR-------LESLAEEMRALearmaaGESDPAILKRYGTLSERFEafggydtdva 140
Cdd:COG4778 80 ---AQASPREILAlrrrtigyvSQFLRviprvsaLDVVAEPLLER------GVDREEARARARELLARLN---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsIPDSqrsqLFDS----LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HGT-VVT 213
Cdd:COG4778 141 ---------LPER----LWDLppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTaIIG 207
|
250 260
....*....|....*....|.
gi 2526491659 214 ISHDRYFLDRTVTRVIEIQDG 234
Cdd:COG4778 208 IFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-239 |
5.63e-21 |
|
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: 92.25 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV--------------GQGRRV 69
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinklkgkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQ----IPVYPAgctVEDVLRSAFAR---------LESLAEEMRALEArmaagesdpaiLKRYGtLSERFeafggyd 136
Cdd:cd03256 81 GMIFQqfnlIERLSV---LENVLSGRLGRrstwrslfgLFPKEEKQRALAA-----------LERVG-LLDKA------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 137 tdvavnkianglsipdSQRSqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVT 213
Cdd:cd03256 139 ----------------YQRA---DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVI 199
|
250 260 270
....*....|....*....|....*....|..
gi 2526491659 214 IS-HD-----RYFldrtvTRVIEIQDGKAEFY 239
Cdd:cd03256 200 VSlHQvdlarEYA-----DRIVGLKDGRIVFD 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
332-522 |
6.55e-21 |
|
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: 91.16 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKH-LFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEA-------YLPQiir 402
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLnGKPIKAKerrksigYVMQ--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 fdHPDWNLVENMMAAKKGLSA-------QSARNRLAAYDFRGEDVFKPVSvLSGGEQSRLRLC--MLMDDEInfLILDEP 473
Cdd:cd03226 79 --DVDYQLFTDSVREELLLGLkeldagnEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAaaLLSGKDL--LIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 474 TNHLDIDSREWIEEAVE---AYDGTLLFVSHDRYFINRFATRIWELADGTIT 522
Cdd:cd03226 154 TSGLDYKNMERVGELIRelaAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
16-217 |
7.29e-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: 92.57 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVvgqgrrvglisqipvyPAGCTVEDVLRSAFARL 95
Cdd:TIGR03873 13 GRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD----------------LAGVDLHGLSRRARARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 96 ESLAEEMRALEARMAAgeSDPAILKRYGTLSerfeAFGG-YDTDVAVNKIANGLSIPDSQRSQLFDSLSGGEKTRVNLGR 174
Cdd:TIGR03873 77 VALVEQDSDTAVPLTV--RDVVALGRIPHRS----LWAGdSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 175 LILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHD 217
Cdd:TIGR03873 151 ALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-217 |
9.00e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQ----IPVYPAgcTVEDVLR-S 90
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevPDSLPL--TVRDLVAmG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 91 AFARLESLAEEMRalEARMAAGESdpaiLKRYGtlserFEAFGGydtdvavnkianglsipdsqRSqlFDSLSGGEKTRV 170
Cdd:NF040873 82 RWARRGLWRRLTR--DDRAAVDDA----LERVG-----LADLAG--------------------RQ--LGELSGGQRQRA 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526491659 171 NLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHD 217
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
332-522 |
9.73e-21 |
|
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: 89.41 E-value: 9.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVkeaylpqiIRFDHPdwnlv 411
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASP----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 412 enMMAAKKGLSAqsarnrlaaydfrgedvfkpVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVE- 490
Cdd:cd03216 70 --RDARRAGIAM--------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRr 127
|
170 180 190
....*....|....*....|....*....|....
gi 2526491659 491 -AYDG-TLLFVSHDRYFINRFATRIWELADGTIT 522
Cdd:cd03216 128 lRAQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
332-524 |
9.75e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSY----------------------GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG 389
Cdd:COG1134 7 VENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 390 PQVkeAYLpqiirFD-----HPDWNLVEN--MMAAKKGLSAQSARNRLAA-YDFRG-EDVFK-PVSVLSGGEQSRLR--L 457
Cdd:COG1134 87 GRV--SAL-----LElgagfHPELTGRENiyLNGRLLGLSRKEIDEKFDEiVEFAElGDFIDqPVKTYSSGMRARLAfaV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 458 CMLMDDEInfLILDEPTNHLDID----SREWIEEAVEAyDGTLLFVSHDRYFINRFATR-IWeLADGTITDY 524
Cdd:COG1134 160 ATAVDPDI--LLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRaIW-LEKGRLVMD 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-502 |
1.54e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-----KTGPQVKE--AYLP------ 398
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgePLDPEDRRriGYLPeergly 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 -------QIIRFdhpdwnlvenmmAAKKGLSAQSARNRLAAY-------DFRGedvfKPVSVLSGGEQSRLRL--CMLMD 462
Cdd:COG4152 84 pkmkvgeQLVYL------------ARLKGLSKAEAKRRADEWlerlglgDRAN----KKVEELSKGNQQKVQLiaALLHD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526491659 463 DEInfLILDEPTNHLDIDSREWIEEAV--EAYDG-TLLFVSHD 502
Cdd:COG4152 148 PEL--LILDEPFSGLDPVNVELLKDVIreLAAKGtTVIFSSHQ 188
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
332-521 |
1.66e-20 |
|
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: 90.27 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGPQVKE---AYLPQiir 402
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvTGVPPERrniGMVFQ--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 fdhpDWNLVENMMAAK--------KGLSAQSARNRLAAYDFRGEDVF---KPVSVLSGGEQSRLRL--CMLMDDEInfLI 469
Cdd:cd03259 80 ----DYALFPHLTVAEniafglklRGVPKAEIRARVRELLELVGLEGllnRYPHELSGGQQQRVALarALAREPSL--LL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 470 LDEPTNHLDIDSREWIEEAVEAY----DGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqrelGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
329-521 |
2.37e-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: 90.26 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLF----EGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIR-- 402
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -------FDHPDWNL---------VENMMAAKKGLSAQSARNRLAAYDFRG----EDVFK--PVSvLSGGEQSRLRLCML 460
Cdd:cd03257 81 rkeiqmvFQDPMSSLnprmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVGvglpEEVLNryPHE-LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 461 MDDEINFLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQaqilDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-217 |
2.49e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGRRVGLISQI---P--- 76
Cdd:COG4152 2 LELKGLTKRFG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRIgylPeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 -VYPAgCTVEDVLRsAFARLE--SLAEEMRALEARMaagesdpailkrygtlsERFEafggydtdvavnkianglsIPDS 153
Cdd:COG4152 81 gLYPK-MKVGEQLV-YLARLKglSKAEAKRRADEWL-----------------ERLG-------------------LGDR 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 154 QRSQLfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTI---SHD 217
Cdd:COG4152 123 ANKKV-EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVifsSHQ 188
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-235 |
3.32e-20 |
|
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: 89.39 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ------GRRVGLISQip 76
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQdvsdlrGRAIPYLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 vyPAGCTVEDVL----RSAFarlESLAEEMRALEA-RMAAGESDPAILKRYGtLSERfeafggydtdvaVNKIANGlsip 151
Cdd:cd03292 79 --KIGVVFQDFRllpdRNVY---ENVAFALEVTGVpPREIRKRVPAALELVG-LSHK------------HRALPAE---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 152 dsqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH---GTVVTISHDRYFLDRTVTRV 228
Cdd:cd03292 137 ----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRV 206
|
....*..
gi 2526491659 229 IEIQDGK 235
Cdd:cd03292 207 IALERGK 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-235 |
3.42e-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: 89.35 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgqgrrvglisqipvypA 80
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV----------------D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 GCTVEDVLRSAFARLESLAEEMrALEARMAAGESdpaiLKRYGtlseRFEAFGGYDTDVAVNKIANGLSIPDSqRSQLFD 160
Cdd:cd03266 66 GFDVVKEPAEARRRLGFVSDST-GLYDRLTAREN----LEYFA----GLYGLKGDELTARLEELADRLGMEEL-LDRRVG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
327-521 |
3.43e-20 |
|
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: 90.14 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDG---------------------- 384
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 385 ---------RIKTGPQVKE----AYLPQIIRFDHP---DWNLVENMMAakkglsaqsarnRLAAYDFRGedvfKPVSVLS 448
Cdd:COG1119 81 glvspalqlRFPRDETVLDvvlsGFFDSIGLYREPtdeQRERARELLE------------LLGLAHLAD----RPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 449 GGEQsrlRLCM----LMDD-EInfLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADG 519
Cdd:COG1119 145 QGEQ---RRVLiaraLVKDpEL--LILDEPTAGLDLGARElllaLLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
..
gi 2526491659 520 TI 521
Cdd:COG1119 220 RV 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
339-522 |
3.62e-20 |
|
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: 90.08 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 339 YGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQV----KEAYLPQI-IRFDHPD---WNL 410
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRIgVVFGQKTqlwWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 411 --VE--NMMAAKKGLSAQSARNRLA----AYDFrGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDS- 481
Cdd:cd03267 111 pvIDsfYLLAAIYDLPPARFKKRLDelseLLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAq 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526491659 482 ---REWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTIT 522
Cdd:cd03267 190 eniRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
330-482 |
3.64e-20 |
|
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: 89.17 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGeRIALIGDNGTGKSTLIKMIVGELYPDDGRI-----KTGPQVKEA-----YLPQ 399
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqDVLKQPQKLrrrigYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIRFdHPDWNLVE--NMMAAKKGLSAQSARNRLAA-------YDFRGedvfKPVSVLSGGEQSRLRLCMLMDDEINFLIL 470
Cdd:cd03264 80 EFGV-YPNFTVREflDYIAWLKGIPSKEVKARVDEvlelvnlGDRAK----KKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170
....*....|..
gi 2526491659 471 DEPTNHLDIDSR 482
Cdd:cd03264 155 DEPTAGLDPEER 166
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
332-521 |
4.33e-20 |
|
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: 89.10 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-----TGPQVKEA-----YLPQ 399
Cdd:cd03263 3 IRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysIRTDRKAArqslgYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 iirFDHPDWNLV--ENM--MAAKKGLSAQSARNRLAAY-------DFRGedvfKPVSVLSGGEQSRLRLCMLMDDEINFL 468
Cdd:cd03263 83 ---FDALFDELTvrEHLrfYARLKGLPKSEIKEEVELLlrvlgltDKAN----KRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 469 ILDEPTNHLDIDSREWIEEAVEAYDG--TLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
338-502 |
5.60e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 338 SYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIRFDhpdWNL---VENM 414
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP---DSLpltVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 415 MA----AKKGL----------SAQSARNRLAAYDFRGedvfKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDID 480
Cdd:NF040873 78 VAmgrwARRGLwrrltrddraAVDDALERVGLADLAG----RQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*
gi 2526491659 481 SREWIEEAV--EAYDG-TLLFVSHD 502
Cdd:NF040873 154 SRERIIALLaeEHARGaTVVVVTHD 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
330-520 |
5.96e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 89.42 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGPQVKEAYLPQIIR- 402
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgediTGLPPHEIARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 FDH----PDWNLVENMMAA-----KKGLSAQSARNRLAAYDFRGEDV----------FKPVSVLSGGEQSRLRLCMLMDD 463
Cdd:cd03219 81 FQIprlfPELTVLENVMVAaqartGSGLLLARARREEREARERAEELlervgladlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 464 EINFLILDEPT---NHLDIDS-REWIEEAVEAyDGTLLFVSHDRYFINRFATRIW------ELADGT 520
Cdd:cd03219 161 DPKLLLLDEPAaglNPEETEElAELIRELRER-GITVLLVEHDMDVVMSLADRVTvldqgrVIAEGT 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
6.18e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.76 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV------GQGRRVGL 71
Cdd:COG1116 5 APALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQipvypagctvEDVL---RSAFARLEsLAEEMRAL---EARMAAGEsdpaILKRYGtLSERFEAFggydtdvavnkia 145
Cdd:COG1116 85 VFQ----------EPALlpwLTVLDNVA-LGLELRGVpkaERRERARE----LLELVG-LAGFEDAY------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 146 nglsiPdsqrSQLfdslSGGEKTRVNLGRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHD 217
Cdd:COG1116 136 -----P----HQL----SGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-193 |
6.34e-20 |
|
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: 88.72 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVG-KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ----------GRRVGLI 72
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIPVYPAGCTVEDVLRsAFARLESLAEEmralearmaagesdpailkrygtlserfeafggyDTDVAVNKIANGLSIPD 152
Cdd:cd03263 81 PQFDALFDELTVREHLR-FYARLKGLPKS----------------------------------EIKEEVELLLRVLGLTD 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2526491659 153 SQRSQLFDsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:cd03263 126 KANKRART-LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-217 |
7.82e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.19 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG-----------QGRRVGLISQIP-VYPAgcTVED 86
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQDAhLFDT--TVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 87 VLRsaFARLESLAEEM-RALEarmAAGESDPAilkrygtlsERFEafGGYDTDVAvnkianglsiPDSQRsqlfdsLSGG 165
Cdd:TIGR02868 428 NLR--LARPDATDEELwAALE---RVGLADWL---------RALP--DGLDTVLG----------EGGAR------LSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLDLH-ATEWLEEYIRSFHG-TVVTISHD 217
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-217 |
8.26e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 89.33 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFevGKNV-LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV-GL---------IS 73
Cdd:COG0411 6 EVRGLTKRF--GGLVaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF-DGRDItGLpphriarlgIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 ---QIPVYPAGCTVEDVLR------------SAFARLESLAEEMRALEARMAagesdpAILKRYGtLSERfeafggydtd 138
Cdd:COG0411 83 rtfQNPRLFPELTVLENVLvaaharlgrgllAALLRLPRARREEREARERAE------ELLERVG-LADR---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 139 vavnkianglsipdsqRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTI 214
Cdd:COG0411 146 ----------------ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDergiTILLI 209
|
...
gi 2526491659 215 SHD 217
Cdd:COG0411 210 EHD 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
332-513 |
8.33e-20 |
|
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: 89.00 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDkhlfEGISLKVEGG-----ERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTgPQVKEAYLPQIIRFDHP 406
Cdd:cd03237 1 YTYPTMKKTL----GEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 407 dwNLVENMMAAK-KGLSAQSARNRLAAYDFRGEDVF-KPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREW 484
Cdd:cd03237 76 --GTVRDLLSSItKDFYTHPYFKTEIAKPLQIEQILdREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|...
gi 2526491659 485 IEEAVEAY----DGTLLFVSHDRYFINRFATRI 513
Cdd:cd03237 154 ASKVIRRFaennEKTAFVVEHDIIMIDYLADRL 186
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-216 |
8.53e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.31 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqG------------RRVG 70
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-GvdirdltleslrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYPAGcTVEDVLRsaFARLE-SLAEEMRAleARMAAgesdpailkrygtLSERFEAF-GGYDTDVAvnkiANGL 148
Cdd:COG1132 418 VVPQDTFLFSG-TIRENIR--YGRPDaTDEEVEEA--AKAAQ-------------AHEFIEALpDGYDTVVG----ERGV 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 sipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISH 216
Cdd:COG1132 476 ------------NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
328-479 |
9.65e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 328 EVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAY----------- 396
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWspaelarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 397 LPQ------------IIRF--------DHPDWNLVENMMAAkKGLSAqsarnrLAAYDFRgedvfkpvsVLSGGEQSRLR 456
Cdd:PRK13548 81 LPQhsslsfpftveeVVAMgraphglsRAEDDALVAAALAQ-VDLAH------LAGRDYP---------QLSGGEQQRVQ 144
|
170 180
....*....|....*....|....*....
gi 2526491659 457 ----LCML--MDDEINFLILDEPTNHLDI 479
Cdd:PRK13548 145 larvLAQLwePDGPPRWLLLDEPTSALDL 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-239 |
1.10e-19 |
|
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: 88.50 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGLISQipvypagct 83
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlrsafarleslaEEMRALEARM------AAGESD---------PaiLKRYGTLSERfEAfggydTDVAVNKIAN-G 147
Cdd:COG1127 75 ----------------KELYELRRRIgmlfqgGALFDSltvfenvafP--LREHTDLSEA-EI-----RELVLEKLELvG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 148 LsiPDSQrsQLFDS-LSGGEKTRVNLGR-LILeDTDILLLDEPTNHLDLHATEWLEEYIR----SFHGTVVTISHDRYFL 221
Cdd:COG1127 131 L--PGAA--DKMPSeLSGGMRKRVALARaLAL-DPEILLYDEPTAGLDPITSAVIDELIRelrdELGLTSVVVTHDLDSA 205
|
250
....*....|....*...
gi 2526491659 222 DRTVTRVIEIQDGKAEFY 239
Cdd:COG1127 206 FAIADRVAVLADGKIIAE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-231 |
1.21e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 88.33 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ-------------G 66
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 RRVGLISQ------IPVYPAGCTVEDVLRSAFARLESLAEEMRALEARMaAGESDPAILKRYgtlserfeafggydtdva 140
Cdd:cd03257 82 KEIQMVFQdpmsslNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRY------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsiPdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLhATEW-----LEEYIRSFHGTVVTIS 215
Cdd:cd03257 143 ----------P--------HELSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQAqildlLKKLQEELGLTLLFIT 203
|
250 260
....*....|....*....|....
gi 2526491659 216 HD----RYFLDRTVT----RVIEI 231
Cdd:cd03257 204 HDlgvvAKIADRVAVmyagKIVEE 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-501 |
1.51e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.86 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQVKEA---------YLP 398
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlCGEPVPSRarharqrvgVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QIIRFDhPDWNLVENMMAAKK--GLSAQSARNRL------AAYDFRGEdvfKPVSVLSGGEQSRLRLCMLMDDEINFLIL 470
Cdd:PRK13537 87 QFDNLD-PDFTVRENLLVFGRyfGLSAAAARALVppllefAKLENKAD---AKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....
gi 2526491659 471 DEPTNHLDIDSREWIEEAVE---AYDGTLLFVSH 501
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRsllARGKTILLTTH 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-235 |
1.52e-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: 86.47 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVglisqipvypagct 83
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDL-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlrsafARLESLAEEMRalearmaagesdpailKRYGTLSERFEAFggydtdvavnkiaNGLSIpdsqRSQLFDSLS 163
Cdd:cd03229 65 ---------TDLEDELPPLR----------------RRIGMVFQDFALF-------------PHLTV----LENIALGLS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
330-502 |
1.64e-19 |
|
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: 87.53 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDK----HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI------KTGPQVKEAYLPQ 399
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 iirfDH---PdW-NLVEN-MMAAK-KGLSAQSARNRLAAY-------DFrgEDVFkPvSVLSGGEQSRLRL--CMLMDDE 464
Cdd:cd03293 81 ----QDallP-WlTVLDNvALGLElQGVPKAEARERAEELlelvglsGF--ENAY-P-HQLSGGMRQRVALarALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2526491659 465 InfLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHD 502
Cdd:cd03293 152 V--LLLDEPFSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-235 |
1.69e-19 |
|
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: 88.16 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEV--------------------GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV 63
Cdd:cd03267 1 IEVSNLSKSYRVyskepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 64 GQ----GRRVGLISQIPVypagctvedvlrsAFARLESLAEEMRALEARmaagesdpAILKR-YGTLSERFEAfggydtd 138
Cdd:cd03267 81 AGlvpwKRRKKFLRRIGV-------------VFGQKTQLWWDLPVIDSF--------YLLAAiYDLPPARFKK------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 139 vAVNKIANGLSIPDSQRSQLfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATE----WLEEYIRSFHGTVVTI 214
Cdd:cd03267 133 -RLDELSELLDLEELLDTPV-RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEnirnFLKEYNRERGTTVLLT 210
|
250 260
....*....|....*....|.
gi 2526491659 215 SHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd03267 211 SHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-216 |
1.78e-19 |
|
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: 85.94 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKnVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVglisqipvypagct 83
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-GKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlrsafarleSLAEEMRALEARMAAgesdpailkrygtlserfeafggydtdVavnkianglsipdSQrsqlfdsLS 163
Cdd:cd03216 65 -------------SFASPRDARRAGIAM---------------------------V-------------YQ-------LS 84
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISH 216
Cdd:cd03216 85 VGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-238 |
1.79e-19 |
|
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: 86.21 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSF-EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVvvgqgrrvgLISQIPVYpagc 82
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVS---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 83 TVEDVLRSAFARLeslaeemralearmaagesdpailkrygtlserfeafggydtdvavnkianglsipdSQRSQLFDS- 161
Cdd:cd03247 68 DLEKALSSLISVL---------------------------------------------------------NQRPYLFDTt 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 162 --------LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HGTVVTISHDRYFLDRtVTRVIEI 231
Cdd:cd03247 91 lrnnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHHLTGIEH-MDKILFL 169
|
....*..
gi 2526491659 232 QDGKAEF 238
Cdd:cd03247 170 ENGKIIM 176
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
332-524 |
2.26e-19 |
|
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: 87.24 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVG--ELY---PDDGRIKTGPQ--VKEAYLPQIIR-- 402
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIpgaPDEGEVLLDGKdiYDLDVDVLELRrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ----FDHPdwNLV-----ENMMAAKK--GLSAQSARNRLAAYDFRGEDVFKPVS------VLSGGEQSRLRL--CMLMDD 463
Cdd:cd03260 83 vgmvFQKP--NPFpgsiyDNVAYGLRlhGIKLKEELDERVEEALRKAALWDEVKdrlhalGLSGGQQQRLCLarALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 464 EInfLILDEPTNHLDIDSREWIEEAVE--AYDGTLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:cd03260 161 EV--LLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
2.91e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.39 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRvglISQIPVYpa 80
Cdd:COG1137 1 MMTLEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD-GED---ITHLPMH-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 gctvedvLR------------SAFARLeSLAEEMRA-LEARmaaGESDPAILKRygtLSERFEAFGgydtdvaVNKIang 147
Cdd:COG1137 74 -------KRarlgigylpqeaSIFRKL-TVEDNILAvLELR---KLSKKEREER---LEELLEEFG-------ITHL--- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2526491659 148 lsipdsqRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEP 188
Cdd:COG1137 130 -------RKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-474 |
2.98e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFeVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVglisqipvypagct 83
Cdd:COG1129 5 LEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL-DGEPV-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedVLRSAFARLE----------SLAEEMRALEARMAAGEsdpaiLKRYGTLSERF------EAFGGYDTDVAVNKIANG 147
Cdd:COG1129 69 ---RFRSPRDAQAagiaiihqelNLVPNLSVAENIFLGRE-----PRRGGLIDWRAmrrrarELLARLGLDIDPDTPVGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 148 LSIpdSQRsQLfdslsggektrVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HG-TVVTISH-------- 216
Cdd:COG1129 141 LSV--AQQ-QL-----------VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISHrldevfei 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 217 -DRYfldrTVTRvieiqDGKaefysgnysfyavekerryqermkqyekeqaKIAQLEKAaeqlrvwafmgmdktyrrAIS 295
Cdd:COG1129 207 aDRV----TVLR-----DGR-------------------------------LVGTGPVA------------------ELT 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 296 MERRIERMrttakptKARKMDARFSSAEFH-GDEVLGIRNVSksygDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKM 374
Cdd:COG1129 229 EDELVRLM-------VGRELEDLFPKRAAApGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARA 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 375 IVGELYPDDGRIK------TGPQVKEA------YLPQ------IIrfdhPDWNLVENMMAA------KKGLSAQSARNRL 430
Cdd:COG1129 298 LFGADPADSGEIRldgkpvRIRSPRDAiragiaYVPEdrkgegLV----LDLSIRENITLAsldrlsRGGLLDRRRERAL 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 431 A-----AYDFRGEDVFKPVSVLSGGEQ-----SRlrlCMLMDDEInfLILDEPT 474
Cdd:COG1129 374 AeeyikRLRIKTPSPEQPVGNLSGGNQqkvvlAK---WLATDPKV--LILDEPT 422
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
347-519 |
3.56e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 347 GISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPDDGRIK---------TGPQ--VKEAYLPQIIR--FDHPDWNLVen 413
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILlngrplsdwSAAElaRHRAYLSQQQSppFAMPVFQYL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 414 MMAAKKGLSAQSARNRLA--AYDFRGEDVF-KPVSVLSGGEQSRLRL---CMLMDDEIN----FLILDEPTNHLDI---- 479
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAqlAEALGLEDKLsRPLTQLSGGEWQRVRLaavLLQVWPTINpegqLLLLDEPMNSLDVaqqa 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526491659 480 --DSreWIEEAVEAyDGTLLFVSHDryfIN---RFATRIWELADG 519
Cdd:COG4138 171 alDR--LLRELCQQ-GITVVMSSHD---LNhtlRHADRVWLLKQG 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-239 |
4.88e-19 |
|
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: 85.80 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVG-----LISQIP-- 76
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDiaarnRIGYLPee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 --VYPAgCTVEDVLRSaFARLeslaeemRALEARMAAGESDpAILKRYGtLSERfeafggydtdvavnkianglsipdsq 154
Cdd:cd03269 79 rgLYPK-MKVIDQLVY-LAQL-------KGLKKEEARRRID-EWLERLE-LSEY-------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 155 RSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVTRVIEI 231
Cdd:cd03269 122 ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
....*...
gi 2526491659 232 QDGKAEFY 239
Cdd:cd03269 202 NKGRAVLY 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
332-521 |
4.97e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 86.00 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD----KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQVKEAYLPQ 399
Cdd:cd03255 3 LKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEKELAAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIRF---DH---PDWNLVEN-MMAAK-KGLSAQSARNRlAAYDFR----GEDVFKPVSVLSGGEQSRLRLC--MLMDDEI 465
Cdd:cd03255 83 HIGFvfqSFnllPDLTALENvELPLLlAGVPKKERRER-AEELLErvglGDRLNHYPSELSGGQQQRVAIAraLANDPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 466 nfLILDEPTNHLDIDSREWI----EEAVEAYDGTLLFVSHDRyFINRFATRIWELADGTI 521
Cdd:cd03255 162 --ILADEPTGNLDSETGKEVmellRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
334-502 |
5.70e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.88 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 334 NVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGR--------IKTGPQVKE--AYLPQIIRF 403
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRRriGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DhPDWNLVEN--MMAAKKGLSAQSARNR----LAAYDFrGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHL 477
Cdd:cd03265 85 D-DELTGWENlyIHARLYGVPGAERRERidelLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180
....*....|....*....|....*....
gi 2526491659 478 DIDSR----EWIEEAVEAYDGTLLFVSHD 502
Cdd:cd03265 163 DPQTRahvwEYIEKLKEEFGMTILLTTHY 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-502 |
6.86e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIRFDHPDWNLV 411
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 412 ENMMAAKKGLSAQS---ARNRLAAydfrGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSR----EW 484
Cdd:PRK09544 87 NRFLRLRPGTKKEDilpALKRVQA----GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQvalyDL 162
|
170
....*....|....*...
gi 2526491659 485 IEEAVEAYDGTLLFVSHD 502
Cdd:PRK09544 163 IDQLRRELDCAVLMVSHD 180
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
330-516 |
6.89e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 90.42 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDK-HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG----PQVKE-------AYL 397
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvplADADAdswrdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQiirfdHP---DWNLVENMMAAKKGLSA---QSARNRLAAYDF---RGEDVFKPV----SVLSGGEQSRLRLCMLMDDE 464
Cdd:TIGR02857 402 PQ-----HPflfAGTIAENIRLARPDASDaeiREALERAGLDEFvaaLPQGLDTPIgeggAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 465 INFLILDEPTNHLDIDSREWIEEAVEAYDG--TLLFVSHDRYFINRfATRIWEL 516
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
229-319 |
9.36e-19 |
|
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: 81.08 E-value: 9.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 229 IEIQDGKAEFYSGNYSFYAVEKERRYQERMKQYEKEQAKIAQLEKAAEQLRVWAfmgmdKTYRRAISMERRIERMRTTAK 308
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKA-----SKAKQAQSRIKALEKMERIEK 75
|
90
....*....|.
gi 2526491659 309 PTKaRKMDARF 319
Cdd:pfam12848 76 PER-DKPKLRF 85
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
332-521 |
1.09e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 85.70 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD-KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGP----QVKEAYLPQI---IRF 403
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLrrqIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DHPDWNLVENMMAAKKGLSA--------QSARNR---------LAAYDFRG--EDVFKPVSVLSGGEQSRLRLCMLMDDE 464
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGrlgrrstwRSLFGLfpkeekqraLAALERVGllDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 465 INFLILDEPTNHLD-IDSREWIE---EAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03256 163 PKLILADEPVASLDpASSRQVMDllkRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
332-521 |
1.51e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.89 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ-VKE----------AYLP 398
Cdd:COG2274 476 LENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdLRQidpaslrrqiGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 Q--------I---IRFDHPDWNLVENMMAAKkglsaqsarnRLAAYDF--------------RGedvfkpvSVLSGGEQS 453
Cdd:COG2274 556 QdvflfsgtIrenITLGDPDATDEEIIEAAR----------LAGLHDFiealpmgydtvvgeGG-------SNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 454 RLRL--CMLMDDEInfLILDEPTNHLDIDSREWIEEAVEAYDG--TLLFVSHDRYFInRFATRIWELADGTI 521
Cdd:COG2274 619 RLAIarALLRNPRI--LILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-201 |
2.12e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRV 69
Cdd:PRK09536 1 MPMIDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraaSRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQIPVYPAGCTVEDVL-------RSAFARLESLAEemRALEARMAAGESDpailkrygtlseRFEAfggydtdvavn 142
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVemgrtphRSRFDTWTETDR--AAVERAMERTGVA------------QFAD----------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 143 kianglsipdsqrsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL-HATEWLE 201
Cdd:PRK09536 135 --------------RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLE 180
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-527 |
2.31e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVG------------L 71
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpakahqlgiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIPVYPAGCTV-EDVLrsafARLESLAEEMRALEARMAAgesdpailkrygtLSERFeafggyDTDVAvnkiANGLSI 150
Cdd:PRK15439 91 VPQEPLLFPNLSVkENIL----FGLPKRQASMQKMKQLLAA-------------LGCQL------DLDSS----AGSLEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 151 PDSQRsqlfdslsggektrVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF----HGtVVTISHDRYFLDRTVT 226
Cdd:PRK15439 144 ADRQI--------------VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELlaqgVG-IVFISHKLPEIRQLAD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 227 RVIEIQDGKAEFysgnysfyavekerryQERMKQYEKEQakIAQlekaaeqlrvwafmgmdktyrrAISMERRIERMRTT 306
Cdd:PRK15439 209 RISVMRDGTIAL----------------SGKTADLSTDD--IIQ----------------------AITPAAREKSLSAS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 307 AKPTKARKMDARFSSAEFhgdEVLGIRNVSksyGDKhlFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:PRK15439 249 QKLWLELPGNRRQQAAGA---PVLTVEDLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 387 K------TGPQVKEA------YLPQI-----IRFDHP-DWNlVENMMAAKKGLSAQSARNRL------AAYDFRGEDVFK 442
Cdd:PRK15439 321 MlngkeiNALSTAQRlarglvYLPEDrqssgLYLDAPlAWN-VCALTHNRRGFWIKPARENAvleryrRALNIKFNHAEQ 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 443 PVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVE--AYDGT-LLFVSHDRYFINRFATRIWELADG 519
Cdd:PRK15439 400 AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRsiAAQNVaVLFISSDLEEIEQMADRVLVMHQG 479
|
....*...
gi 2526491659 520 TITDYPCG 527
Cdd:PRK15439 480 EISGALTG 487
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
327-523 |
2.47e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.32 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGDK----HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQV----KEAYLP 398
Cdd:COG1136 2 SPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QIiRFDH-----------PDWNLVEN-MMAAK-KGLSAQSARNRLAAY-------DFRGedvfKPVSVLSGGEQSRLRLC 458
Cdd:COG1136 82 RL-RRRHigfvfqffnllPELTALENvALPLLlAGVSRKERRERARELlervglgDRLD----HRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 459 --MLMDDEInfLILDEPTNHLDIDSREWI----EEAVEAYDGTLLFVSHDRYFINRfATRIWELADGTITD 523
Cdd:COG1136 157 raLVNRPKL--ILADEPTGNLDSKTGEEVlellRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
330-522 |
2.52e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.13 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYG--DKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKtgpqvkeaylpqiirFDHPD 407
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------------LDGVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 408 WNLVENMMAAKKGLSAQSarnrlaAYDFRG---EDVFKPvsvLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD-IDSRE 483
Cdd:cd03247 66 VSDLEKALSSLISVLNQR------PYLFDTtlrNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2526491659 484 WIEEAVE-AYDGTLLFVSHDRYFINRFaTRIWELADGTIT 522
Cdd:cd03247 137 LLSLIFEvLKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-238 |
2.88e-18 |
|
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: 83.62 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEVG-KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGrrvglISQIPvypa 80
Cdd:cd03369 6 EIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGID-----ISTIP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 gctvedvlrsafarleslaeeMRALEARMAAGESDPAILKryGTLSERFEAFGGYDTDvavnKIANGLSIPDSQrsqlfD 160
Cdd:cd03369 77 ---------------------LEDLRSSLTIIPQDPTLFS--GTIRSNLDPFDEYSDE----EIYGALRVSEGG-----L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIR-SFHG-TVVTISHdRYfldRTVT---RVIEIQDGK 235
Cdd:cd03369 125 NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIReEFTNsTILTIAH-RL---RTIIdydKILVMDAGE 200
|
....
gi 2526491659 236 -AEF 238
Cdd:cd03369 201 vKEY 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-216 |
4.64e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 83.82 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG-RRVGLIS---QIPVY 78
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDiREVTLDSlrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 79 PAGC-----TVEDVLRsaFARLESLAEEMRalEARMAAgESDPAILKrygtLSErfeafgGYDTDVAvnkiANGLSipds 153
Cdd:cd03253 81 PQDTvlfndTIGYNIR--YGRPDATDEEVI--EAAKAA-QIHDKIMR----FPD------GYDTIVG----ERGLK---- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 154 qrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HGTVVTISH 216
Cdd:cd03253 138 --------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-235 |
5.46e-18 |
|
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: 83.19 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFevGKNV-LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV----------GQGRRVGLI 72
Cdd:cd03265 1 IEVENLVKKY--GDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprEVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIPvypagcTVEDVLrSAFARLEslaeemraLEARMAagesdpailkrygtlserfeafgGYDTDVAVNKIANGLSIPD 152
Cdd:cd03265 79 FQDL------SVDDEL-TGWENLY--------IHARLY-----------------------GVPGAERRERIDELLDFVG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 153 --SQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIR----SFHGTVVTISHDRYFLDRTVT 226
Cdd:cd03265 121 llEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklkeEFGMTILLTTHYMEEAEQLCD 200
|
....*....
gi 2526491659 227 RVIEIQDGK 235
Cdd:cd03265 201 RVAIIDHGR 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-188 |
6.24e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 83.36 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRrvglISQIPVYPagct 83
Cdd:cd03218 1 LRAENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD----ITKLPMHK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlR------------SAFARLeSLAEEMRA-LEARmaaGESDPAILKRYGTLSERFeafggydtdvavnkianglSI 150
Cdd:cd03218 72 -----RarlgigylpqeaSIFRKL-TVEENILAvLEIR---GLSKKEREEKLEELLEEF-------------------HI 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 2526491659 151 pDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEP 188
Cdd:cd03218 124 -THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
329-521 |
1.81e-17 |
|
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: 85.73 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSY--GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPDDGRIK-----TGPQVKEAYLPQII 401
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISgevllDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 R-----FDHPDWNL----VENMMA---AKKGLSAQSARNR-LAAYDFRGEDVF--KPVSVLSGGEQSRLRLCMLMDDEIN 466
Cdd:COG1123 83 RrigmvFQDPMTQLnpvtVGDQIAealENLGLSRAEARARvLELLEAVGLERRldRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 467 FLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:COG1123 163 LLIADEPTTALDVTTQaeilDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
330-518 |
2.01e-17 |
|
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: 82.00 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLfEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-------KTGPQVKE--AYLPQi 400
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkdiTNLPPEKRdiSYVPQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 irfDH---PDWNLVENM---MAAKKGLSAQSARNRLAAYDFRGEDVF---KPVSvLSGGEQSRLRLCM--LMDDEInfLI 469
Cdd:cd03299 79 ---NYalfPHMTVYKNIaygLKKRKVDKKEIERKVLEIAEMLGIDHLlnrKPET-LSGGEQQRVAIARalVVNPKI--LL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 470 LDEPTNHLDIDS----REWIEEAVEAYDGTLLFVSHDryfinrfATRIWELAD 518
Cdd:cd03299 153 LDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD-------FEEAWALAD 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-217 |
2.12e-17 |
|
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: 81.46 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDY-----DEGTV-------------VVGQ 65
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVlldgkdiydldvdVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 66 GRRVGLISQIP-VYPAgcTVEDVLRSAfARLESLAEeMRALEARMAAGesdpaiLKRYGtLSERfeafggydtdvaVNKI 144
Cdd:cd03260 80 RRRVGMVFQKPnPFPG--SIYDNVAYG-LRLHGIKL-KEELDERVEEA------LRKAA-LWDE------------VKDR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 145 ANGLSipdsqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHD 217
Cdd:cd03260 137 LHALG------------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-235 |
2.15e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV------GQGR----RVG 70
Cdd:PRK13536 39 TVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpARARlaraRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIpvypagctveDVLRSAFARLESLAEEMRALeaRMAAGESDPAI--LKRYGTLSERfeafggYDTDVAvnkiangl 148
Cdd:PRK13536 118 VVPQF----------DNLDLEFTVRENLLVFGRYF--GMSTREIEAVIpsLLEFARLESK------ADARVS-------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 sipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFL---DRTV 225
Cdd:PRK13536 172 ------------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMeeaERLC 239
|
250
....*....|
gi 2526491659 226 TRVIEIQDGK 235
Cdd:PRK13536 240 DRLCVLEAGR 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-501 |
2.38e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 334 NVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQV---------KEAYLPQIIRF 403
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVpararlaraRIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DhPDWNLVENMMAAKK--GLSAQSARNRLAA-YDF-RGED-VFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD 478
Cdd:PRK13536 126 D-LEFTVRENLLVFGRyfGMSTREIEAVIPSlLEFaRLESkADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180
....*....|....*....|....*.
gi 2526491659 479 IDSREWIEE---AVEAYDGTLLFVSH 501
Cdd:PRK13536 205 PHARHLIWErlrSLLARGKTILLTTH 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
2.93e-17 |
|
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: 80.70 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGeRVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG----------RRVGLIS 73
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIPVYPAGCTVEDVLRSAfARLEslaeemraleaRMAAGESDPAI---LKRYGTlserfeafggydTDVAVNKIAnglsi 150
Cdd:cd03264 79 QEFGVYPNFTVREFLDYI-AWLK-----------GIPSKEVKARVdevLELVNL------------GDRAKKKIG----- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 151 pdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDlhatewLEEYIRsFHGTVVTISHDRYFL 221
Cdd:cd03264 130 ----------SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD------PEERIR-FRNLLSELGEDRIVI 183
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
290-522 |
3.21e-17 |
|
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: 85.20 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 290 YRRAIsmeRRIERMRTTAKPTKARKmdarfSSAEFHGDEVLGIRNVSKSY--GDKHLFEGISLKVEGGERIALIGDNGTG 367
Cdd:COG4987 302 VRAAA---RRLNELLDAPPAVTEPA-----EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 368 KSTLIKMIVGELYPDDGRIK---------TGPQVKE--AYLPQ---IirFDHpdwNLVENMMAAKKGLSAQSARNRLAA- 432
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLRRriAVVPQrphL--FDT---TLRENLRLARPDATDEELWAALERv 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 433 ------------YDFR-GEDVFKpvsvLSGGEQSRLRL--CMLMDDEInfLILDEPTNHLDIDS-REWIEEAVEAYDG-T 495
Cdd:COG4987 449 glgdwlaalpdgLDTWlGEGGRR----LSGGERRRLALarALLRDAPI--LLLDEPTEGLDAATeQALLADLLEALAGrT 522
|
250 260
....*....|....*....|....*..
gi 2526491659 496 LLFVSHDRYFINRFaTRIWELADGTIT 522
Cdd:COG4987 523 VLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
330-521 |
3.63e-17 |
|
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: 80.26 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVG-ELY-PDDGRiktgpqvkeaylpqiIRFDHPD 407
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhPKYeVTEGE---------------ILFKGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 408 WNLVENMMAAKKG--LSAQSarnrlaAYDFRG---EDVFKPVSV-LSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDS 481
Cdd:cd03217 66 ITDLPPEERARLGifLAFQY------PPEIPGvknADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526491659 482 REWIEEAVEAY---DGTLLFVSHDRYFINRF-ATRIWELADGTI 521
Cdd:cd03217 140 LRLVAEVINKLreeGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-502 |
8.56e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSY-----------GDKHLF----------EGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGP 390
Cdd:COG4586 4 VENLSKTYrvyekepglkgALKGLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 391 QV----KEAYLPQI---------IRFDHPdwnLVE--NMMAAKKGLSAQSARNRLAAYDfrgeDVF-------KPVSVLS 448
Cdd:COG4586 84 YVpfkrRKEFARRIgvvfgqrsqLWWDLP---AIDsfRLLKAIYRIPDAEYKKRLDELV----ELLdlgelldTPVRQLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 449 GGEQSRLRLC--MLMDDEInfLILDEPTNHLDIDS----REWIEEAVEAYDGTLLFVSHD 502
Cdd:COG4586 157 LGQRMRCELAaaLLHRPKI--LFLDEPTIGLDVVSkeaiREFLKEYNRERGTTILLTSHD 214
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-188 |
9.46e-17 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 80.01 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG-----------QGRR-VGL 71
Cdd:TIGR04406 2 LVAENLIKSYK-KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmheRARLgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIPVYPAGCTVEDVLRSAFARLESLAEEMRALEARmaagesdpailkrygTLSERFEafggydtdvavnkIANglsip 151
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLE---------------ALLEEFQ-------------ISH----- 127
|
170 180 190
....*....|....*....|....*....|....*..
gi 2526491659 152 dsQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEP 188
Cdd:TIGR04406 128 --LRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-236 |
1.09e-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: 80.14 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQG-----ERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLISQ--IPVYPAgcTVEDVLRSaf 92
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQyiKADYEG--TVRDLLSS-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 93 arleslaeemralearmaagesdpaILKRYGTLSErfeafggYDTDvavnkIANGLSIPDSQRSQLFDsLSGGEKTRVNL 172
Cdd:cd03237 85 -------------------------ITKDFYTHPY-------FKTE-----IAKPLQIEQILDREVPE-LSGGELQRVAI 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 173 GRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIeIQDGKA 236
Cdd:cd03237 127 AACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-VFEGEP 193
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
326-520 |
1.17e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 80.08 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 326 GDEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGpqvkeayLP- 398
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrdiTG-------LPp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 ------------QIIR-FdhPDWNLVENMMAA---KKGLSAQSARNRLAAYDFRGEDV-----------------FKPVS 445
Cdd:COG0411 74 hriarlgiartfQNPRlF--PELTVLENVLVAahaRLGRGLLAALLRLPRARREEREAreraeellervgladraDEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 446 VLSGGEQSRLRL--CMLMDDEInfLILDEPT---NHLDIDS-REWIEEAVEAYDGTLLFVSHDRYFINRFATRIW----- 514
Cdd:COG0411 152 NLSYGQQRRLEIarALATEPKL--LLLDEPAaglNPEETEElAELIRRLRDERGITILLIEHDMDLVMGLADRIVvldfg 229
|
....*..
gi 2526491659 515 -ELADGT 520
Cdd:COG0411 230 rVIAEGT 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
332-521 |
1.59e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG--------PQV---KEAYLPQ- 399
Cdd:COG4559 4 AENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawsPWElarRRAVLPQh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 -----------IIRF--------DHPDWNLVENMMAAKkGLSAqsarnrLAAYDFRGedvfkpvsvLSGGEQSRLR---- 456
Cdd:COG4559 84 sslafpftveeVVALgraphgssAAQDRQIVREALALV-GLAH------LAGRSYQT---------LSGGEQQRVQlarv 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 457 LCML---MDDEINFLILDEPTNHLDID--------SREWIEEaveayDGTLLFVSHDryfIN---RFATRIWELADGTI 521
Cdd:COG4559 148 LAQLwepVDGGPRWLFLDEPTSALDLAhqhavlrlARQLARR-----GGGVVAVLHD---LNlaaQYADRILLLHQGRL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-235 |
1.72e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 79.16 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLISQIpv 77
Cdd:cd03258 1 MIELK--NVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDLTLLSGK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 78 ypagctvedvlrsafarleslaeEMRALEARMAagesdpAILKRYGTLSERfeafggydtDVAVNkIANGLSI---PDSQ 154
Cdd:cd03258 76 -----------------------ELRKARRRIG------MIFQHFNLLSSR---------TVFEN-VALPLEIagvPKAE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 155 RSQ----------LFD-------SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVT 213
Cdd:cd03258 117 IEErvlellelvgLEDkadaypaQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTqsilALLRDINRELGLTIVL 196
|
250 260
....*....|....*....|..
gi 2526491659 214 ISHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd03258 197 ITHEMEVVKRICDRVAVMEKGE 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-193 |
1.91e-16 |
|
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: 79.20 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG----------RRVGLISQIPVYPAGCTV 84
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDvrdytlaslrRQIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVlrsAFARLESLAEEMRAlEARMAAGESdpailkrygtLSERFEafGGYDTDVAVNKIanglsipdsqrsqlfdSLSG 164
Cdd:cd03251 94 ENI---AYGRPGATREEVEE-AARAANAHE----------FIMELP--EGYDTVIGERGV----------------KLSG 141
|
170 180
....*....|....*....|....*....
gi 2526491659 165 GEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
330-521 |
2.18e-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: 77.26 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-------------GPQVke 394
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpnelGDHV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 395 AYLPQiirfdhpDWNLvenmmaakkgLSAQSARNrlaaydfrgedvfkpvsVLSGGEQSRLRLCMLMDDEINFLILDEPT 474
Cdd:cd03246 79 GYLPQ-------DDEL----------FSGSIAEN-----------------ILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526491659 475 NHLDIDSREWIEEAVE---AYDGTLLFVSHDRYFINRfATRIWELADGTI 521
Cdd:cd03246 125 SHLDVEGERALNQAIAalkAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
330-479 |
5.19e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ------VKE-----AYLP 398
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlsSRQlarrlALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QI------------IRFDHPDWNLVENMMAAKKGLSAQSARNRLAAYDFrgedVFKPVSVLSGGEQSRLRLCMLMDDEIN 466
Cdd:PRK11231 83 QHhltpegitvrelVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170
....*....|...
gi 2526491659 467 FLILDEPTNHLDI 479
Cdd:PRK11231 159 VVLLDEPTTYLDI 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
330-523 |
5.58e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDG-------------------RIKTGP 390
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtvlvagddvealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 391 Q-------------VKEAYLPQIIRFDHPDwnlvENMMAAkkglsAQSARNRLAAYDFrgedVFKPVSVLSGGEQSRLRL 457
Cdd:PRK09536 84 QdtslsfefdvrqvVEMGRTPHRSRFDTWT----ETDRAA-----VERAMERTGVAQF----ADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 458 CMLMDDEINFLILDEPTNHLDIDSR----EWIEEAVEayDG-TLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQvrtlELVRRLVD--DGkTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-238 |
6.08e-16 |
|
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: 77.15 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSF-EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRVG 70
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYPAGctvedVLRSAFARLESLAEEM--RALEarmAAGesdpailkrygtLSERFEAF-GGYDTDVAVNKiang 147
Cdd:cd03244 82 IIPQDPVLFSG-----TIRSNLDPFGEYSDEElwQALE---RVG------------LKEFVESLpGGLDTVVEEGG---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 148 lsipdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS-FHG-TVVTISHdRyfLDrTV 225
Cdd:cd03244 138 ------------ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDcTVLTIAH-R--LD-TI 201
|
250
....*....|....*..
gi 2526491659 226 T---RVIEIQDGK-AEF 238
Cdd:cd03244 202 IdsdRILVLDKGRvVEF 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-189 |
6.53e-16 |
|
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: 77.09 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV-GL---------ISQIPvypagctvEDvl 88
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDItGLppheraragIGYVP--------EG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 89 RSAFARLeSLAEEMraleaRMAAGESDPAILKRygTLSERFEAFggydtdvavnkianglsiP--DSQRSQLFDSLSGGE 166
Cdd:cd03224 84 RRIFPEL-TVEENL-----LLGAYARRRAKRKA--RLERVYELF------------------PrlKERRKQLAGTLSGGE 137
|
170 180
....*....|....*....|...
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPT 189
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-235 |
8.45e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV------VVGQGR----RVGLIS 73
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepVPSRARharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIPVYPAGCTVEDVLRsAFARLESL-AEEMRALEarmaagesdPAILKrYGTLSERFEAFGGydtdvavnkianglsipd 152
Cdd:PRK13537 87 QFDNLDPDFTVRENLL-VFGRYFGLsAAAARALV---------PPLLE-FAKLENKADAKVG------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 153 sqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHDRYFL---DRTVTRVI 229
Cdd:PRK13537 138 --------ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMeeaERLCDRLC 209
|
....*.
gi 2526491659 230 EIQDGK 235
Cdd:PRK13537 210 VIEEGR 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
332-521 |
1.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.78 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFE-----GISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGPQVKeayLPQI 400
Cdd:PRK13637 5 IENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdiTDKKVK---LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 -----IRFDHPDWNLVENMMA-------AKKGLSAQSARNRL-AAYDFRGED--VFKPVSV--LSGGEQSRLRLCMLMDD 463
Cdd:PRK13637 82 rkkvgLVFQYPEYQLFEETIEkdiafgpINLGLSEEEIENRVkRAMNIVGLDyeDYKDKSPfeLSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 464 EINFLILDEPTNHLDIDSREWIEEAV----EAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-521 |
1.47e-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: 76.09 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG--------PQVKEA---YLPQ 399
Cdd:cd03245 6 RNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPADLRRnigYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 I-----------IRFDHPDWNLVENMMAAKKGLSAQSARNRLAAYDFR-GEDVFKpvsvLSGGEQSRLRLCMLMDDEINF 467
Cdd:cd03245 86 DvtlfygtlrdnITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQiGERGRG----LSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 468 LILDEPTNHLDIDSREWIEEAVEAY--DGTLLFVSHdRYFINRFATRIWELADGTI 521
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
330-492 |
1.84e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.09 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI----KTGPQVKEAYLPQIIRFDH 405
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 -----PDWNLVENM--MAAKKGLSAQSARNRLAAYDFRG-EDVfkPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHL 477
Cdd:TIGR01189 81 lpglkPELSALENLhfWAAIHGGAQRTIEDALAAVGLTGfEDL--PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170
....*....|....*
gi 2526491659 478 DIDSREWIEEAVEAY 492
Cdd:TIGR01189 159 DKAGVALLAGLLRAH 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-72 |
2.02e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---------------------VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVV 62
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90
....*....|
gi 2526491659 63 VgQGRRVGLI 72
Cdd:COG1134 85 V-NGRVSALL 93
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-521 |
2.03e-15 |
|
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: 75.52 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSYGDKHL-FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ----VKEAYLPQIIR----- 402
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdLRGRAIPYLRRkigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 FDH----PDWNLVENMMAAKK--GLSAQSARNRLAA----YDFRGEDVFKPvSVLSGGEQSRLRLCMLMDDEINFLILDE 472
Cdd:cd03292 84 FQDfrllPDRNVYENVAFALEvtGVPPREIRKRVPAalelVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 473 PTNHLDID-SREWIE--EAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03292 163 PTGNLDPDtTWEIMNllKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-240 |
2.22e-15 |
|
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: 75.41 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVD---QGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG---------------QGRRVGLISQ-IPVYPA 80
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIGLVFQqYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 GCTVEDVlrsAFARLESLAEEMRALEARMAAGESDPAILKRYgtlserfeafggydtdvavnkianglsipdsqrsqlFD 160
Cdd:cd03297 90 LNVRENL---AFGLKRKRNREDRISVDELLDLLGLDHLLNRY------------------------------------PA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIR----SFHGTVVTISHDRYFLDRTVTRVIEIQDGKA 236
Cdd:cd03297 131 QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKqikkNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
....
gi 2526491659 237 EFYS 240
Cdd:cd03297 211 QYIG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-219 |
2.34e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRVGLISQIPVYPAGCTVE 85
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 86 DVLrsafarleslaeemralearmAAGESdpAILKRYGTLSERFEAFggydtdvaVNKianglSIPDSQRSQLFD----S 161
Cdd:PRK11231 95 ELV---------------------AYGRS--PWLSLWGRLSAEDNAR--------VNQ-----AMEQTRINHLADrrltD 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL-HATEwLEEYIRSFHG---TVVTISHD-----RY 219
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInHQVE-LMRLMRELNTqgkTVVTVLHDlnqasRY 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
332-521 |
2.81e-15 |
|
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: 74.98 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKeAYLPQIIR-----FD-- 404
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRdiamvFQny 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 --HPDWNLVENMM----AAKKGLSAQSARNRLAAYDFRGEDVF--KPvSVLSGGEQSRLRLCMLMDDEINFLILDEPTNH 476
Cdd:cd03301 82 alYPHMTVYDNIAfglkLRKVPKDEIDERVREVAELLQIEHLLdrKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526491659 477 LD----IDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03301 161 LDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
333-522 |
3.15e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.05 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ-VKE----------AYLPQ- 399
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdIRDltleslrrqiGVVPQd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 -------I---IRFDHPDWNLVENMMAAKKglsAQsarnrlaAYDF--------------RGedvfkpvSVLSGGEqsRL 455
Cdd:COG1132 423 tflfsgtIrenIRYGRPDATDEEVEEAAKA---AQ-------AHEFiealpdgydtvvgeRG-------VNLSGGQ--RQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 456 RLC----MLMDDEInfLILDEPTNHLDIDSREWIEEAVEAY--DGTLLFVSHdryfinRFAT-----RIWELADGTIT 522
Cdd:COG1132 484 RIAiaraLLKDPPI--LILDEATSALDTETEALIQEALERLmkGRTTIVIAH------RLSTirnadRILVLDDGRIV 553
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-235 |
3.66e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGK--------------------NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV 63
Cdd:COG4586 2 IEVENLSKTYRVYEkepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 64 GqG-----------RRVGLI----SQ----IPVypagctvedvlrsafarLESLaeemrALEARMaAGESDPAILKRYGT 124
Cdd:COG4586 82 L-GyvpfkrrkefaRRIGVVfgqrSQlwwdLPA-----------------IDSF-----RLLKAI-YRIPDAEYKKRLDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 125 LSERFEafggydtdvavnkIANGLSIPDSQrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWL 200
Cdd:COG4586 138 LVELLD-------------LGELLDTPVRQ-------LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKeairEFL 197
|
250 260 270
....*....|....*....|....*....|....*...
gi 2526491659 201 EEYIRSFHGTVVTISHDryfLD---RTVTRVIEIQDGK 235
Cdd:COG4586 198 KEYNRERGTTILLTSHD---MDdieALCDRVIVIDHGR 232
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-226 |
3.85e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 75.54 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVKSFEvGKNVLDGLTFQVDQGE-RVgLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ----------------GR 67
Cdd:COG4674 12 YVEDLTVSFD-GFKALNDLSLYVDPGElRV-IIGPNGAGKTTLMDVITGKTRPDSGSVLFGGtdltgldeheiarlgiGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 68 RVglisQIP-VYPAgCTVEDVLRSAFARLESLaeeMRALEARMAAGESDpailkRYGTLSERFeafggydtdvavnkian 146
Cdd:COG4674 90 KF----QKPtVFEE-LTVFENLELALKGDRGV---FASLFARLTAEERD-----RIEEVLETI----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 147 GLSipdSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHDRYF---L 221
Cdd:COG4674 140 GLT---DKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHDMEFvrqI 216
|
....*
gi 2526491659 222 DRTVT 226
Cdd:COG4674 217 ARKVT 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-235 |
4.30e-15 |
|
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: 74.43 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN----VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgRRVGLISQIP-VY 78
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--GSIAYVSQEPwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 79 PAgcTVEDVLRsaFArlESLAEEM--RALEArmAAGESDPAILKrygtlserfeafGGYDTDVAVNKIanglsipdsqrs 156
Cdd:cd03250 79 NG--TIRENIL--FG--KPFDEERyeKVIKA--CALEPDLEILP------------DGDLTEIGEKGI------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 157 qlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWL-EEYIRSF---HGTVVTISHDRYFLDRtVTRVIEIQ 232
Cdd:cd03250 127 ----NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLLPH-ADQIVVLD 201
|
...
gi 2526491659 233 DGK 235
Cdd:cd03250 202 NGR 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
329-473 |
4.72e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TG-PQVKEA-----Y 396
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgediTHlPMHKRArlgigY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 397 LPQ---IIRfdhpdwNL-VE-NMMAA--KKGLSAQSARNRLAAY--DFRGEDVFK-PVSVLSGGEQSRLrlcmlmddEI- 465
Cdd:COG1137 83 LPQeasIFR------KLtVEdNILAVleLRKLSKKEREERLEELleEFGITHLRKsKAYSLSGGERRRV--------EIa 148
|
170
....*....|....*
gi 2526491659 466 -------NFLILDEP 473
Cdd:COG1137 149 ralatnpKFILLDEP 163
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
328-520 |
5.10e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 74.78 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 328 EVLGIRNVSKSY-----GDKHL--FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIktgpqvkeaylpqI 400
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-------------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRFDHPDWNLVE----NMMAAKK---GLSAQ--SARNRLAAYDF-----------------RGEDVFK-----------P 443
Cdd:COG4778 70 VRHDGGWVDLAQasprEILALRRrtiGYVSQflRVIPRVSALDVvaepllergvdreearaRARELLArlnlperlwdlP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 444 VSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSR----EWIEEAVEAydGT-LLFVSHDRYFINRFATRIWELAD 518
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR--GTaIIGIFHDEEVREAVADRVVDVTP 227
|
..
gi 2526491659 519 GT 520
Cdd:COG4778 228 FS 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-236 |
5.11e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.40 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgrrvglisqipvypaGC 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD----------------GA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 83 TVEDVLRSAFARleslaeemralearmaagesdpailkRYGTLSERFEAFGGydtdvavnkianglSIPDsqrsqlfDSL 162
Cdd:cd03246 65 DISQWDPNELGD--------------------------HVGYLPQDDELFSG--------------SIAE-------NIL 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 163 SGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS---FHGTVVTISHdRYFLDRTVTRVIEIQDGKA 236
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
348-519 |
5.19e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPDDGRIKTGPQ-----------VKEAYLPQIIR--FDHPDWNLVENM 414
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQpleawsaaelaRHRAYLSQQQTppFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 415 MAAKKGLSA-QSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRL---CMLMDDEIN----FLILDEPTNHLDIDSREWIE 486
Cdd:PRK03695 94 QPDKTRTEAvASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLaavVLQVWPDINpagqLLLLDEPMNSLDVAQQAALD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 2526491659 487 EAVEAY---DGTLLFVSHDRYFINRFATRIWELADG 519
Cdd:PRK03695 174 RLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
332-524 |
7.28e-15 |
|
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: 74.64 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKH-LFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLP------------ 398
Cdd:cd03295 3 FENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvelrrkigyviq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QIIRFDHpdWNLVENMMAAKKGLSAQSARNRLAAYDFRGEDVFKPVSV-------LSGGEQSRLRLCMLMDDEINFLILD 471
Cdd:cd03295 83 QIGLFPH--MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFadrypheLSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 472 EPTNHLDIDSREWIEEAV----EAYDGTLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:cd03295 161 EPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-229 |
8.55e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 26 QVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGrrvglISQIPVY----PAGcTVEDVLRSAFARLESlaee 101
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----ISYKPQYikpdYDG-TVEDLLRSITDDLGS---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 102 mralearmaagesdpailkRYgtlserfeafggYDTDvavnkIANGLSIPDsqrsqLFDS----LSGGEKTRVNLGRLIL 177
Cdd:PRK13409 431 -------------------SY------------YKSE-----IIKPLQLER-----LLDKnvkdLSGGELQRVAIAACLS 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 178 EDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVI 229
Cdd:PRK13409 470 RDADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.25e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 73.06 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGlisqiPVYPAGCT 83
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVT-----DLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRS-AFARLESLAEEMR-ALEARmaaGESDPAILKRygtlserfeafggydtdvaVNKIANGLSIpdsqrSQLFD- 160
Cdd:cd03301 74 IAMVFQNyALYPHMTVYDNIAfGLKLR---KVPKDEIDER-------------------VREVAELLQI-----EHLLDr 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 161 ---SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH----GTVVTISHD 217
Cdd:cd03301 127 kpkQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrlgTTTIYVTHD 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-235 |
1.42e-14 |
|
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: 73.41 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG----------RRVGL 71
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDirdisrkslrSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIPVYPAGcTVEDVLRsaFARLESLAEEMraLEARMAAGeSDPAILKRYgtlserfeafGGYDTDVAvnkiANGlsip 151
Cdd:cd03254 82 VLQDTFLFSG-TIMENIR--LGRPNATDEEV--IEAAKEAG-AHDFIMKLP----------NGYDTVLG----ENG---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 152 dsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS-FHG-TVVTISHdRYFLDRTVTRVI 229
Cdd:cd03254 138 --------GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH-RLSTIKNADKIL 208
|
....*.
gi 2526491659 230 EIQDGK 235
Cdd:cd03254 209 VLDDGK 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-235 |
1.54e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLvkSF---EVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQgrrvgliSQIPVYPa 80
Cdd:PRK11160 339 LTLNNV--SFtypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-------QPIADYS- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 gctvEDVLRSAFA----RLESLAEEMR---ALEARMAAGESDPAILKRYGtLSERFEAFGGYDTdvavnkianglSIPDS 153
Cdd:PRK11160 409 ----EAALRQAISvvsqRVHLFSATLRdnlLLAAPNASDEALIEVLQQVG-LEKLLEDDKGLNA-----------WLGEG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 154 QRSqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDlHATE-----WLEEYIRsfHGTVVTISHDRYFLDRtVTRV 228
Cdd:PRK11160 473 GRQ-----LSGGEQRRLGIARALLHDAPLLLLDEPTEGLD-AETErqileLLAEHAQ--NKTVLMITHRLTGLEQ-FDRI 543
|
....*..
gi 2526491659 229 IEIQDGK 235
Cdd:PRK11160 544 CVMDNGQ 550
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
332-502 |
2.05e-14 |
|
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: 73.14 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQI--IRFDHPDWN 409
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 410 LVENMMAAKK---GLSAQSARNRLAAYDFRG--EDVFKPV----------SVLSGGEQSRLRLCMLMDDEINFLILDEPT 474
Cdd:cd03296 85 LFRHMTVFDNvafGLRVKPRSERPPEAEIRAkvHELLKLVqldwladrypAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190
....*....|....*....|....*....|..
gi 2526491659 475 NHLDIDSRE----WIEEAVEAYDGTLLFVSHD 502
Cdd:cd03296 165 GALDAKVRKelrrWLRRLHDELHVTTVFVTHD 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
330-473 |
2.12e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.96 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG-------PQVKEA-----YL 397
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklPMHKRArlgigYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQ---IIRfdhpDWNLVENMMAA--KKGLSAQSARNRLAAY--DFRGEDVFK-PVSVLSGGEQSRLRL-CMLMDDEiNFL 468
Cdd:cd03218 81 PQeasIFR----KLTVEENILAVleIRGLSKKEREEKLEELleEFHITHLRKsKASSLSGGERRRVEIaRALATNP-KFL 155
|
....*
gi 2526491659 469 ILDEP 473
Cdd:cd03218 156 LLDEP 160
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
329-473 |
2.25e-14 |
|
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: 73.08 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG-------PQVKEA-----Y 396
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlPMHERArlgigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 397 LPQ---IIRfdhpDWNLVENMMAA---KKGLSAQSARNRLAAY--DFRGEDVFK-PVSVLSGGEQSRLRLCMLMDDEINF 467
Cdd:TIGR04406 81 LPQeasIFR----KLTVEENIMAVleiRKDLDRAEREERLEALleEFQISHLRDnKAMSLSGGERRRVEIARALATNPKF 156
|
....*.
gi 2526491659 468 LILDEP 473
Cdd:TIGR04406 157 ILLDEP 162
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
571-631 |
2.37e-14 |
|
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: 67.88 E-value: 2.37e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 571 RRQLTICERDIARAEERIAALEADMEAAAC--DYEKLNELVGQKDAAQAELDALYERWEQLSE 631
Cdd:pfam16326 7 QRELEELEAEIEKLEEEIAELEAQLADPELysDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-217 |
2.53e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRV-GL------IS 73
Cdd:COG3839 1 MASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG-GRDVtDLppkdrnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIP----VYPAGcTVEDVLrsAFArleslaeemraLEARmaaGESDPAILKRygtlserfeafggydtdvaVNKIANGLS 149
Cdd:COG3839 79 MVFqsyaLYPHM-TVYENI--AFP-----------LKLR---KVPKAEIDRR-------------------VREAAELLG 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 150 IpdsqrSQLFD----SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH----GTVVTISHD 217
Cdd:COG3839 123 L-----EDLLDrkpkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHrrlgTTTIYVTHD 193
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-235 |
2.64e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-----------GRRVGLISQIP----VypaGCTV 84
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvRRQVGMVFQNPdnqfV---GATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVLrsAFArLESLA---EEMralearmaagesdpailkrygtlSERFEAfggydtdvAVNKIaNGLSIPDSQRSqlfdS 161
Cdd:PRK13635 100 QDDV--AFG-LENIGvprEEM-----------------------VERVDQ--------ALRQV-GMEDFLNREPH----R 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDryfLDRTVT--RVIEIQDGK 235
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkgiTVLSITHD---LDEAAQadRVIVMNKGE 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-233 |
2.72e-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: 71.03 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIPVYPAgct 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlrsafarleslaeemralearmaagesdpailkryGTLserfeafggydtdvavnkianglsipdsqRSQLF---- 159
Cdd:cd03223 78 ---------------------------------------GTL-----------------------------REQLIypwd 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 160 DSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISHdRYFLDRTVTRVIEIQD 233
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-235 |
2.91e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLvkSFEV-GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDY--DEGTVVV-GQ-----------GRRV 69
Cdd:COG0396 2 EIKNL--HVSVeGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLdGEdilelspderaRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQIPVYPAGCTVEDVLRSAF-ARLE---SLAEEMRALEARMAAGESDPAILKRYgtlserfeafggydtdvaVNkia 145
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNFLRTALnARRGeelSAREFLKLLKEKMKELGLDEDFLDRY------------------VN--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 146 nglsipdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLD 222
Cdd:COG0396 139 --------------EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILD 204
|
250
....*....|....
gi 2526491659 223 R-TVTRVIEIQDGK 235
Cdd:COG0396 205 YiKPDFVHVLVDGR 218
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-222 |
4.35e-14 |
|
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: 72.29 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYD--EGTVVV-GQG---------RRVGL 71
Cdd:TIGR01978 1 LKIKDLHVSVE-DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFkGQDllelepderARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 I--SQIPVYPAGCTVEDVLRSAF-ARLE-------SLAEEMRALEARMAAGESDPAILKRYgtLSERFeafggydtdvav 141
Cdd:TIGR01978 80 FlaFQYPEEIPGVSNLEFLRSALnARRSargeeplDLLDFEKLLKEKLALLDMDEEFLNRS--VNEGF------------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 142 nkianglsipdsqrsqlfdslSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHA----TEWLEEYiRSFHGTVVTISHD 217
Cdd:TIGR01978 146 ---------------------SGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAlkivAEGINRL-REPDRSFLIITHY 203
|
....*
gi 2526491659 218 RYFLD 222
Cdd:TIGR01978 204 QRLLN 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-217 |
4.36e-14 |
|
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: 72.37 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG---------QGRRVGLIS 73
Cdd:cd03296 2 SIEVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QIPVYPAGCTVEDVLrsAFArLESLAEEMRALEARMAAGESDPAILKRYGTLSERFEAfggydtdvavnkianglsipds 153
Cdd:cd03296 81 QHYALFRHMTVFDNV--AFG-LRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA---------------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 154 qrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHD 217
Cdd:cd03296 136 -------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHD 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
332-502 |
5.07e-14 |
|
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: 71.88 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQvKEAYLPQIIR-----FDH- 405
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPPHKRpvntvFQNy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 ---PDWNLVENMMAA--KKGLSAQSARNRLA-AYDFRGEDVF--KPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHL 477
Cdd:cd03300 82 alfPHLTVFENIAFGlrLKKLPKAEIKERVAeALDLVQLEGYanRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180
....*....|....*....|....*....
gi 2526491659 478 DIDSREWIEEAVEAYDG----TLLFVSHD 502
Cdd:cd03300 162 DLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
289-502 |
6.04e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 74.70 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 289 TYRRAISMERRIERMRTTAKPTKArkmdarfssAEFHGDEVLG-------IRNVSKSY-GDKHLFEGISLKVEGGERIAL 360
Cdd:TIGR02868 296 QLTRVRAAAERIVEVLDAAGPVAE---------GSAPAAGAVGlgkptleLRDLSAGYpGAPPVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 361 IGDNGTGKSTLIKMIVGELYPDDGRIKTG----PQVKEAYLPQIIRFDHPDWNLV-----ENMMAAKKG-----LSAQSA 426
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvSSLDQDEVRRRVSVCAQDAHLFdttvrENLRLARPDatdeeLWAALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 427 RNRLAAYDFRGEDVFKPV-----SVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDID-SREWIEEAVEAYDG-TLLFV 499
Cdd:TIGR02868 447 RVGLADWLRALPDGLDTVlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLI 526
|
...
gi 2526491659 500 SHD 502
Cdd:TIGR02868 527 THH 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-189 |
6.21e-14 |
|
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: 71.55 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQG---------RRVGL-ISQIP----VYPaGCTV 84
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF-DGeditglpphRIARLgIGYVPegrrIFP-SLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVLRSAFARLESLAEEMRALEarmaagesdpAILKRYGTLSERfeafggydtdvavnkianglsipdsqRSQLFDSLSG 164
Cdd:COG0410 96 EENLLLGAYARRDRAEVRADLE----------RVYELFPRLKER--------------------------RRQRAGTLSG 139
|
170 180
....*....|....*....|....*
gi 2526491659 165 GEKTRVNLGRLILEDTDILLLDEPT 189
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-222 |
6.59e-14 |
|
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: 74.82 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 26 QVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGrrvglISQIPVYPAG---CTVEDVLRSAFARleslaeem 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----ISYKPQYISPdydGTVEEFLRSANTD-------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 103 ralearmaagesdpailkrygtlserfeafgGYDTDVAVNKIANGLSIpdsqrSQLFDS----LSGGEKTRVNLGRLILE 178
Cdd:COG1245 429 -------------------------------DFGSSYYKTEIIKPLGL-----EKLLDKnvkdLSGGELQRVAIAACLSR 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2526491659 179 DTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHDRYFLD 222
Cdd:COG1245 473 DADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLID 520
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
333-522 |
7.61e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.66 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMI-------VGELYPDDGRIKtGPQVKEaylpQIIR--- 402
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-DPKVDE----RLIRqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ---FDH----PDWNLVENMM-------AAKKGLSAQSARNRLAAYDFRGEDVFKPvSVLSGGEQSRLRLCMLMDDEINFL 468
Cdd:PRK09493 80 gmvFQQfylfPHLTALENVMfgplrvrGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 469 ILDEPTNHLDIDSREWIEEAVE--AYDG-TLLFVSHDRYFINRFATRIWELADGTIT 522
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQdlAEEGmTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
330-521 |
7.86e-14 |
|
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: 71.52 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGelYPD----DGRIKTGPQVKEAYLPQ------ 399
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDerarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 -IIRFDHP-DWNLVENMMAAKKGLSAQSARN----------------RLAAYDFRGEDVFKPVSV-LSGGEQSRLRLCML 460
Cdd:TIGR01978 79 lFLAFQYPeEIPGVSNLEFLRSALNARRSARgeepldlldfekllkeKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 461 MDDEINFLILDEPTNHLDIDSREWIEEAVEAY---DGTLLFVSHDRYFINRFA-TRIWELADGTI 521
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKpDYVHVLLDGRI 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
333-491 |
8.48e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK--TGPQVKEAYLPQIIRFDH----- 405
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldGGDIDDPDVAEACHYLGHrnamk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 PDWNLVENMM--AAKKGLSAQSARNRLAAYDFRG-EDVfkPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSR 482
Cdd:PRK13539 86 PALTVAENLEfwAAFLGGEELDIAAALEAVGLAPlAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
....*....
gi 2526491659 483 EWIEEAVEA 491
Cdd:PRK13539 164 ALFAELIRA 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-216 |
1.02e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRrvgliSQIPVYPAGCTVedvlrsafarl 95
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-----IDDPDVAEACHY----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 96 eslaeemralearmaAGESDPaiLKRYGTLSE--RFEA--FGGYDTDVAVNKIANGLS----IPdsqrsqlFDSLSGGEK 167
Cdd:PRK13539 78 ---------------LGHRNA--MKPALTVAEnlEFWAafLGGEELDIAAALEAVGLAplahLP-------FGYLSAGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 168 TRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSfH----GTVVTISH 216
Cdd:PRK13539 134 RRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HlaqgGIVIAATH 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
330-523 |
1.27e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ-------------VKEAY 396
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 397 LPQIIR------FDHPD-WN---LVENMMAAKK---GLSAQSARNRLAAY------DFRGEDVFkPVSvLSGGEQSRLRL 457
Cdd:PRK10619 86 QLRLLRtrltmvFQHFNlWShmtVLENVMEAPIqvlGLSKQEARERAVKYlakvgiDERAQGKY-PVH-LSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 458 CMLMDDEINFLILDEPTNHLDidsREWIEEAVE-----AYDG-TLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALD---PELVGEVLRimqqlAEEGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-235 |
1.31e-13 |
|
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: 74.01 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG--------QGRRVGLISQ 74
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslkdidRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 IPVYP---AGCTVEDVLRSAfarLESLAEEMRALEARMAagESDPAIlkrygtlsERFEAfgGYDTDVAVNKianglsip 151
Cdd:TIGR01193 553 LPQEPyifSGSILENLLLGA---KENVSQDEIWAACEIA--EIKDDI--------ENMPL--GYQTELSEEG-------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 152 dsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLhATEW--LEEYIRSFHGTVVTISHdRYFLDRTVTRVI 229
Cdd:TIGR01193 610 --------SSISGGQKQRIALARALLTDSKVLILDESTSNLDT-ITEKkiVNNLLNLQDKTIIFVAH-RLSVAKQSDKII 679
|
....*.
gi 2526491659 230 EIQDGK 235
Cdd:TIGR01193 680 VLDHGK 685
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-216 |
1.52e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLvkSFEVGKNVL-DGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRvglISQipvypagc 82
Cdd:PRK13538 2 LEARNL--ACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW-QGEP---IRR-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 83 tvedvLRSAFAR-------LESLAEEMRALE-----ARMAAGESDPAI---LKRYGTlsERFEafggydtDVAVNkiang 147
Cdd:PRK13538 68 -----QRDEYHQdllylghQPGIKTELTALEnlrfyQRLHGPGDDEALweaLAQVGL--AGFE-------DVPVR----- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 148 lsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSfH----GTVVTISH 216
Cdd:PRK13538 129 -------------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ-HaeqgGMVILTTH 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
330-474 |
1.82e-13 |
|
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: 70.16 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ----------VKE--AYL 397
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppherARAgiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQIIR-FdhPDWNLVEN-MMAAKKGLSAQSARNRLAAYD-------FRGedvfKPVSVLSGGEQSRLRLCM--LMDDEIn 466
Cdd:cd03224 81 PEGRRiF--PELTVEENlLLGAYARRRAKRKARLERVYElfprlkeRRK----QLAGTLSGGEQQMLAIARalMSRPKL- 153
|
....*...
gi 2526491659 467 fLILDEPT 474
Cdd:cd03224 154 -LLLDEPS 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
329-474 |
2.15e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK--------TGPqvKEAylpqi 400
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvriRSP--RDA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IR------FDHPdwNLVENM---------MAAKKG--LSAQSARNRLAA----YDFRgEDVFKPVSVLSGGEQSRLrlcm 459
Cdd:COG3845 78 IAlgigmvHQHF--MLVPNLtvaenivlgLEPTKGgrLDRKAARARIRElserYGLD-VDPDAKVEDLSVGEQQRV---- 150
|
170 180
....*....|....*....|...
gi 2526491659 460 lmddEI--------NFLILDEPT 474
Cdd:COG3845 151 ----EIlkalyrgaRILILDEPT 169
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-72 |
2.34e-13 |
|
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: 69.87 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---------------------VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVV 62
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90
....*....|
gi 2526491659 63 VgQGRRVGLI 72
Cdd:cd03220 81 V-RGRVSSLL 89
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
330-503 |
2.47e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.67 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRiktgpqvkeaylpqiIRFDHPDWN 409
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR---------------ILLDGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 410 LVE------NMM-----------AAK--------KGLSAQSARNR---------LAAYDFRgedvfKPvSVLSGGEQSRL 455
Cdd:COG3842 71 GLPpekrnvGMVfqdyalfphltVAEnvafglrmRGVPKAEIRARvaellelvgLEGLADR-----YP-HQLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 456 RL--CMLMDDEInfLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSHDR 503
Cdd:COG3842 145 ALarALAPEPRV--LLLDEPLSALDAKLREemreELRRLQRELGITFIYVTHDQ 196
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-235 |
2.53e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEVG--------KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLI 72
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIPVYPAGCTVEDVLRSAFARL-------ESLAEEMRALEARMAAGesdpailkRYGTLSERFEAFGgydtdvavnkia 145
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVnprktvrEIIREPLRHLLSLDKAE--------RLARASEMLRAVD------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 146 nglsIPDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLH----ATEWLEEYIRSFHGTVVTISHDRYFL 221
Cdd:PRK10419 140 ----LDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQFGTACLFITHDLRLV 215
|
250
....*....|....
gi 2526491659 222 DRTVTRVIEIQDGK 235
Cdd:PRK10419 216 ERFCQRVMVMDNGQ 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-217 |
2.53e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 12 SFEV-GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVvvgqgrrvgLISQIPVypagctvEDVLRS 90
Cdd:PRK10575 18 SFRVpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI---------LLDAQPL-------ESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 91 AFAR-LESLAEEMRALEArMAAGESdpAILKRY---GTLSeRFEAFGGYDTDVAVNKIanGLSiPDSQRsqLFDSLSGGE 166
Cdd:PRK10575 82 AFARkVAYLPQQLPAAEG-MTVREL--VAIGRYpwhGALG-RFGAADREKVEEAISLV--GLK-PLAHR--LVDSLSGGE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPTNHLDL-HATEWLE--EYIRSFHG-TVVTISHD 217
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLSQERGlTVIAVLHD 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
332-521 |
2.70e-13 |
|
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: 69.56 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHL-FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK----TGPQVKE-------AYLPQ 399
Cdd:cd03254 5 FENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgiDIRDISRkslrsmiGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 --------I---IRFDHPDwNLVENMMAAKKGLSAQSARNRLA-AYDF----RGEDvfkpvsvLSGGEQSRLRL--CMLM 461
Cdd:cd03254 85 dtflfsgtImenIRLGRPN-ATDEEVIEAAKEAGAHDFIMKLPnGYDTvlgeNGGN-------LSQGERQLLAIarAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 462 DDEInfLILDEPTNHLDIDSREWIEEAVEA--YDGTLLFVSHdRYFINRFATRIWELADGTI 521
Cdd:cd03254 157 DPKI--LILDEATSNIDTETEKLIQEALEKlmKGRTSIIIAH-RLSTIKNADKILVLDDGKI 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
311-521 |
3.24e-13 |
|
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: 72.85 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 311 KARKMDarfSSAEFHGDevLGIRNVSKSYG-DKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG 389
Cdd:TIGR01193 460 NKKKRT---ELNNLNGD--IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 390 P----QVKEAYLPQIIRF--DHP---DWNLVENM-MAAKKGLSAQSARNRLAAYDFRGE----------DVFKPVSVLSG 449
Cdd:TIGR01193 535 GfslkDIDRHTLRQFINYlpQEPyifSGSILENLlLGAKENVSQDEIWAACEIAEIKDDienmplgyqtELSEEGSSISG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 450 GEQSRLRLCMLMDDEINFLILDEPTNHLD-IDSREWIEEAVEAYDGTLLFVSHdRYFINRFATRIWELADGTI 521
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
311-520 |
3.63e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 311 KARKMDARFSSAEFHGDEVLGIRNVS-KSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPD-DGRIKT 388
Cdd:COG4178 344 AADALPEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 389 GPQVKEAYLPQIIRF----------------DHPDWNLVENMMAAkkGLSAQSAR-NRLAAYDfrgedvfkpvSVLSGGE 451
Cdd:COG4178 423 PAGARVLFLPQRPYLplgtlreallypataeAFSDAELREALEAV--GLGHLAERlDEEADWD----------QVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 452 QSRL---RLCMLMDDeinFLILDEPTNHLDIDSREWIEEAV--EAYDGTLLFVSHdRYFINRFATRIWELADGT 520
Cdd:COG4178 491 QQRLafaRLLLHKPD---WLFLDEATSALDEENEAALYQLLreELPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
330-492 |
3.82e-13 |
|
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: 68.67 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGP----QVKEAYLPQIIRFDH 405
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 PD-----WNLVENMMAAKKGLSAQSARNRLAAYDFRG-EDVfkPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDI 479
Cdd:cd03231 81 APgikttLSVLENLRFWHADHSDEQVEEALARVGLNGfEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|...
gi 2526491659 480 DSREWIEEAVEAY 492
Cdd:cd03231 159 AGVARFAEAMAGH 171
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-233 |
4.14e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 69.83 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVG--------KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQgrrvglisq 74
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQ--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 iPVY---PAGctvedvlRSAFARLESLA--EEMRALEARMAAGESDPAILKRYGTLSERfeafggyDTDVAVNKIANGLS 149
Cdd:TIGR02769 74 -DLYqldRKQ-------RRAFRRDVQLVfqDSPSAVNPRMTVRQIIGEPLRHLTSLDES-------EQKARIAELLDMVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 150 IPDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLH----ATEWLEEYIRSFHGTVVTISHD----RYFL 221
Cdd:TIGR02769 139 LRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVlqavILELLRKLQQAFGTAYLFITHDlrlvQSFC 218
|
250
....*....|....*.
gi 2526491659 222 DRTVT----RVIEIQD 233
Cdd:TIGR02769 219 QRVAVmdkgQIVEECD 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
4.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 2 IEIQVNNLVKSFEVGK----NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgqgrrvglisqipV 77
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW-------------I 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 78 YpagctVEDVLRSAFARLESLAEEMRALEARMAAGESDPAILKRYGTL-----SERFEA-------FG----GYDTDVAV 141
Cdd:PRK13651 68 F-----KDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKEIRRRVGVVfqfaeYQLFEQtiekdiiFGpvsmGVSKEEAK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 142 NKIANGLSI---PDS--QRSQlFDsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH---GTVVT 213
Cdd:PRK13651 143 KRAAKYIELvglDESylQRSP-FE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNkqgKTIIL 220
|
250 260
....*....|....*....|...
gi 2526491659 214 ISHD-RYFLDRTvTRVIEIQDGK 235
Cdd:PRK13651 221 VTHDlDNVLEWT-KRTIFFKDGK 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-241 |
5.40e-13 |
|
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: 68.84 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDE---GTVVV-GQGR-------RVGLISQIPVYPAGCTVE 85
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRkpdqfqkCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 86 DVLRsaFARLESLAEEMralearmaageSDPAILKRYGTLSERfeafggydtDVAVNKIANglsipdsqrsQLFDSLSGG 165
Cdd:cd03234 100 ETLT--YTAILRLPRKS-----------SDAIRKKRVEDVLLR---------DLALTRIGG----------NLVKGISGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGKAeFYSG 241
Cdd:cd03234 148 ERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-217 |
5.40e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 68.80 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRvglISQIPVYPAGct 83
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKD---ITNLPPHKRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRSaFARLESL-AEEMRALEARMAagESDPAILKRygtlserfeafggydtdvavnKIANGLSIP--DSQRSQLFD 160
Cdd:cd03300 74 VNTVFQN-YALFPHLtVFENIAFGLRLK--KLPKAEIKE---------------------RVAEALDLVqlEGYANRKPS 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHD 217
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-519 |
7.26e-13 |
|
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: 68.09 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 355 GERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQV-----KEAYLPQIIR-----------FDHpdWNLVENMMAAK 418
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrKKINLPPQQRkiglvfqqyalFPH--LNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 419 KGLSA----QSARNRLAAYDFrGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWI----EEAVE 490
Cdd:cd03297 101 KRKRNredrISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLlpelKQIKK 179
|
170 180
....*....|....*....|....*....
gi 2526491659 491 AYDGTLLFVSHDRYFINRFATRIWELADG 519
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
329-501 |
7.92e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQVK---EAYLPQIIRFD 404
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIRrqrDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 H-----PDWNLVENM---MAAKKGLSAQSARNRLAAYDFRG-EDVfkPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTN 475
Cdd:PRK13538 81 HqpgikTELTALENLrfyQRLHGPGDDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 2526491659 476 HLDIDSREWIEEAVEAY---DGTLLFVSH 501
Cdd:PRK13538 159 AIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-522 |
9.61e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 335 VSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG----PQVKEAYLP----QI--IRF 403
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLKNREVPflrrQIgmIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DHP---DWNLVEN--MMAAKKGLSAQSARNRL-AAYDFRG-EDVFKPVSV-LSGGEQSRLRLCMLMDDEINFLILDEPTN 475
Cdd:PRK10908 87 DHHllmDRTVYDNvaIPLIIAGASGDDIRRRVsAALDKVGlLDKAKNFPIqLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526491659 476 HLDIDSREWIEEAVEAYDG---TLLFVSHDRYFINRFATRIWELADGTIT 522
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-235 |
1.03e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.55 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG------------RRVG 70
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKltddkkninelrQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQ-IPVYPAGCTVEDV---LRSAFARLESLAEEmRALEarmaagesdpaILKRYGtLSERFEAFGGydtdvavnkian 146
Cdd:cd03262 80 MVFQqFNLFPHLTVLENItlaPIKVKGMSKAEAEE-RALE-----------LLEKVG-LADKADAYPA------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 147 glsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDlhaTEWLEEYIRSF------HGTVVTISHDRYF 220
Cdd:cd03262 135 --------------QLSGGQQQRVAIARALAMNPKVMLFDEPTSALD---PELVGEVLDVMkdlaeeGMTMVVVTHEMGF 197
|
250
....*....|....*
gi 2526491659 221 LDRTVTRVIEIQDGK 235
Cdd:cd03262 198 AREVADRVIFMDDGR 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
333-524 |
1.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQIIR-----FDH 405
Cdd:PRK13652 7 RDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKfvglvFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 PDWNL----VENMMA---AKKGLSAQSARNRL-AAYDFRG-EDVFKPVS-VLSGGEQSRLRLCMLMDDEINFLILDEPTN 475
Cdd:PRK13652 87 PDDQIfsptVEQDIAfgpINLGLDEETVAHRVsSALHMLGlEELRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 476 HLDIDSRE----WIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:PRK13652 167 GLDPQGVKelidFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-234 |
1.08e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELdydEGTVVVGQGRRVGLISqIPVYPAGCTveDVLRSAFAR--LE 96
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVTGDVT-LNGEPLAAI--DAPRLARLRavLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 97 SLAEEMRALEARmaagesDPAILKRYGTlSERFEAFGGYDTDVAVNKIANGLSIPDSQRSqlFDSLSGGEKTRVNLGRLI 176
Cdd:PRK13547 90 QAAQPAFAFSAR------EIVLLGRYPH-ARRAGALTHRDGEIAWQALALAGATALVGRD--VTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 177 LE---------DTDILLLDEPTNHLDL-HATEWLE---EYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDG 234
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLaHQHRLLDtvrRLARDWNLGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
1.40e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.80 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ----------GRRV 69
Cdd:COG4604 1 MIEIK--NVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLdvattpsrelAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQIPVYPAGCTVEDVLrsAFAR-------LESLAEEM--RALEaRMAAGEsdpailkrygtLSERFeafggydtdva 140
Cdd:COG4604 78 AILRQENHINSRLTVRELV--AFGRfpyskgrLTAEDREIidEAIA-YLDLED-----------LADRY----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsipdsqrsqlFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL-HATEW---LEEYIRSFHGTVVTISH 216
Cdd:COG4604 133 ------------------LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkHSVQMmklLRRLADELGKTVVIVLH 194
|
.
gi 2526491659 217 D 217
Cdd:COG4604 195 D 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
325-479 |
1.53e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 325 HGDEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQV-----------K 393
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 394 EAYLPQiiRFDHPDWNLVENMMAAKKgLSAQSARNRLAAYDF-RGEDV-----FKP-----VSVLSGGEQSRLRLCMLMD 462
Cdd:PRK10575 87 VAYLPQ--QLPAAEGMTVRELVAIGR-YPWHGALGRFGAADReKVEEAislvgLKPlahrlVDSLSGGERQRAWIAMLVA 163
|
170
....*....|....*..
gi 2526491659 463 DEINFLILDEPTNHLDI 479
Cdd:PRK10575 164 QDSRCLLLDEPTSALDI 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-193 |
1.71e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRrvglISQIPVYP- 79
Cdd:PRK10895 1 MATLTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDED----ISLLPLHAr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 80 --AGCTVEDVLRSAFARLESLAEEMRALEARmaageSDPAILKRYGTLSERFEAFggydtdvavnKIANglsipdsQRSQ 157
Cdd:PRK10895 76 arRGIGYLPQEASIFRRLSVYDNLMAVLQIR-----DDLSAEQREDRANELMEEF----------HIEH-------LRDS 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 2526491659 158 LFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK10895 134 MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-193 |
1.78e-12 |
|
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: 70.13 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQG------------RRVGLISQIPVYPAGCT 83
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL-DGhdladytlaslrRQVALVSQDVVLFNDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVlrsAFARLESLAEEmRALEARMAAgesdpailkrygtlserfeafggYDTDVaVNKIANGLSIPDSQRSQLfdsLS 163
Cdd:TIGR02203 423 ANNI---AYGRTEQADRA-EIERALAAA-----------------------YAQDF-VDKLPLGLDTPIGENGVL---LS 471
|
170 180 190
....*....|....*....|....*....|
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
2.13e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.97 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG---------QGRRVGL 71
Cdd:COG3842 3 MPALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglppEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQipvypagcTVED-VlrsAFArLESLAEEMRALEARMAagesdpAILKRYG--TLSERFeafggydtdvavnkiangl 148
Cdd:COG3842 82 VFQdyalfphlTVAEnV---AFG-LRMRGVPKAEIRARVA------ELLELVGleGLADRY------------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 149 siPdsqrsqlfDSLSGGEKTRVNLGR-LILEdTDILLLDEPTNHLDLHATE----WLEEYIRSFHGTVVTISHDR 218
Cdd:COG3842 133 --P--------HQLSGGQQQRVALARaLAPE-PRVLLLDEPLSALDAKLREemreELRRLQRELGITFIYVTHDQ 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-238 |
2.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVG----KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ-------------G 66
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 RRVGLISQIPVYpagctvedvlrsafarleSLAEEmrALEARMA-----AGESDPAILKRygtlserfeafggydtdvaV 141
Cdd:PRK13637 83 KKVGLVFQYPEY------------------QLFEE--TIEKDIAfgpinLGLSEEEIENR-------------------V 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 142 NKIAN--GLSIPDSQRSQLFDsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTIS 215
Cdd:PRK13637 124 KRAMNivGLDYEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeynmTIILVS 202
|
250 260
....*....|....*....|...
gi 2526491659 216 HDRYFLDRTVTRVIEIQDGKAEF 238
Cdd:PRK13637 203 HSMEDVAKLADRIIVMNKGKCEL 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-236 |
3.04e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.45 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIPVYPAGCtvedvLRSAFARL 95
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGT-----LREALLYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 96 ESlAEEMRALEARmaagesdpAILKRYG--TLSERFeafggyDTDVAVNKIanglsipdsqrsqlfdsLSGGEKTRVNLG 173
Cdd:COG4178 450 AT-AEAFSDAELR--------EALEAVGlgHLAERL------DEEADWDQV-----------------LSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 174 RLILEDTDILLLDEPTNHLDLHATEWLEEYIRS--FHGTVVTISH----DRYFldrtvTRVIEIQDGKA 236
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHrstlAAFH-----DRVLELTGDGS 561
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-195 |
3.71e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 2 IEIQVNNL-VKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYdEGTVVV----------GQGRR-V 69
Cdd:PRK11174 348 VTIEAEDLeILSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKIngielreldpESWRKhL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQIPVYPAGCTVEDVLrsaFARLESLAEEMRALEARMAAGEsdpailkrygtlserFeafggydtdvaVNKIANGLS 149
Cdd:PRK11174 426 SWVGQNPQLPHGTLRDNVL---LGNPDASDEQLQQALENAWVSE---------------F-----------LPLLPQGLD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 150 IPDSQRSQlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLH 195
Cdd:PRK11174 477 TPIGDQAA---GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-231 |
3.77e-12 |
|
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: 65.59 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGrrvGLISQIPVYPAGCTV---EDVLRSAF 92
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLYlghAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 93 ARLESLaEEMRALEARMAAGESdpaiLKRYGtlserfeaFGGYDtDVAVNkianglsipdsqrsqlfdSLSGGEKTRVNL 172
Cdd:cd03231 89 SVLENL-RFWHADHSDEQVEEA----LARVG--------LNGFE-DRPVA------------------QLSAGQQRRVAL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 173 GRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSfH----GTVVTISHDRYFLDRTVTRVIEI 231
Cdd:cd03231 137 ARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-HcargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
330-479 |
4.85e-12 |
|
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: 66.38 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDG-------------------RIKTGP 390
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGtvdlagvdlhglsrrararRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 391 QVKEAYLPQIIR---------------FDHPDWNLVENMMAAKKGLSAQSARNrlaaydfrgedvfkpVSVLSGGEQSRL 455
Cdd:TIGR03873 82 QDSDTAVPLTVRdvvalgriphrslwaGDSPHDAAVVDRALARTELSHLADRD---------------MSTLSGGERQRV 146
|
170 180
....*....|....*....|....
gi 2526491659 456 RLCMLMDDEINFLILDEPTNHLDI 479
Cdd:TIGR03873 147 HVARALAQEPKLLLLDEPTNHLDV 170
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-237 |
4.85e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKnVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV---------VVGQGRRVGLISQ 74
Cdd:PRK10851 3 IEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 IPVYPAGCTVEDVLrsAFArLESLAEEMRAlearmaagesDPAILKRygtlserfeafggydtdvavnKIANGLSIpdSQ 154
Cdd:PRK10851 82 HYALFRHMTVFDNI--AFG-LTVLPRRERP----------NAAAIKA---------------------KVTQLLEM--VQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 155 RSQLFD----SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDRYFLDRTVT 226
Cdd:PRK10851 126 LAHLADrypaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelkfTSVFVTHDQEEAMEVAD 205
|
250
....*....|.
gi 2526491659 227 RVIEIQDGKAE 237
Cdd:PRK10851 206 RVVVMSQGNIE 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-217 |
6.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVG-KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVV----------VGQGR-RVGL 71
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenLKEIRkKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIP----VypaGCTVEDVLrsAFarleslaeemrALEARMAAGESDPAILKRYGTlserfeafggydtdvAVNkIANG 147
Cdd:PRK13632 88 IFQNPdnqfI---GATVEDDI--AF-----------GLENKKVPPKKMKDIIDDLAK---------------KVG-MEDY 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 148 LsipdsQRSQLFdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHD 217
Cdd:PRK13632 136 L-----DKEPQN--LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-235 |
6.95e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQ----------GRRVGLISQIPVYPAGCTVE 85
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEhiqhyaskevARRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 86 DvlrsafarleslaeemraLEARmaagesdpailKRYGTlSERFEAFGGYDTDvAVNKIANGLSIPDSQRsQLFDSLSGG 165
Cdd:PRK10253 100 E------------------LVAR-----------GRYPH-QPLFTRWRKEDEE-AVTKAMQATGITHLAD-QSVDTLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLDL-HATEWLE---EYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:PRK10253 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllsELNREKGYTLAAVLHDLNQACRYASHLIALREGK 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
332-521 |
7.09e-12 |
|
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: 65.71 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKH--LFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQIIR------ 402
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASLRRqiglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -----FDHpdwNLVENMMAAKKGLSAQSARN--RLA-AYDF--RGEDVFKPV-----SVLSGGEQSRLRLC--MLMDDEI 465
Cdd:cd03251 83 qdvflFND---TVAENIAYGRPGATREEVEEaaRAAnAHEFimELPEGYDTVigergVKLSGGQRQRIAIAraLLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 466 nfLILDEPTNHLDIDSREWIEEAVE--AYDGTLLFVSHdRYFINRFATRIWELADGTI 521
Cdd:cd03251 160 --LILDEATSALDTESERLVQAALErlMKNRTTFVIAH-RLSTIENADRIVVLEDGKI 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
332-521 |
9.03e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQVK--EAYLPQI-IRFDHpd 407
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfHGTDVSrlHARDRKVgFVFQH-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 408 WNLVENMMAAKK---GLSAQSARNRLAAYDFRgEDVFKPVSV-------------LSGGEQSRLRLCMLMDDEINFLILD 471
Cdd:PRK10851 83 YALFRHMTVFDNiafGLTVLPRRERPNAAAIK-AKVTQLLEMvqlahladrypaqLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 472 EPTNHLDI----DSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK10851 162 EPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
329-523 |
9.39e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHL----FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ------------V 392
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaeL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 393 KEAYLPQIIRFDH--PDWNLVEN-----MMAAKKGLSAQS-ARNRLAAYDFRGEDVFKPvSVLSGGEQSRLRLCMLMDDE 464
Cdd:PRK11629 85 RNQKLGFIYQFHHllPDFTALENvamplLIGKKKPAEINSrALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 465 INFLILDEPTNHLDIDSREWIEE---AVEAYDGT-LLFVSHDRYFINRFaTRIWELADGTITD 523
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQllgELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
332-521 |
1.04e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.49 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKE----------AYLPQ- 399
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVATtpsrelakrlAILRQe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 --II------------RFDHP-------DWNLVENMMAAkkgLSAQSARNRlaaydFRGEdvfkpvsvLSGGEQSRLRLC 458
Cdd:COG4604 84 nhINsrltvrelvafgRFPYSkgrltaeDREIIDEAIAY---LDLEDLADR-----YLDE--------LSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 459 MLMDDEINFLILDEPTNHLDID-SREW---IEEAVEAYDGTLLFVSHDryfIN---RFATRIWELADGTI 521
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKhSVQMmklLRRLADELGKTVVIVLHD---INfasCYADHIVAMKDGRV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-235 |
1.28e-11 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 64.87 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG----------RRVGLISQIPVYPAGCTVEDV 87
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDirdlnlrwlrSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 88 LRSAFARleSLAEEMRAleARMAagESDPAILKrygtLSErfeafgGYDTDVAvnkiANGLsipdsqrsqlfdSLSGGEK 167
Cdd:cd03249 98 RYGKPDA--TDEEVEEA--AKKA--NIHDFIMS----LPD------GYDTLVG----ERGS------------QLSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 168 TRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFhgTVVTISHdRYFLDRTVTRVIEIQDGK 235
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEklvqEALDRAMKGR--TTIVIAH-RLSTIRNADLIAVLQNGQ 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-235 |
1.51e-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: 64.09 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDY--DEGTVVVgQGrrvglisqipvypag 81
Cdd:cd03217 1 LEIKDLHVSVG-GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILF-KG--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 ctvEDVLrsafarleSLAEEMRALEARMAAGESDPAIlkrygtlserfeafggydtdvavnkiaNGLSIPDSQRSqLFDS 161
Cdd:cd03217 64 ---EDIT--------DLPPEERARLGIFLAFQYPPEI---------------------------PGVKNADFLRY-VNEG 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTV-TRVIEIQDGK 235
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKpDRVHVLYDGR 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
348-518 |
1.51e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.94 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIvGELYP-DDGRIKTGPQVKEAYLPQiirfdHPdwnlvenmmaakkglsaqsa 426
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQ-----RP-------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 427 rnrlaaYDFRG---EDVFKPVS-VLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSHd 502
Cdd:cd03223 74 ------YLPLGtlrEQLIYPWDdVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH- 146
|
170
....*....|....*.
gi 2526491659 503 RYFINRFATRIWELAD 518
Cdd:cd03223 147 RPSLWKFHDRVLDLDG 162
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
329-521 |
1.64e-11 |
|
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: 65.21 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSY---------GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQ 391
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 392 VKEAYLP--QIIRFDHP---------DWNLVE---NMMAAKKglSAQSAR--NRLAAYDFRGEDVFKPVSVLSGGEQSRL 455
Cdd:TIGR02769 82 QRRAFRRdvQLVFQDSPsavnprmtvRQIIGEplrHLTSLDE--SEQKARiaELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 456 RLCMLMDDEINFLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQavilELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
330-502 |
1.95e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.70 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGpqvkEAYLPQI---IRFDHP 406
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEAredTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 407 D-----WNLV-ENMMAAKKGLSAQSARNRLAAYDF--RGEDVfkPvSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD 478
Cdd:PRK11247 89 DarllpWKKViDNVGLGLKGQWRDAALQALAAVGLadRANEW--P-AALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180
....*....|....*....|....*...
gi 2526491659 479 ----IDSREWIEEAVEAYDGTLLFVSHD 502
Cdd:PRK11247 166 altrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-482 |
1.98e-11 |
|
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: 66.77 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGEL---DYDEGTVVVGQgrrvglisqiPVYPA 80
Cdd:TIGR02633 2 LEMKGIVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWDGEIYWSGS----------PLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 GctVEDVLRSAFARLE---SLAEEMRALEARMAAGE-SDPAILKRYGTLSERFEafggydtdvavnKIANGLSIPDSQRS 156
Cdd:TIGR02633 71 N--IRDTERAGIVIIHqelTLVPELSVAENIFLGNEiTLPGGRMAYNAMYLRAK------------NLLRELQLDADNVT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 157 QLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HGTV-VTISHDRYFLDRTVTRVIEIQD 233
Cdd:TIGR02633 137 RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLkaHGVAcVYISHKLNEVKAVCDTICVIRD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 234 GKAefysgnysfyavekerryqermkqyekeqakiaqlekaaeqlrvwafmgMDKTYRRAISMERRIERMrttakptKAR 313
Cdd:TIGR02633 217 GQH-------------------------------------------------VATKDMSTMSEDDIITMM-------VGR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 314 KMDARFSSaEFH--GDEVLGIRNVSKSYGD---KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPD------ 382
Cdd:TIGR02633 241 EITSLYPH-EPHeiGDVILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfegnv 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 383 --DGR---IKTGPQVKEAYLPQII--RFDH---PDWNLVENM-MAAKKGLSAQSARNRLAAYDFRGEDV----------F 441
Cdd:TIGR02633 319 fiNGKpvdIRNPAQAIRAGIAMVPedRKRHgivPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIqrlkvktaspF 398
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2526491659 442 KPVSVLSGGEQSR--LRLCMLMDDEInfLILDEPTNHLDIDSR 482
Cdd:TIGR02633 399 LPIGRLSGGNQQKavLAKMLLTNPRV--LILDEPTRGVDVGAK 439
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-235 |
1.99e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.26 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFevGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKIL-------TGEL-----DYD-EGTVVVGQGR- 67
Cdd:COG4161 2 SIQLKNINCFY--GSHqALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLniaghQFDfSQKPSEKAIRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 68 ---RVGLI-SQIPVYPAgCTVEDVLRSAFARLESLAEEmralEARMAAGEsdpaILKRYGtLSERFEAFggydtdvavnk 143
Cdd:COG4161 80 lrqKVGMVfQQYNLWPH-LTVMENLIEAPCKVLGLSKE----QAREKAMK----LLARLR-LTDKADRF----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 144 ianglsiPDSqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVT---ISHDRYF 220
Cdd:COG4161 139 -------PLH--------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqviVTHEVEF 203
|
250
....*....|....*
gi 2526491659 221 LDRTVTRVIEIQDGK 235
Cdd:COG4161 204 ARKVASQVVYMEKGR 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
332-521 |
2.02e-11 |
|
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: 63.93 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDK----HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAylPQIIRFD-- 404
Cdd:cd03266 4 ADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKE--PAEARRRlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 -HPDWNLVENMMAAKK---------GLSAQSARNRL--AAYDFRGEDVF-KPVSVLSGGEQSRLRLCMLMDDEINFLILD 471
Cdd:cd03266 82 fVSDSTGLYDRLTAREnleyfaglyGLKGDELTARLeeLADRLGMEELLdRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 472 EPTNHLDIDSREWIEEAVEAYDG---TLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
332-503 |
2.16e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-KTGPQVKEAYLPQ---IIRFDH-- 405
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGEDVTHRSIQQrdiCMVFQSya 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 --PDWNLVEN------MMAAKKGLSAQSARNRLAAYDFRG-EDVFkpVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNH 476
Cdd:PRK11432 89 lfPHMSLGENvgyglkMLGVPKEERKQRVKEALELVDLAGfEDRY--VDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190
....*....|....*....|....*....|.
gi 2526491659 477 LDID----SREWIEEAVEAYDGTLLFVSHDR 503
Cdd:PRK11432 167 LDANlrrsMREKIRELQQQFNITSLYVTHDQ 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
328-507 |
2.27e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 328 EVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELY--PDDGRIKtgpqVKEAYLPQiirfdh 405
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD----VPDNQFGR------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 pDWNLVENMmaAKKGlSAQSARNRLA------AYDFRgedvfKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD- 478
Cdd:COG2401 99 -EASLIDAI--GRKG-DFKDAVELLNavglsdAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDr 169
|
170 180 190
....*....|....*....|....*....|...
gi 2526491659 479 ----IDSREWIEEAVEAyDGTLLFVSHDRYFIN 507
Cdd:COG2401 170 qtakRVARNLQKLARRA-GITLVVATHHYDVID 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
320-521 |
2.59e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 320 SSAEFHGDevlgirNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQvkeaylpQ 399
Cdd:PRK10253 4 SVARLRGE------QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIRFDHPDwnlvenmMAAKKGLSAQSA-------------RNRLAAYD----FRGED----------------VFKPVSV 446
Cdd:PRK10253 71 IQHYASKE-------VARRIGLLAQNAttpgditvqelvaRGRYPHQPlftrWRKEDeeavtkamqatgithlADQSVDT 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 447 LSGGEQSRLRLCMLMDDEINFLILDEPTNHLD----IDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-217 |
2.64e-11 |
|
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: 64.24 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG----------RRVG-L 71
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDireqdpvelrRKIGyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIPVYPAGCTVEDVlrSAFARLESLAEEM---RALEARMAAGESDPAILKRYgtlserfeafggydtdvavnkiangl 148
Cdd:cd03295 81 IQQIGLFPHMTVEENI--ALVPKLLKWPKEKireRADELLALVGLDPAEFADRY-------------------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 149 siPDSqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWL-EEYIR---SFHGTVVTISHD 217
Cdd:cd03295 133 --PHE--------LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqEEFKRlqqELGKTIVFVTHD 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
332-502 |
2.88e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.44 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIV-------GELYPDDGRIKTGPQVK-------EAYL 397
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsGDLFIGEKRMNDVPPAErgvgmvfQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PqiirfdHPDWNLVENM------MAAKKGLSAQSARN-----RLAAYDFRgedvfKPVSvLSGGEQSRLRLCMLMDDEIN 466
Cdd:PRK11000 86 L------YPHLSVAENMsfglklAGAKKEEINQRVNQvaevlQLAHLLDR-----KPKA-LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2526491659 467 FLILDEPTNHLD----IDSREWIEEAVEAYDGTLLFVSHD 502
Cdd:PRK11000 154 VFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
329-521 |
3.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHL-FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVK-------EAYLPQ 399
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIRFDHPDWNL----VENMMA---AKKGLSAQSARNR----LAAYDFRGEDVfKPVSVLSGGEQSRLRLC--MLMDDEIn 466
Cdd:PRK13639 81 GIVFQNPDDQLfaptVEEDVAfgpLNLGLSKEEVEKRvkeaLKAVGMEGFEN-KPPHHLSGGQKKRVAIAgiLAMKPEI- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 467 fLILDEPTNHLDIDSREWIEEAVeaYD-----GTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK13639 159 -IVLDEPTSGLDPMGASQIMKLL--YDlnkegITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-216 |
3.78e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.26 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 18 NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG-----------RRVGLISQIPVYPAGcTVED 86
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 87 VLRSAFARleslAEEMRALEARMAAGESDpailkrygTLSErFEAfgGYDTDVavnkianglsipDSQRSQLfdslSGGE 166
Cdd:cd03248 107 NIAYGLQS----CSFECVKEAAQKAHAHS--------FISE-LAS--GYDTEV------------GEKGSQL----SGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISH 216
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
329-477 |
3.81e-11 |
|
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: 65.62 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPD---DGRIK-TGPQVKEAYLPQI---- 400
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYwSGSPLKASNIRDTerag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRFDHPDWNLVENMMAA-----------KKGLSAQS-----ARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDE 464
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAeniflgneitlPGGRMAYNamylrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170
....*....|...
gi 2526491659 465 INFLILDEPTNHL 477
Cdd:TIGR02633 160 ARLLILDEPSSSL 172
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-193 |
3.96e-11 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 62.57 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 11 KSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDY--DEGTVvvgqgrrvgLISQIPVYPagctveDVL 88
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEV---------LINGRPLDK------RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 89 R--SAFARLESLAeemralearmaagesdpailkrYGTLSERfEAFggydtdvavnKIANGLSipdsqrsqlfdSLSGGE 166
Cdd:cd03213 81 RkiIGYVPQDDIL----------------------HPTLTVR-ETL----------MFAAKLR-----------GLSGGE 116
|
170 180
....*....|....*....|....*..
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-235 |
4.00e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDgLTFQVDQGERVGLLGRNGAGKTTLFKIL-------TGELD-----YD-EGTVVVGQGRR-- 68
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhFDfSKTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 69 --VGLI-SQIPVYPAgCTVEDVLRSAFARLESLAEEmralEARMAAGEsdpaILKRYgtlseRFEAFggydtdvavnkia 145
Cdd:PRK11124 82 rnVGMVfQQYNLWPH-LTVQQNLIEAPCRVLGLSKD----QALARAEK----LLERL-----RLKPY------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 146 nglsipdSQRSQLfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVT---ISHDRYFLD 222
Cdd:PRK11124 135 -------ADRFPL--HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqviVTHEVEVAR 205
|
250
....*....|...
gi 2526491659 223 RTVTRVIEIQDGK 235
Cdd:PRK11124 206 KTASRVVYMENGH 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
329-508 |
4.85e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQVKE---AYLPQIIRFD 404
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfERQSIKKdlcTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 H-----PDWNLVENMMAAKKGLSAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDI 479
Cdd:PRK13540 81 HrsginPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 2526491659 480 DSREWIEEAVEAY---DGTLLFVSHDRYFINR 508
Cdd:PRK13540 161 LSLLTIITKIQEHrakGGAVLLTSHQDLPLNK 192
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
332-386 |
4.89e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.71 E-value: 4.89e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:COG3839 6 LENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI 60
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
336-513 |
4.96e-11 |
|
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: 61.82 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 336 SKSYGDKHLFEGISlKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTgPQVKEAYLPQIIRfdhpdwnlvenmm 415
Cdd:cd03222 7 VKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYID------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 416 aakkglsaqsarnrlaaydfrgedvfkpvsvLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSR----EWIEEAVEA 491
Cdd:cd03222 72 -------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEE 120
|
170 180
....*....|....*....|..
gi 2526491659 492 YDGTLLFVSHDRYFINRFATRI 513
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRI 142
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-521 |
5.35e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.62 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHL--FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG----PQVKEAYLPQII-- 401
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNgqpiADYSEAALRQAIsv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 ---RFDHPDWNLVENMMAAKKglsaqsarnrlAAYDFRGEDVFKPVSV--------------------LSGGEQSRLRLC 458
Cdd:PRK11160 419 vsqRVHLFSATLRDNLLLAAP-----------NASDEALIEVLQQVGLeklleddkglnawlgeggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 459 --MLMDDEInfLILDEPTNHLDIDSREWIEEAVEAY--DGTLLFVSHDRYFINRFaTRIWELADGTI 521
Cdd:PRK11160 488 raLLHDAPL--LLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
330-517 |
5.44e-11 |
|
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: 62.24 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVsKSYGDKH---LFEGISLkveggeriaLIGDNGTGKSTLIKMIVGELYPDDGRIKTGpqvkEAYLPQIIR---- 402
Cdd:cd03240 4 LSIRNI-RSFHERSeieFFSPLTL---------IVGQNGAGKTTIIEALKYALTGELPPNSKG----GAHDPKLIRegev 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -------FDHPDWNLVEnmmaakkglsaqsARNRLAAYDF----RGEDVFKP----VSVLSGGEQS------RLRLCMLM 461
Cdd:cd03240 70 raqvklaFENANGKKYT-------------ITRSLAILENvifcHQGESNWPlldmRGRCSGGEKVlasliiRLALAETF 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 462 DDEINFLILDEPTNHLDIDSREW-IEEAVEAYDGTLLF----VSHDRYFINRfATRIWELA 517
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFqlivITHDEELVDA-ADHIYRVE 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-237 |
6.49e-11 |
|
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: 64.36 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 23 LTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRrvglisqipvypagctvedVLRSAFARLEsLAEEM 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGR-------------------TLFDSRKGIF-LPPEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 103 RAL-----EARMAAGESDPAILkRYGTLSERfeafgGYDTDVAVNKIANGLSI-PDSQRsqLFDSLSGGEKTRVNLGRLI 176
Cdd:TIGR02142 75 RRIgyvfqEARLFPHLSVRGNL-RYGMKRAR-----PSERRISFERVIELLGIgHLLGR--LPGRLSGGEKQRVAIGRAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 177 LEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGT----VVTISHDRYFLDRTVTRVIEIQDGKAE 237
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfgipILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-216 |
7.30e-11 |
|
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: 61.99 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRrvgLISQIPVYPAGCtvedvlrSAFARL 95
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP---LAEQRDEPHENI-------LYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 96 ESLAEEMRALE-----ARMAAGESDpailkrygTLSERFEAFG--GYdTDVAVNkianglsipdsqrsqlfdSLSGGEKT 168
Cdd:TIGR01189 82 PGLKPELSALEnlhfwAAIHGGAQR--------TIEDALAAVGltGF-EDLPAA------------------QLSAGQQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 169 RVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSfH----GTVVTISH 216
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA-HlargGIVLLTTH 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
329-474 |
7.94e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK--------TGPQVKEAylpQI 400
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfRSPRDAQA---AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRFDHPDWNLV------ENMM----AAKKGL-----SAQSARNRLAAYDFRgEDVFKPVSVLSGGEQSRLRLCMLMDDEI 465
Cdd:COG1129 81 IAIIHQELNLVpnlsvaENIFlgrePRRGGLidwraMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
....*....
gi 2526491659 466 NFLILDEPT 474
Cdd:COG1129 160 RVLILDEPT 168
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
332-502 |
8.16e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.21 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYG---DKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQIIR----- 402
Cdd:PRK13650 7 VKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHkigmv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 FDHPDWNL----VENMMA---AKKGLSAQSARNRL-AAYDFRGEDVFK---PvSVLSGGEQSRLRLCMLMDDEINFLILD 471
Cdd:PRK13650 87 FQNPDNQFvgatVEDDVAfglENKGIPHEEMKERVnEALELVGMQDFKereP-ARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2526491659 472 EPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHD 502
Cdd:PRK13650 166 EATSMLDPEGRleliKTIKGIRDDYQMTVISITHD 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
349-521 |
8.60e-11 |
|
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: 62.13 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 349 SLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGpQVKEAYLPQIIR-----------FDH------------ 405
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAPPADRpvsmlfqennlFAHltveqnvglgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 406 PDWNLVENMMAAKKGLSAQSArnrLAAYDFRgedvfKPvSVLSGGEQSRLRL--CMLMDDEInfLILDEPTNHLDIDSRE 483
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVG---LAGLEKR-----LP-GELSGGERQRVALarVLVRDKPV--LLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2526491659 484 WIEEAV----EAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:cd03298 166 EMLDLVldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-193 |
9.65e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQG--------------RRV 69
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGepikydkksllevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQIP--VYPAGCTVEDVlrsAFARLeSLAEEMRALEARMAAGesdpaiLKRYGTlsERFEafggydtdvavNKIANg 147
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDV---AFGPL-NLGLSKEEVEKRVKEA------LKAVGM--EGFE-----------NKPPH- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 148 lsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK13639 137 -------------HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-193 |
1.03e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.32 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNL-VKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFkiltgeldydegtvvvgqgrrvglisqipvypag 81
Cdd:TIGR01271 1217 QMDVQGLtAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL---------------------------------- 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 ctvedvlrSAFARLESLAEEMR---------ALEA-RMAAGESDPAILKRYGTLSERFEAFGGYdTDVAVNKIAN--GL- 148
Cdd:TIGR01271 1263 --------SALLRLLSTEGEIQidgvswnsvTLQTwRKAFGVIPQKVFIFSGTFRKNLDPYEQW-SDEEIWKVAEevGLk 1333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 149 ----SIPDSQRSQLFDS---LSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:TIGR01271 1334 svieQFPDKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-523 |
1.19e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 328 EVLGIRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQV-KEAYLPQIIR-- 402
Cdd:PRK13635 4 EIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlSEETVWDVRRqv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ---FDHPDWNLV------------ENmmaakKGLS-------AQSARNRLAAYDFRGEDvfkPVSvLSGGEQSRLRLCML 460
Cdd:PRK13635 84 gmvFQNPDNQFVgatvqddvafglEN-----IGVPreemverVDQALRQVGMEDFLNRE---PHR-LSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 461 MDDEINFLILDEPTNHLDIDSREWIEEAV----EAYDGTLLFVSHDryfINR--FATRIWELADGTITD 523
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVrqlkEQKGITVLSITHD---LDEaaQADRVIVMNKGEILE 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-237 |
1.29e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.44 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLvkSFEVGKN----VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG----------RR 68
Cdd:PRK13650 5 IEVKNL--TFKYKEDqekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLlteenvwdirHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 69 VGLISQIPVYP-AGCTVEDVLrsAFArLESLA---EEM--RALEARMAAGESDpailkrygtLSERFEAfggydtdvavn 142
Cdd:PRK13650 83 IGMVFQNPDNQfVGATVEDDV--AFG-LENKGiphEEMkeRVNEALELVGMQD---------FKEREPA----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 143 kianglsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS----FHGTVVTISHDr 218
Cdd:PRK13650 140 ------------------RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD- 200
|
250 260
....*....|....*....|.
gi 2526491659 219 yfLDRTV--TRVIEIQDGKAE 237
Cdd:PRK13650 201 --LDEVAlsDRVLVMKNGQVE 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-217 |
1.54e-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: 61.58 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSfeVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG---------QGRRVGLISQ 74
Cdd:cd03299 1 LKVENLSKD--WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 75 IPVYPAGCTVEdvlrsafarlESLAEEMRALEarmaagESDPAILKRygtlserfeafggydtdvaVNKIANGLSIpdsq 154
Cdd:cd03299 79 NYALFPHMTVY----------KNIAYGLKKRK------VDKKEIERK-------------------VLEIAEMLGI---- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 155 rSQLFD----SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLH----ATEWLEEYIRSFHGTVVTISHD 217
Cdd:cd03299 120 -DHLLNrkpeTLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRtkekLREELKKIRKEFGVTVLHVTHD 189
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-235 |
1.59e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.97 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILtGELDYDEGTV--VVGQG------------ 66
Cdd:PRK10535 5 LELKDIRRSYPSGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTSGTyrVAGQDvatldadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 RR--VGLISQ----IPVYPAGCTVEdvLRSAFARLESLAEEMRALEarmaagesdpaILKRYGtLSERFeafggydtdva 140
Cdd:PRK10535 84 RRehFGFIFQryhlLSHLTAAQNVE--VPAVYAGLERKQRLLRAQE-----------LLQRLG-LEDRV----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsipDSQRSQLfdslSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATE----WLEEYIRSFHgTVVTISH 216
Cdd:PRK10535 139 -----------EYQPSQL----SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEevmaILHQLRDRGH-TVIIVTH 202
|
250
....*....|....*....
gi 2526491659 217 DRYFLDRTvTRVIEIQDGK 235
Cdd:PRK10535 203 DPQVAAQA-ERVIEIRDGE 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-521 |
1.83e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 343 HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPqvkeAYLPQIIRFDhpDWNLVENM 414
Cdd:PRK10771 13 HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtTTPP----SRRPVSMLFQ--ENNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 415 MAAKK---GL-------SAQSARNRLAAYDFRGEDVFK--PvSVLSGGEQSRLRL--CMLMDDEInfLILDEPTNHLDID 480
Cdd:PRK10771 87 TVAQNiglGLnpglklnAAQREKLHAIARQMGIEDLLArlP-GQLSGGQRQRVALarCLVREQPI--LLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526491659 481 SR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK10771 164 LRqemlTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
329-513 |
1.85e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQvKEAYLPQIIR------ 402
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-DLSHVPPYQRpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -----FDHpdwnlvenmMAAKKGLSAQSARNRLAAYDF--RGEDVFKPVSV----------LSGGEQSRLRLCMLMDDEI 465
Cdd:PRK11607 98 qsyalFPH---------MTVEQNIAFGLKQDKLPKAEIasRVNEMLGLVHMqefakrkphqLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 466 NFLILDEPTNHLDIDSREWIEEAV----EAYDGTLLFVSHDRYFINRFATRI 513
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVvdilERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-235 |
2.07e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 23 LTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYdEGTVVVG-----------QGRRVGLISQ-------IPVY------ 78
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAgqpleawsaaeLARHRAYLSQqqtppfaMPVFqyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 79 -PAGCTVEDVlrsafarlESLAEEmralearmaagesdpailkrygtLSERFeafggydtdvavnKIANGLSIPDSQrsq 157
Cdd:PRK03695 94 qPDKTRTEAV--------ASALNE-----------------------VAEAL-------------GLDDKLGRSVNQ--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 158 lfdsLSGGEKTRVNLGRLILE-------DTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISHDryfLDRTV-- 225
Cdd:PRK03695 127 ----LSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD---LNHTLrh 199
|
250
....*....|.
gi 2526491659 226 -TRVIEIQDGK 235
Cdd:PRK03695 200 aDRVWLLKQGK 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
325-521 |
2.36e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.95 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 325 HGDEVLGIRNVSKSY---GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI----KTGPQVKEAYL 397
Cdd:cd03248 7 HLKGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 ----------PQI--------IRFDHPDWNLvENMMAAKKGLSAQSARNRLA-AYDfrgEDVFKPVSVLSGGEQSRLRLC 458
Cdd:cd03248 87 hskvslvgqePVLfarslqdnIAYGLQSCSF-ECVKEAAQKAHAHSFISELAsGYD---TEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 459 MLMDDEINFLILDEPTNHLDIDSREWIEEAVeaYDG----TLLFVSHDRYFINRfATRIWELADGTI 521
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQAL--YDWperrTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
332-523 |
2.75e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLP------------Q 399
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirqlrQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIRFDHPDWNL------VENMMAA-------KKGLSAQSARNRLAAYDFRGEDVFKPvSVLSGGEQSRLRLCMLMDDEIN 466
Cdd:PRK11264 86 HVGFVFQNFNLfphrtvLENIIEGpvivkgePKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 467 FLILDEPTNHLDidsREWIEEAVEAYDG------TLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK11264 165 VILFDEPTSALD---PELVGEVLNTIRQlaqekrTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
325-488 |
3.20e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 325 HGDEVLGIRNVSkSYGDKHLfEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVkeAYLPQIirfd 404
Cdd:TIGR01271 424 NGDDGLFFSNFS-LYVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI--SFSPQT---- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 hpDW----NLVENMMAakkGLSAQSARNR-----------LAAYDFRGEDVFKPVSV-LSGGEQSRLRLCMLMDDEINFL 468
Cdd:TIGR01271 496 --SWimpgTIKDNIIF---GLSYDEYRYTsvikacqleedIALFPEKDKTVLGEGGItLSGGQRARISLARAVYKDADLY 570
|
170 180
....*....|....*....|
gi 2526491659 469 ILDEPTNHLDIDSREWIEEA 488
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFES 590
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-485 |
3.36e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV-------------G 70
Cdd:PRK10762 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY-LGKEVtfngpkssqeagiG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQ-IPVYPAGCTVEDVL-----RSAFARLesLAEEMRAlearmaagESDpAILKRygtlserfeafggydtdvavnki 144
Cdd:PRK10762 83 IIHQeLNLIPQLTIAENIFlgrefVNRFGRI--DWKKMYA--------EAD-KLLAR----------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 145 angLSIPDSQRsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF----HGtVVTISHdryf 220
Cdd:PRK10762 129 ---LNLRFSSD-KLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELksqgRG-IVYISH---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 221 ldrtvtrvieiqdgkaefysgnysfyavekerryqeRMKQyekeqakIAQLEKAAEQLRVWAFMGMDKTyrRAISMERRI 300
Cdd:PRK10762 200 ------------------------------------RLKE-------IFEICDDVTVFRDGQFIAEREV--ADLTEDSLI 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 301 ERMrttakptKARKMDARFSSAEF-HGDEVLGIRNVSKSyGdkhlFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGEL 379
Cdd:PRK10762 235 EMM-------VGRKLEDQYPRLDKaPGEVRLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAL 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 380 YPDDGRIKTGPQVKEAYLPQ--------IIRFDHPDWNLV------ENM-MAA-----KKGLSAQSARNRLAAYDFRgeD 439
Cdd:PRK10762 303 PRTSGYVTLDGHEVVTRSPQdglangivYISEDRKRDGLVlgmsvkENMsLTAlryfsRAGGSLKHADEQQAVSDFI--R 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 440 VF--------KPVSVLSGGEQSRLRLCM-LMDDEiNFLILDEPTNHLDIDSREWI 485
Cdd:PRK10762 381 LFniktpsmeQAIGLLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDVGAKKEI 434
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-235 |
4.06e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 60.58 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG-----------RRVGLISQIPVYPAGCTV 84
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlrRQVGVVLQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVlrsafARLESLAEEMRALEARMAAGESDpAILKrygtLSErfeafgGYDTDVAVNKIanglsipdsqrsqlfdSLSG 164
Cdd:cd03252 94 DNI-----ALADPGMSMERVIEAAKLAGAHD-FISE----LPE------GYDTIVGEQGA----------------GLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 165 GEKTRVNLGRLILEDTDILLLDEPTNHLDlhaTEWLEEYIRSFHG-----TVVTISHdRYFLDRTVTRVIEIQDGK 235
Cdd:cd03252 142 GQRQRIAIARALIHNPRILIFDEATSALD---YESEHAIMRNMHDicagrTVIIIAH-RLSTVKNADRIIVMEKGR 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-235 |
4.31e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgrrvGLISQIPvypagctvedvlRSAFARLESLA 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK-----GSVAYVP------------QQAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 100 EEM---RALEArmaagesdpailKRYGTLSErfeafggydtdvAVNKIANGLSIPDSQRSQLFD---SLSGGEKTRVNLG 173
Cdd:TIGR00957 717 ENIlfgKALNE------------KYYQQVLE------------ACALLPDLEILPSGDRTEIGEkgvNLSGGQKQRVSLA 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 174 RLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG-----TVVTISHDRYFLDRtVTRVIEIQDGK 235
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknkTRILVTHGISYLPQ-VDVIIVMSGGK 838
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
327-519 |
4.31e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGD-KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIR--- 402
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ---FDHPD--------WNLV----ENMmaakkGLSAQSARNR----LAA---YDFRGedvfKPVSVLSGGEQSRLRLC-- 458
Cdd:PRK13647 82 glvFQDPDdqvfsstvWDDVafgpVNM-----GLDKDEVERRveeaLKAvrmWDFRD----KPPYHLSYGQKKRVAIAgv 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 459 MLMDDEInfLILDEPTNHLDIDSREWIEEAVEAYDG---TLLFVSHDRYFINRFATRIWELADG 519
Cdd:PRK13647 153 LAMDPDV--IVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
329-521 |
4.41e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKH----LFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGElypDDG-----RIKTGP--QVKEAYL 397
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGssgevSLVGQPlhQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQiIRFDH-----------PDWNLVENMM--AAKKGLSAQSARNRLAAYDFR---GEDVFKPVSVLSGGEQSRLRLCMLM 461
Cdd:PRK10584 83 AK-LRAKHvgfvfqsfmliPTLNALENVElpALLRGESSRQSRNGAKALLEQlglGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 462 DDEINFLILDEPTNHLDIDSREWIEEAV----EAYDGTLLFVSHDRYFINRFATRIwELADGTI 521
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRL-RLVNGQL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
4.55e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFEVGKN---VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGeLD-YDEGTVVV-GQG--------- 66
Cdd:COG1135 1 MIELE--NLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSVLVdGVDltalserel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 ----RRVGLISQipvypagctvedvlrsAFARLESL-AEE--MRALEarmAAGESDPAILKRYGTLSERfeafggydtdV 139
Cdd:COG1135 78 raarRKIGMIFQ----------------HFNLLSSRtVAEnvALPLE---IAGVPKAEIRKRVAELLEL----------V 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 140 avnkianGLSipD------SQrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEyIRSFHG 209
Cdd:COG1135 129 -------GLS--DkadaypSQ-------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INRELG 191
|
....*....
gi 2526491659 210 -TVVTISHD 217
Cdd:COG1135 192 lTIVLITHE 200
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-234 |
4.70e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGK---NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGeLDYDEGTVVVGQG-------------- 66
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDTPTSGDVIFNGqpmsklssaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 --RRVGLISQIpvypagctveDVLRSAFARLESLAeeMRALEARMAAGESDPAILKRYGtlserfeafggydtdvavnki 144
Cdd:PRK11629 85 rnQKLGFIYQF----------HHLLPDFTALENVA--MPLLIGKKKPAEINSRALEMLA--------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 145 ANGLSipdsQRSQLFDS-LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSfHGT---VVTisH 216
Cdd:PRK11629 132 AVGLE----HRANHRPSeLSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAdsifQLLGELNRL-QGTaflVVT--H 204
|
250
....*....|....*...
gi 2526491659 217 DRYFLDRtVTRVIEIQDG 234
Cdd:PRK11629 205 DLQLAKR-MSRQLEMRDG 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
348-521 |
5.46e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGEL----YPDDGRIKTG-------------PQV--KEAYLPQIIR----FD 404
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVTGDvtlngeplaaidaPRLarLRAVLPQAAQpafaFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 HPDWNLVENMMAAKKGlSAQSARNR---LAAYDFRGED--VFKPVSVLSGGEQSRLRLCMLM------DDEI---NFLIL 470
Cdd:PRK13547 100 AREIVLLGRYPHARRA-GALTHRDGeiaWQALALAGATalVGRDVTTLSGGELARVQFARVLaqlwppHDAAqppRYLLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 471 DEPTNHLDIDSREWIEEAVEAYD-----GTLLFVsHDRYFINRFATRIWELADGTI 521
Cdd:PRK13547 179 DEPTAALDLAHQHRLLDTVRRLArdwnlGVLAIV-HDPNLAARHADRIAMLADGAI 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-527 |
5.76e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 339 YGDKHLFEgISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG----------PQVKEAYLPQIIRFDHPDW 408
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 409 NLVENMMAAKKGLSAQS-----------ARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHL 477
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNfgipkekaekiAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 478 DIDSR-EWIE--EAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITDypCG 527
Cdd:PRK13643 176 DPKARiEMMQlfESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS--CG 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-241 |
6.84e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKnVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTvvvgqGRRVGLISQIpVYPAGCT 83
Cdd:PRK09984 5 IRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSA-----GSHIELLGRT-VQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRS------AFARLeSLAEEMRALE-ARMAAGESDP--AILKRYGTLSERFEAFGGYdTDVAVNKIANglsipdsq 154
Cdd:PRK09984 78 ARDIRKSrantgyIFQQF-NLVNRLSVLEnVLIGALGSTPfwRTCFSWFTREQKQRALQAL-TRVGMVHFAH-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 155 rsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGT-----VVTISHDRYFLdRTVTRVI 229
Cdd:PRK09984 148 --QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgitvVVTLHQVDYAL-RYCERIV 224
|
250
....*....|..
gi 2526491659 230 EIQDGKAeFYSG 241
Cdd:PRK09984 225 ALRQGHV-FYDG 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-193 |
6.86e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 10 VKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELdydEGTVVVGQGRrvglISQIPVYPagctvEDVLR 89
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVD----VPDNQFGR-----EASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 90 SAFARLESLAEEMRALEarmAAGESDPAILKRygtlserfeafggydtdvavnkianglsipdsqrsqLFDSLSGGEKTR 169
Cdd:COG2401 104 DAIGRKGDFKDAVELLN---AVGLSDAVLWLR------------------------------------RFKELSTGQKFR 144
|
170 180
....*....|....*....|....
gi 2526491659 170 VNLGRLILEDTDILLLDEPTNHLD 193
Cdd:COG2401 145 FRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
325-524 |
6.92e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 59.35 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 325 HGDevLGIRNVSKSYGdKHL---FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQvkeaylpQII 401
Cdd:cd03369 4 HGE--IEVENLSVRYA-PDLppvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI-------DIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 RFDHPDWNLVENMMAAKKGLSAQSARNRLAAYD-FRGEDVFKPVSVLSGGEQ----SRLRLCML--MDDEINFLILDEPT 474
Cdd:cd03369 74 TIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDeYSDEEIYGALRVSEGGLNlsqgQRQLLCLAraLLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 475 NHLDIDSREWIEEAV--EAYDGTLLFVSHDRYFINRFAtRIWELADGTITDY 524
Cdd:cd03369 154 ASIDYATDALIQKTIreEFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
330-521 |
7.00e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLF---------EGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQV 392
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 393 KEAYLP--QIIRFDHPD---------WNLVENMMAAkKGLS--AQSARNR--LAAYDFRGEDVFKPVSVLSGGEQSRLRL 457
Cdd:PRK10419 84 RKAFRRdiQMVFQDSISavnprktvrEIIREPLRHL-LSLDkaERLARASemLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 458 CMLMDDEINFLILDEPTNHLDIDSREWI----EEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVirllKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-235 |
7.27e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.05 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG----------RRVGLISQIPVYPAGCTVEDV 87
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPlvqydhhylhRQVALVGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 88 lrsAFARLESLAEEMRAleARMAAGESDpailkrygtlserF--EAFGGYDTDVavnkianglsipDSQRSQLfdslSGG 165
Cdd:TIGR00958 576 ---AYGLTDTPDEEIMA--AAKAANAHD-------------FimEFPNGYDTEV------------GEKGSQL----SGG 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYiRSFHG-TVVTISHdRYFLDRTVTRVIEIQDGK 235
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES-RSRASrTVLLIAH-RLSTVERADQILVLKKGS 690
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-260 |
7.97e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSfeVGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYD--EGTVVVgQGR---------- 67
Cdd:CHL00131 7 ILEIK--NLHAS--VNENeILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILF-KGEsildlepeer 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 68 -RVG--LISQIPVYPAGCTVEDVLRSAF-ARLESLAEEmralearmaagESDPaiLKRYGTLSERFEafggydtdvAVNK 143
Cdd:CHL00131 82 aHLGifLAFQYPIEIPGVSNADFLRLAYnSKRKFQGLP-----------ELDP--LEFLEIINEKLK---------LVGM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 144 IANGLSipdsqrSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGT---VVTISHDRYF 220
Cdd:CHL00131 140 DPSFLS------RNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSensIILITHYQRL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2526491659 221 LDRTVTRVIEI-QDGKAeFYSGNYSFyAVEKERRYQERMKQ 260
Cdd:CHL00131 214 LDYIKPDYVHVmQNGKI-IKTGDAEL-AKELEKKGYDWLKQ 252
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
332-407 |
9.44e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.00 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLF--EGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQI-----IRF 403
Cdd:PRK13632 10 VENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIrkkigIIF 89
|
....
gi 2526491659 404 DHPD 407
Cdd:PRK13632 90 QNPD 93
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-235 |
9.84e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV-VVGQG----------RRVGLI 72
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREvnaenekwvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 SQIP---VYpAGCTVEDVlrsAFArleslaeemrALEARMAAGEsdpaILKRYGtlsERFEAFGGYDTdvavnkiangls 149
Cdd:PRK13647 85 FQDPddqVF-SSTVWDDV---AFG----------PVNMGLDKDE----VERRVE---EALKAVRMWDF------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 150 ipdsqRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVT 226
Cdd:PRK13647 132 -----RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWAD 206
|
....*....
gi 2526491659 227 RVIEIQDGK 235
Cdd:PRK13647 207 QVIVLKEGR 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-198 |
9.86e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG-RRVGLIS---QIPV 77
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDiRTVTRASlrrNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 78 Y--PAGC---TVEDVLRsaFARLESLAEEMRALEARMAAGEsdpAILKRYGtlserfeafgGYDTDVAvnkianglsipd 152
Cdd:PRK13657 414 VfqDAGLfnrSIEDNIR--VGRPDATDEEMRAAAERAQAHD---FIERKPD----------GYDTVVG------------ 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 153 sQRSQlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLhATE 198
Cdd:PRK13657 467 -ERGR---QLSGGERQRLAIARALLKDPPILILDEATSALDV-ETE 507
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-239 |
1.01e-09 |
|
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: 59.87 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNL-VKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFkiltgeldydegtvvvgqgrrvglisqipvypag 81
Cdd:cd03289 2 QMTVKDLtAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLL---------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 ctvedvlrSAFARLESLAEE----------MRALEARMAAGESDPAILKRYGTLSERFEAFGGYdTDVAVNKIAN--GL- 148
Cdd:cd03289 48 --------SAFLRLLNTEGDiqidgvswnsVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKW-SDEEIWKVAEevGLk 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 ----SIPDSQRSQLFDS---LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIR-SFHGTVVTISHDRYF 220
Cdd:cd03289 119 svieQFPGQLDFVLVDGgcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHRIE 198
|
250
....*....|....*....
gi 2526491659 221 LDRTVTRVIEIQDGKAEFY 239
Cdd:cd03289 199 AMLECQRFLVIEENKVRQY 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-259 |
1.03e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLI----SQIPVYPagctvEDVLRSAFAR 94
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVV-NGQTINLVrdkdGQLKVAD-----KNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 95 LE------SLAEEMRALEARMAAgesdPAILKRYGTLSERFEAFggydtdvavnKIANGLSIPDSQRSQLFDSLSGGEKT 168
Cdd:PRK10619 94 LTmvfqhfNLWSHMTVLENVMEA----PIQVLGLSKQEARERAV----------KYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 169 RVNLGRLILEDTDILLLDEPTNHLDlhaTEWLEEYIRSFH------GTVVTISHDRYFLDRTVTRVIEIQDGKAEFYSGN 242
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALD---PELVGEVLRIMQqlaeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*..
gi 2526491659 243 YSFYAVEKERRYQERMK 259
Cdd:PRK10619 237 EQLFGNPQSPRLQQFLK 253
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
329-497 |
1.16e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG-------PQVKEA-----Y 396
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllPLHARArrgigY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 397 LPQ---IIRfdhpDWNLVENMMAA---KKGLSAQSARNRLAAY--DFRGEDVFKPV-SVLSGGEQSRLRLCMLMDDEINF 467
Cdd:PRK10895 83 LPQeasIFR----RLSVYDNLMAVlqiRDDLSAEQREDRANELmeEFHIEHLRDSMgQSLSGGERRRVEIARALAANPKF 158
|
170 180 190
....*....|....*....|....*....|....
gi 2526491659 468 LILDEPTNHLD----IDSREWIEEAVEAYDGTLL 497
Cdd:PRK10895 159 ILLDEPFAGVDpisvIDIKRIIEHLRDSGLGVLI 192
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
332-521 |
1.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFE-----GISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI---------KTGPQVKEAYL 397
Cdd:PRK13651 5 VKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQI---------------IR------FDHPDWNLVENMM-------AAKKGLSAQSARNRLAAYDfrgEDVFKPVSV--- 446
Cdd:PRK13651 85 EKLviqktrfkkikkikeIRrrvgvvFQFAEYQLFEQTIekdiifgPVSMGVSKEEAKKRAAKYI---ELVGLDESYlqr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 447 ----LSGGEQSRLRLCMLMDDEINFLILDEPTNHLDidsREWIEEAVEAYDG------TLLFVSHDRYFINRFATRIWEL 516
Cdd:PRK13651 162 spfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLD---PQGVKEILEIFDNlnkqgkTIILVTHDLDNVLEWTKRTIFF 238
|
....*
gi 2526491659 517 ADGTI 521
Cdd:PRK13651 239 KDGKI 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
327-524 |
1.62e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMI--VGELYPD---------DGRIKTGPQVKEA 395
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivyNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 396 YLPQIIR--FDHPD---WNLVENMMAAK--KGLSAQSARNRLAAYDFRGEDVFKPVS--------VLSGGEQSRLRLCML 460
Cdd:PRK14239 83 DLRKEIGmvFQQPNpfpMSIYENVVYGLrlKGIKDKQVLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 461 MDDEINFLILDEPTNHLDIDSREWIEEAVEAY--DGTLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
329-477 |
1.67e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPD---DGRIKTGPQVKEAYLPQ------ 399
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRdterag 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 --IIrfdHPDWNLVENMMAAKK-GLSAQSARNRLAAYD---FRGE----------DVFKPVSVLSGGEQSRLRLCMLMDD 463
Cdd:PRK13549 84 iaII---HQELALVKELSVLENiFLGNEITPGGIMDYDamyLRAQkllaqlkldiNPATPVGNLGLGQQQLVEIAKALNK 160
|
170
....*....|....
gi 2526491659 464 EINFLILDEPTNHL 477
Cdd:PRK13549 161 QARLLILDEPTASL 174
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
330-487 |
1.71e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGPQVK-------EAY 396
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAErgvvfqnEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 397 LPqiirfdhpdW-NLVEN------MMAAKKGLSAQSARNRLAAYDFRGEDVfKPVSVLSGGEQSRLRLCMLMDDEINFLI 469
Cdd:PRK11248 82 LP---------WrNVQDNvafglqLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170
....*....|....*...
gi 2526491659 470 LDEPTNHLDIDSREWIEE 487
Cdd:PRK11248 152 LDEPFGALDAFTREQMQT 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-217 |
1.72e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQI----PVYP 79
Cdd:PRK09544 5 VSLENVSVSFG-QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlyldTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 80 agCTVedvlrSAFARLeslaeemraleaRMAAGESD--PAIlkrygtlsERFEAfggydtdvavnkiANGLSIPdsqrsq 157
Cdd:PRK09544 84 --LTV-----NRFLRL------------RPGTKKEDilPAL--------KRVQA-------------GHLIDAP------ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 158 lFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYI----RSFHGTVVTISHD 217
Cdd:PRK09544 118 -MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIdqlrRELDCAVLMVSHD 180
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
333-521 |
1.78e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.75 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-----------------GPQVKE 394
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtraslrrniAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 395 AYL-----PQIIRFDHPDWNLVENMMAAKkglsaqsarnRLAAYDF--RGEDVFKPV-----SVLSGGEQSRLRL--CML 460
Cdd:PRK13657 418 AGLfnrsiEDNIRVGRPDATDEEMRAAAE----------RAQAHDFieRKPDGYDTVvgergRQLSGGERQRLAIarALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 461 MDDEInfLILDEPTNHLDIDSREWIEEAVEAydgtllfVSHDRY-FI-------NRFATRIWELADGTI 521
Cdd:PRK13657 488 KDPPI--LILDEATSALDVETEAKVKAALDE-------LMKGRTtFIiahrlstVRNADRILVFDNGRV 547
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
2.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.05 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgqgrrvglisqipvypa 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 gctvedvlrsafaRLESLAEEmRALEARMAAG----ESDPAIlkrYGTLSERFEAFG----GYDTDVAVNKIANGLSIP- 151
Cdd:PRK13652 64 -------------RGEPITKE-NIREVRKFVGlvfqNPDDQI---FSPTVEQDIAFGpinlGLDEETVAHRVSSALHMLg 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 152 -DSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HG-TVVTISHD 217
Cdd:PRK13652 127 lEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpetYGmTVIFSTHQ 197
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-235 |
2.44e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG--------------RRV 69
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQ---------------IPVYPAGCTVEDVLRsafarleslaeemraleaRMAAGesdpaiLKRYGTLSErfeafgg 134
Cdd:PRK10908 82 GMIFQdhhllmdrtvydnvaIPLIIAGASGDDIRR------------------RVSAA------LDKVGLLDK------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 135 ydtdvavnkiANGLSIpdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTI 214
Cdd:PRK10908 131 ----------AKNFPI----------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTV 190
|
250 260
....*....|....*....|....
gi 2526491659 215 ---SHDRYFLDRTVTRVIEIQDGK 235
Cdd:PRK10908 191 lmaTHDIGLISRRSYRMLTLSDGH 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-235 |
2.58e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.18 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFevGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFK-------ILTGELDYDeGTVVVGQGRRVGLI 72
Cdd:PRK09493 1 MIEFK--NVSKHF--GPTqVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVD-GLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 73 --------SQIPVYPAGCTVEDVlrsAFA--RLESLAEEmralEARMAAGEsdpaILKRYGtLSERFEAFGGydtdvavn 142
Cdd:PRK09493 76 rqeagmvfQQFYLFPHLTALENV---MFGplRVRGASKE----EAEKQARE----LLAKVG-LAERAHHYPS-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 143 kianglsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDlhaTEWLEEYIRSFHG------TVVTISH 216
Cdd:PRK09493 136 ------------------ELSGGQQQRVAIARALAVKPKLMLFDEPTSALD---PELRHEVLKVMQDlaeegmTMVIVTH 194
|
250
....*....|....*....
gi 2526491659 217 DRYFLDRTVTRVIEIQDGK 235
Cdd:PRK09493 195 EIGFAEKVASRLIFIDKGR 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
348-510 |
2.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG-----PQVKEAYLPQIIR-----FDHPDWNLVEN---- 413
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitPETGNKNLKKLRKkvslvFQFPEAQLFENtvlk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 414 --MMAAKK-GLSAQSARNRLAAYDFR---GEDVF-KPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIE 486
Cdd:PRK13641 106 dvEFGPKNfGFSEDEAKEKALKWLKKvglSEDLIsKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170 180
....*....|....*....|....*..
gi 2526491659 487 EAVEAYDG---TLLFVSHDRYFINRFA 510
Cdd:PRK13641 186 QLFKDYQKaghTVILVTHNMDDVAEYA 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-238 |
2.89e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.34 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgrrvglisqipvypaGCTVEDVlrsafarlesl 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID----------------GLNIAKI----------- 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 99 aeEMRALEARMAAGESDPAILKryGTLSERFEAFGGY-DTDV-----------AVNKIANGLsipDSQRSQLFDSLSGGE 166
Cdd:TIGR00957 1354 --GLHDLRFKITIIPQDPVLFS--GSLRMNLDPFSQYsDEEVwwalelahlktFVSALPDKL---DHECAEGGENLSVGQ 1426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS-FHG-TVVTISHdRYFLDRTVTRVIEIQDGK-AEF 238
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqFEDcTVLTIAH-RLNTIMDYTRVIVLDKGEvAEF 1500
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
327-527 |
3.30e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQVK----EAYLPQI- 400
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDIStlkpEIYRQQVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 ----------------------IRFDHPDwnlvENMMAAKkglsaqsarnrLAAYDFRGEDVFKPVSVLSGGEQSRLRLC 458
Cdd:PRK10247 85 ycaqtptlfgdtvydnlifpwqIRNQQPD----PAIFLDD-----------LERFALPDTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 459 MLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDG----TLLFVSHDRYFINRfatriwelADGTITDYPCG 527
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDKDEINH--------ADKVITLQPHA 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
330-386 |
4.27e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 4.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 330 LGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-235 |
4.48e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 56.73 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 26 QVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ---------GRRVGLISQIPVYPAGCTVE---DVLRSAFA 93
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappaDRPVSMLFQENNLFAHLTVEqnvGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 94 RLEslAEEMRALEArmaagesdpaILKRYGtlserfeaFGGYDtdvavnkianglsipdsqrSQLFDSLSGGEKTRVNLG 173
Cdd:cd03298 100 KLT--AEDRQAIEV----------ALARVG--------LAGLE-------------------KRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 174 RLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-241 |
4.70e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.80 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 8 NLVKSFeVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELD------YDEGTVVVGQG-----------RRVG 70
Cdd:PRK14271 26 NLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrYSGDVLLGGRSifnyrdvlefrRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYPAGCTVEDVLRSAFARLESLAEEMRalearmaagesdpailkryGTLSERFEAFGGYDtdvavnkianglsi 150
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFR-------------------GVAQARLTEVGLWD-------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 151 pdSQRSQLFDS---LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHDryfldrtV 225
Cdd:PRK14271 152 --AVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN-------L 222
|
250
....*....|....*.
gi 2526491659 226 TRVIEIQDGKAEFYSG 241
Cdd:PRK14271 223 AQAARISDRAALFFDG 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-235 |
5.44e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGK---NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV-VVGQ-------------- 65
Cdd:PRK10584 7 VEVHHLKKSVGQGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQplhqmdeearaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 66 GRRVGLISQ----IPVYPAgctVEDVLRSAFARLESLAEemralearmaAGESDPAILKRYGtLSERFEafggydtdvav 141
Cdd:PRK10584 87 AKHVGFVFQsfmlIPTLNA---LENVELPALLRGESSRQ----------SRNGAKALLEQLG-LGKRLD----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 142 nkianglsipdsqrsQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYI----RSFHGTVVTISHD 217
Cdd:PRK10584 142 ---------------HLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
250
....*....|....*...
gi 2526491659 218 RYFLDRtVTRVIEIQDGK 235
Cdd:PRK10584 207 LQLAAR-CDRRLRLVNGQ 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-216 |
5.80e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEVGKNV--LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGR------------R 68
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrsK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 69 VGLISQIPVYPAGCTVEDVLRSAFA--RLESLAEEMR-----------ALEARMAAGESDPAILKRYGTLSERFEAFGGY 135
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNIKYSLYSlkDLEALSNYYNedgndsqenknKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 136 DT--DVAVNKIANGL-------SIPDSQRSQL---FDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEY 203
Cdd:PTZ00265 542 QTikDSEVVDVSKKVlihdfvsALPDKYETLVgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*..
gi 2526491659 204 IRSFHGT----VVTISH 216
Cdd:PTZ00265 622 INNLKGNenriTIIIAH 638
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-217 |
6.31e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNV--LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV-----------VVGQGRRVG 70
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgelltaenVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPVYP-AGCTVEDVLrsafarleSLAEEMRALEARMAAGESDPAILkrygtlserfeafggydtdvAVNKIANGLS 149
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDV--------AFGMENQGIPREEMIKRVDEALL--------------------AVNMLDFKTR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 150 IPdsqrsqlfDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRS----FHGTVVTISHD 217
Cdd:PRK13642 137 EP--------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEikekYQLTVLSITHD 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
348-523 |
6.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGP-----QVKEAYLPQI-----IRFDHPDWNLVEN---- 413
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVrkrigMVFQFPESQLFEDtver 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 414 -MMAAKK--GLSAQSARNRlaAYDFRGEDVFkPVSVL-------SGGEQSRLRLC--MLMDDEInfLILDEPTNHLDIDS 481
Cdd:PRK13646 106 eIIFGPKnfKMNLDEVKNY--AHRLLMDLGF-SRDVMsqspfqmSGGQMRKIAIVsiLAMNPDI--IVLDEPTAGLDPQS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 482 R----EWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK13646 181 KrqvmRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
327-521 |
6.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGD-KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIR--- 402
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -----FDHPDWNL------------VENMMAAKKGLS--AQSARNRLAAYDFRGedvfKPVSVLSGGEQSRLRLCMLMDD 463
Cdd:PRK13636 83 svgmvFQDPDNQLfsasvyqdvsfgAVNLKLPEDEVRkrVDNALKRTGIEHLKD----KPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 464 EINFLILDEPTNHLD----IDSREWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-193 |
6.70e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.88 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 3 EIQVNNLVKSFEvGKNV--LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGRR----------V 69
Cdd:PRK11176 341 DIEFRNVTFTYP-GKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLRdytlaslrnqV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 70 GLISQiPVYPAGCTVEDVLrsAFARLESLAEEMRALEARMAagesdpailkrygtlserfeafggYDTDVaVNKIANGLs 149
Cdd:PRK11176 420 ALVSQ-NVHLFNDTIANNI--AYARTEQYSREQIEEAARMA------------------------YAMDF-INKMDNGL- 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526491659 150 ipDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK11176 471 --DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
332-502 |
7.58e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.30 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD-KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGR-----IKTGPQVKeayLPQI----- 400
Cdd:PRK13644 4 LENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvlvsgIDTGDFSK---LQGIrklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRFDHPDWNLV------------ENM----MAAKKGLSAQSARNRLAAYDFRgedvfKPVSvLSGGEQSRLRLCMLMDDE 464
Cdd:PRK13644 81 IVFQNPETQFVgrtveedlafgpENLclppIEIRKRVDRALAEIGLEKYRHR-----SPKT-LSGGQGQCVALAGILTME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2526491659 465 INFLILDEPTNHLDIDSREWIEEAVEAYD---GTLLFVSHD 502
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHN 195
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-217 |
7.60e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.34 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYD---EGTVVVG---------QGRRVGLISQIPVYPAGCT 83
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNgrrltalpaEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLrsAFARLESLAEEMRALEARMAagesdpaiLKRYGtLSERFEAfggydtDVAvnkianglsipdsqrsqlfdSLS 163
Cdd:COG4136 93 VGENL--AFALPPTIGRAQRRARVEQA--------LEEAG-LAGFADR------DPA--------------------TLS 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLD--LHAT--EWLEEYIRSFHGTVVTISHD 217
Cdd:COG4136 136 GGQRARVALLRALLAEPRALLLDEPFSKLDaaLRAQfrEFVFEQIRQRGIPALLVTHD 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
329-516 |
8.02e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-------KTGPQVKE-AYLPQI 400
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRFmAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRFDhPDWNLVENM--MAAKKGLSA-QSARNRLAAYDFRG-EDVFkpVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNH 476
Cdd:PRK13543 91 PGLK-ADLSTLENLhfLCGLHGRRAkQMPGSALAIVGLAGyEDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526491659 477 LDIDSREWIEEAVEAY---DGTLLFVSHDRYFINRFATRIWEL 516
Cdd:PRK13543 168 LDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-189 |
8.63e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.43 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG-------QGRRVgLISQIPVYPAGctvedvlRSA 91
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKI-MREAVAIVPEG-------RRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 92 FARLEslAEEMRALEARMAAGESDPAILKR-YGTLSERFEafggydtdvavnkianglsipdsQRSQLFDSLSGGEKTRV 170
Cdd:PRK11614 92 FSRMT--VEENLAMGGFFAERDQFQERIKWvYELFPRLHE-----------------------RRIQRAGTMSGGEQQML 146
|
170
....*....|....*....
gi 2526491659 171 NLGRLILEDTDILLLDEPT 189
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPS 165
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-488 |
8.74e-09 |
|
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: 57.17 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVkeAYLPQIirfdhpDW----NLVENMMAakkGLSA 423
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI--SFSSQF------SWimpgTIKENIIF---GVSY 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 424 QSARNR-----------LAAYDFRGEDVFKPVSV-LSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEA 488
Cdd:cd03291 125 DEYRYKsvvkacqleedITKFPEKDNTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
9.35e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.68 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ---------GRRVGL 71
Cdd:PRK11264 1 MSAIEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQI-----------PVYPAGCTVEDVLRSAFarleslaeeMRALEARMAAGESDPAILKRYGtLSERFEAFggydtdva 140
Cdd:PRK11264 80 IRQLrqhvgfvfqnfNLFPHRTVLENIIEGPV---------IVKGEPKEEATARARELLAKVG-LAGKETSY-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 141 vnkianglsipdSQRsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISHD 217
Cdd:PRK11264 142 ------------PRR------LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHE 203
|
250
....*....|....*...
gi 2526491659 218 RYFLDRTVTRVIEIQDGK 235
Cdd:PRK11264 204 MSFARDVADRAIFMDQGR 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
340-501 |
1.00e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 340 GDKhLFEGISLKVEGGERIALIGDNGTGKSTLIKmIVGELYPD-DGRIKTGPQVKEAYLPQ------------IIrfdHP 406
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVyGGRLTKPAKGKLFYVPQrpymtlgtlrdqII---YP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 407 DwnLVENMMaaKKGLSAQSARNRLAAYDF-----RG---EDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLD 478
Cdd:TIGR00954 539 D--SSEDMK--RRGLSDKDLEQILDNVQLthileREggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|...
gi 2526491659 479 IDSREWIEEAVEAYDGTLLFVSH 501
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-235 |
1.02e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGEL--DYDEGTVVVGQG------------RRVGLISQIPVYP-AG 81
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpDDNPNSKITVDGitltaktvwdirEKVGIVFQNPDNQfVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 CTVEDVLrsAFArleslaeemraLEARmaaGESDPAILKrygtlserfeafggydtdvAVNKIANGLSIPDSQRSQLfDS 161
Cdd:PRK13640 100 ATVGDDV--AFG-----------LENR---AVPRPEMIK-------------------IVRDVLADVGMLDYIDSEP-AN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISHDryfLDRTV--TRVIEIQDGK 235
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD---IDEANmaDQVLVLDDGK 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-236 |
1.24e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.92 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 24 TFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVG--LISQIPV---------YPAgCTVEDVLrsAF 92
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTalPPAERPVsmlfqennlFPH-LTVAQNI--GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 93 ARLESL---AEEMRALEArmaagesdpaILKRYGtlserFEAFGGYdtdvavnkianglsipdsqrsqLFDSLSGGEKTR 169
Cdd:COG3840 95 GLRPGLkltAEQRAQVEQ----------ALERVG-----LAGLLDR----------------------LPGQLSGGQRQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 170 VNLGRLILEDTDILLLDEPTNHLD-------LHateWLEEYIRSFHGTVVTISHDryfLD---RTVTRVIEIQDGKA 236
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDpalrqemLD---LVDELCRERGLTVLMVTHD---PEdaaRIADRVLLVADGRI 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-194 |
1.40e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVV-----VGQGRRVGLISQIP-- 76
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqpTRQALQKNLVAYVPqs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 -----VYPAgcTVEDVLrsAFARLESLAEEMRALEARMAAGEsdpAILKRYGTLSERFEAFGgydtdvavnkianglsip 151
Cdd:PRK15056 87 eevdwSFPV--LVEDVV--MMGRYGHMGWLRRAKKRDRQIVT---AALARVDMVEFRHRQIG------------------ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526491659 152 dsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL 194
Cdd:PRK15056 142 ---------ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
329-523 |
1.42e-08 |
|
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: 55.90 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDK----HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKtgpqVKEAYLPQI---- 400
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR----LAGQDLFALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 ---IRFDH-----------PDWNLVENMM----------AAKK--------GLSAqsarnRLAAYdfrgedvfkPvSVLS 448
Cdd:COG4181 84 rarLRARHvgfvfqsfqllPTLTALENVMlplelagrrdARARarallervGLGH-----RLDHY---------P-AQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 449 GGEQSRLRL--CMLMDDEInfLILDEPTNHLDIDSREWIEEAVEA----YDGTLLFVSHDRYFINRfATRIWELADGTIT 522
Cdd:COG4181 149 GGEQQRVALarAFATEPAI--LFADEPTGNLDAATGEQIIDLLFElnreRGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
.
gi 2526491659 523 D 523
Cdd:COG4181 226 E 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
323-523 |
1.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 323 EFHGDEVLGirNVSKSYGDKHLFE-----GISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYL 397
Cdd:PRK13645 2 DFSKDIILD--NVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQI-----------IRFDHPDWNLVENMMAAKKGLS-AQSARNRLAAYDfRGEDVFKPVSV-----------LSGGEQSR 454
Cdd:PRK13645 80 KKIkevkrlrkeigLVFQFPEYQLFQETIEKDIAFGpVNLGENKQEAYK-KVPELLKLVQLpedyvkrspfeLSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 455 LRLCMLMDDEINFLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-501 |
1.59e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQvdQGERVGLLGRNGAGKTTLFKILTGELdydegtvVVGQGRRVglisqipvypagCTVEDVLRSAFARLESLA 99
Cdd:PRK10938 21 LPSLTLN--AGDSWAFVGANGSGKSALARALAGEL-------PLLSGERQ------------SQFSHITRLSFEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 100 EEmralearmaagesdpaILKRYGT--LSERFEAFGGYDTDVavnkIANGLSipDSQRSQL--------------FDSLS 163
Cdd:PRK10938 80 SD----------------EWQRNNTdmLSPGEDDTGRTTAEI----IQDEVK--DPARCEQlaqqfgitalldrrFKYLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTIshdryfldrtVTRVIEIQDgkaeFYS 240
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLV----------LNRFDEIPD----FVQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 241 gnysFYAVEKERRYQER-MKQYEKEQAKIAQLeKAAEQLRVWAFMGMDKTyrraismerriermrtTAKPTKARKmDARF 319
Cdd:PRK10938 204 ----FAGVLADCTLAETgEREEILQQALVAQL-AHSEQLEGVQLPEPDEP----------------SARHALPAN-EPRI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 320 SsaefhgdevlgIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVG---ELYPDD----GR------- 385
Cdd:PRK10938 262 V-----------LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpQGYSNDltlfGRrrgsget 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 386 ---IKTgpqvKEAYLPQIIRFDHPDWNLVENMMaakkgLS----------AQSARNR------LAAYDFRGEDVFKPVSV 446
Cdd:PRK10938 331 iwdIKK----HIGYVSSSLHLDYRVSTSVRNVI-----LSgffdsigiyqAVSDRQQklaqqwLDILGIDKRTADAPFHS 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 447 LSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSH 501
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQlvrrFVDVLISEGETQLLFVSH 460
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-251 |
1.60e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFK------------ILTGELDYDEGTV------VVGQ 65
Cdd:PRK14239 6 LQVSDLSVYYN-KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYNGHNIysprtdTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 66 GRRVGLISQIP-VYPagctvedvlrsaFARLESLAEEMRAlearmaAGESDPAILkrygtlserfeafggydtDVAVNKI 144
Cdd:PRK14239 85 RKEIGMVFQQPnPFP------------MSIYENVVYGLRL------KGIKDKQVL------------------DEAVEKS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 145 ANGLSIPDSQRSQLFDS---LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEyirsfhgTVVTISHDRYFL 221
Cdd:PRK14239 129 LKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEE-------TLLGLKDDYTML 201
|
250 260 270
....*....|....*....|....*....|....
gi 2526491659 222 drTVTRVIE----IQDGKAEFYSGNYSFYAVEKE 251
Cdd:PRK14239 202 --LVTRSMQqasrISDRTGFFLDGDLIEYNDTKQ 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-198 |
1.73e-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: 57.52 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG-RRVGLIS---QIPVYPAGcTV--EDVLRS- 90
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDiRDVTQASlraAIGIVPQD-TVlfNDTIAYn 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 91 -AFARLESLAEEMRAlEARMAAgeSDPAILKrygtLSErfeafgGYDTDVAvnkiANGLSipdsqrsqlfdsLSGGEKTR 169
Cdd:COG5265 452 iAYGRPDASEEEVEA-AARAAQ--IHDFIES----LPD------GYDTRVG----ERGLK------------LSGGEKQR 502
|
170 180
....*....|....*....|....*....
gi 2526491659 170 VNLGRLILEDTDILLLDEPTNHLDLHaTE 198
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSR-TE 530
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
327-523 |
2.01e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDD---GRIKT-GPQVKEAYLPQI 400
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVdGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 -----IRFDHPDWNLV------------ENMMAAKKGLS--AQSARNRLAAYDFRGEDvfkPvSVLSGGEQSRLRLCMLM 461
Cdd:PRK13640 83 rekvgIVFQNPDNQFVgatvgddvafglENRAVPRPEMIkiVRDVLADVGMLDYIDSE---P-ANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 462 DDEINFLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSHDryfINR--FATRIWELADGTITD 523
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEqilkLIRKLKKKNNLTVISITHD---IDEanMADQVLVLDDGKLLA 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-524 |
2.02e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 334 NVSKSY---GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMI--VGELYpdDGRIKTGPQV----KEAYLPQIIR-- 402
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIY--DSKIKVDGKVlyfgKDIFQIDAIKlr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ------FDHPD----WNLVENMMAAKK--GLSAQSARNRLAAYDFRGEDVFK--------PVSVLSGGEQSRLRLCMLMD 462
Cdd:PRK14246 90 kevgmvFQQPNpfphLSIYDNIAYPLKshGIKEKREIKKIVEECLRKVGLWKevydrlnsPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 463 DEINFLILDEPTNHLDIDSREWIEEAVEAYDG--TLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-232 |
2.05e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVvvgqgrrvglisQIPVYPAGctvedvlRSAFARLESL 98
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI------------QIDGKTAT-------RGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 99 AEEMRALEARMAAGESDPAILKRYGTLSERFEafggydtdvavnkiANGLSIPD--SQRSQLFDSLSGGEKTRVNLGRLI 176
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLCGLHGRRAKQMP--------------GSALAIVGlaGYEDTLVRQLSAGQKKRLALARLW 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 177 LEDTDILLLDEPTNHLDLHA----TEWLEEYIRSFHGTVVTiSHDRYFLDRTVTRVIEIQ 232
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDLEGitlvNRMISAHLRGGGAALVT-THGAYAAPPVRTRMLTLE 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
329-389 |
2.08e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 2.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG 389
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-217 |
2.09e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV------VVGQGRRVGLISQIP- 76
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkpVEGPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 VYPAGCTVEDVlrsAFA-RLESLAEEMRALEARmaagesdpAILKRYGtlserFEAFGgydtdvavnkianglsipdsqr 155
Cdd:PRK11248 81 LLPWRNVQDNV---AFGlQLAGVEKMQRLEIAH--------QMLKKVG-----LEGAE---------------------- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 156 SQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEE-YIRSFHGT---VVTISHD 217
Cdd:PRK11248 123 KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTlLLKLWQETgkqVLLITHD 188
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
332-502 |
2.33e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI----KTGPQVKEAYLPQIIR----- 402
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgENIPAMSRSRLYTVRKrmsml 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ------------FDHPDWNLVENMMAAKKGLSAqSARNRLAAYDFRGEDVFKPvSVLSGGEQSRLRLCMLMDDEINFLIL 470
Cdd:PRK11831 90 fqsgalftdmnvFDNVAYPLREHTQLPAPLLHS-TVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 2526491659 471 DEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHD 502
Cdd:PRK11831 168 DEPFVGQDPITMgvlvKLISELNSALGVTCVVVSHD 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-235 |
2.46e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.35 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQvnNLVKSFEVGK---NVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQG---------- 66
Cdd:PRK11153 1 MIELK--NISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQDltalsekelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 ---RRVGLISQIPVYPAGCTVED-VlrsAFArLEslaeemralearmAAGESDPAILKRYGTLSERFeafggydtdvavn 142
Cdd:PRK11153 79 karRQIGMIFQHFNLLSSRTVFDnV---ALP-LE-------------LAGTPKAEIKARVTELLELV------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 143 kianGLS-IPDSQRSQlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVTISHD 217
Cdd:PRK11153 129 ----GLSdKADRYPAQ----LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINRELGLTIVLITHE 200
|
250
....*....|....*...
gi 2526491659 218 RYFLDRTVTRVIEIQDGK 235
Cdd:PRK11153 201 MDVVKRICDRVAVIDAGR 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
333-501 |
2.50e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSY---GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI----KTGPQVKEAYLPQIIRF-- 403
Cdd:TIGR00958 482 QDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgVPLVQYDHHYLHRQVALvg 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 -------------------DHPDwnlvENMMAAkkglsAQSArnrlAAYDFRGE-------DVFKPVSVLSGGEQSRLRL 457
Cdd:TIGR00958 562 qepvlfsgsvreniaygltDTPD----EEIMAA-----AKAA----NAHDFIMEfpngydtEVGEKGSQLSGGQKQRIAI 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2526491659 458 CMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDGTLLFVSH 501
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-52 |
3.10e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 3.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTG 52
Cdd:PRK13549 6 LEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-235 |
3.13e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 6 VNNLVKSFE-VGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGL-ISQIPVYPAGCT 83
Cdd:TIGR01257 931 VKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-GKDIETnLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLrsaFARLeSLAEEMrALEARMAAGESDPAILKRYGTLSErfeafggydtdvavnkiaNGLSipdSQRSQLFDSLS 163
Cdd:TIGR01257 1010 QHNIL---FHHL-TVAEHI-LFYAQLKGRSWEEAQLEMEAMLED------------------TGLH---HKRNEEAQDLS 1063
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:TIGR01257 1064 GGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
329-482 |
3.52e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------------KTGPQVke 394
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmadarhrrAVCPRI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 395 AYLPQII-RFDHPDWNLVENM--MAAKKGLSAQSARNRLAA-------YDFRGedvfKPVSVLSGGEQSRLRLC-MLMDD 463
Cdd:NF033858 79 AYMPQGLgKNLYPTLSVFENLdfFGRLFGQDAAERRRRIDEllratglAPFAD----RPAGKLSGGMKQKLGLCcALIHD 154
|
170
....*....|....*....
gi 2526491659 464 EiNFLILDEPTNHLDIDSR 482
Cdd:NF033858 155 P-DLLILDEPTTGVDPLSR 172
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-235 |
3.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.09 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKN-----VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ------------G 66
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdiR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 67 RRVGLISQIPVYPAGCTV--EDVlrsAFARlESLAEEmrALEARMAAGESdpaiLKRYGTLSERfeafggydtdvavnKI 144
Cdd:PRK13633 85 NKAGMVFQNPDNQIVATIveEDV---AFGP-ENLGIP--PEEIRERVDES----LKKVGMYEYR--------------RH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 145 ANGLsipdsqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHdryF 220
Cdd:PRK13633 141 APHL-------------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---Y 204
|
250
....*....|....*..
gi 2526491659 221 LDRTVT--RVIEIQDGK 235
Cdd:PRK13633 205 MEEAVEadRIIVMDSGK 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
332-386 |
3.84e-08 |
|
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: 54.51 E-value: 3.84e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 332 IRNVSKSYGDK----HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV 62
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-501 |
4.04e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.53 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMI--VGELYPD---------DGR-------IKTGP 390
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvsgevylDGQdifkmdvIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 391 QVKEAY-LPQIIrfdhPDWNLVEN---------MMAAKKGLSA------------QSARNRLAAydfrgedvfkPVSVLS 448
Cdd:PRK14247 83 RVQMVFqIPNPI----PNLSIFENvalglklnrLVKSKKELQErvrwalekaqlwDEVKDRLDA----------PAGKLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 449 GGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAY--DGTLLFVSH 501
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
330-521 |
4.11e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSY--GDKHL--FEGISLKVEGGERIALIGDNGTGKSTLIKmIVGEL-YPDDGRIKTGPQ----VKEAYLPQI 400
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IR----FDHPDWNLVENMMAAKK--------GLSAQSARNRLAAYDFR---GEDVFKPVSVLSGGEQSRLRLCMLMDDEI 465
Cdd:PRK10535 84 RRehfgFIFQRYHLLSHLTAAQNvevpavyaGLERKQRLLRAQELLQRlglEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 466 NFLILDEPTNHLDIDSRE---WIEEAVEAYDGTLLFVSHDRYFINRfATRIWELADGTI 521
Cdd:PRK10535 164 QVILADEPTGALDSHSGEevmAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
330-399 |
4.16e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 54.01 E-value: 4.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 330 LGIRNVSKSYGDKH-----LFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVkeAYLPQ 399
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQ 73
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
336-478 |
4.49e-08 |
|
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: 53.71 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 336 SKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGEL--YPDDGRIK-TGPQVKEAYLPQIIRF----D--HP 406
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLiNGRPLDKRSFRKIIGYvpqdDilHP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 407 DWNLVENMM-AAKkglsaqsarnrlaaydFRGedvfkpvsvLSGGEQSRLRLC--MLMDDEInfLILDEPTNHLD 478
Cdd:cd03213 96 TLTVRETLMfAAK----------------LRG---------LSGGERKRVSIAleLVSNPSL--LFLDEPTSGLD 143
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
330-501 |
4.64e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSY-GDKHLfEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ------VKEAyLPQIIR 402
Cdd:PRK11288 5 LSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasTTAA-LAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 FDHPDWNLVENMMAA---------------KKGLSAQSARNRLAAYdfrGEDV--FKPVSVLSGGEQSRLRLC-MLMDDE 464
Cdd:PRK11288 83 IIYQELHLVPEMTVAenlylgqlphkggivNRRLLNYEAREQLEHL---GVDIdpDTPLKYLSIGQRQMVEIAkALARNA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2526491659 465 --INFlilDEPTNHLdiDSREwIE------EAVEAYDGTLLFVSH 501
Cdd:PRK11288 160 rvIAF---DEPTSSL--SARE-IEqlfrviRELRAEGRVILYVSH 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
329-386 |
4.69e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.34 E-value: 4.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-510 |
4.86e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMI--VGELYPD---DGRIKTGPQ------VKEAYLPQI 400
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFFNQniyerrVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 IRFDHPDWNLV-----ENMMAAKKGLS----------AQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEI 465
Cdd:PRK14258 90 VSMVHPKPNLFpmsvyDNVAYGVKIVGwrpkleiddiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526491659 466 NFLILDEPTNHLDIDSREWIEEAVEAY----DGTLLFVSHDRYFINRFA 510
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLS 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-194 |
4.94e-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: 56.46 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVvvGQGRRVGLISQIPVYPAGCTVEDVLrsafarlesl 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGRISFSPQTSWIMPGTIKDNII---------- 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 99 aeemralearmaagesdpailkrYGTLSERFEafggYDTDVAVNKIANGLSI-PDSQRSQLFD---SLSGGEKTRVNLGR 174
Cdd:TIGR01271 509 -----------------------FGLSYDEYR----YTSVIKACQLEEDIALfPEKDKTVLGEggiTLSGGQRARISLAR 561
|
170 180
....*....|....*....|
gi 2526491659 175 LILEDTDILLLDEPTNHLDL 194
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDV 581
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
329-521 |
5.08e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIK----MIVGELYPDDGRIKTGPQV-KEAYLPQIIR- 402
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVqREGRLARDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 ------FDHPDWNLV------ENMMAAKKG-----------LSAQSARNRLAAYDFRGEDVF--KPVSVLSGGEQSRLRL 457
Cdd:PRK09984 84 srantgYIFQQFNLVnrlsvlENVLIGALGstpfwrtcfswFTREQKQRALQALTRVGMVHFahQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 458 CMLMDDEINFLILDEPTNHLDIDSREWIEEA---VEAYDGTLLFVS-HDRYFINRFATRIWELADGTI 521
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTlrdINQNDGITVVVTlHQVDYALRYCERIVALRQGHV 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-196 |
5.15e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGLISQIPVYPAG---CTvEDVLRSAF 92
Cdd:PRK11288 265 GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD-GKPIDIRSPRDAIRAGimlCP-EDRKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 93 ARLESLAEEMrALEARmaagesdPAILKRYGTLSERFEAfggydtDVAVNKIANgLSIPDSQRSQLFDSLSGGEKTRVNL 172
Cdd:PRK11288 343 IPVHSVADNI-NISAR-------RHHLRAGCLINNRWEA------ENADRFIRS-LNIKTPSREQLIMNLSGGNQQKAIL 407
|
170 180
....*....|....*....|....
gi 2526491659 173 GRLILEDTDILLLDEPTNHLDLHA 196
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGA 431
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-193 |
5.80e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.82 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGE----LDYDeGTVVVgQGRRVGLiSQIPVypagctvedvlRSAF 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRspkgVKGS-GSVLL-NGMPIDA-KEMRA-----------ISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 93 ARLESL------AEEMRALEARMAagesdpaiLKRYGTLSERFEAFGGYDTDVAVNKIANGL-SIPDSQRSqlfdsLSGG 165
Cdd:TIGR00955 104 VQQDDLfiptltVREHLMFQAHLR--------MPRRVTKKEKRERVDEVLQALGLRKCANTRiGVPGRVKG-----LSGG 170
|
170 180
....*....|....*....|....*...
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:TIGR00955 171 ERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
328-521 |
6.53e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.94 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 328 EVLGIRNVSkSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPddGRIKTGPQVK---EAYLPQIIRFD 404
Cdd:PRK10418 3 QQIELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLldgKPVAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 H---------PDWNLVENMMA-AKKGLSA---QSARNRL-AAYDFRG-EDVFKPVSV----LSGGEQSRLRLCMLMDDEI 465
Cdd:PRK10418 80 KiatimqnprSAFNPLHTMHThARETCLAlgkPADDATLtAALEAVGlENAARVLKLypfeMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 466 NFLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQarilDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-218 |
6.76e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLIS------------QIPVYpAGCT 83
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDISTLKpeiyrqqvsycaQTPTL-FGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRSAFaRLESLAEEMRALEARMAagesdpailkrygtlseRFEafggydtdvavnkianglsIPDSQRSQLFDSLS 163
Cdd:PRK10247 97 VYDNLIFPW-QIRNQQPDPAIFLDDLE-----------------RFA-------------------LPDTILTKNIAELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLH----ATEWLEEYIRSFHGTVVTISHDR 218
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDK 198
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-235 |
6.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG----------QGRR--VGL 71
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklQGIRklVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 72 ISQIP-VYPAGCTVEDVLrsAFARlESLAeeMRALEARmaagesdpailKRygtlserfeafggydTDVAVNKIanGLsi 150
Cdd:PRK13644 82 VFQNPeTQFVGRTVEEDL--AFGP-ENLC--LPPIEIR-----------KR---------------VDRALAEI--GL-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 151 pDSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFH---GTVVTISHDRYFLdRTVTR 227
Cdd:PRK13644 127 -EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEEL-HDADR 204
|
....*...
gi 2526491659 228 VIEIQDGK 235
Cdd:PRK13644 205 IIVMDRGK 212
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
355-513 |
7.14e-08 |
|
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: 51.99 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 355 GERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTgpqvkeaylpqiirfdhpdwnlvenmmaakkgLSAQSARNRLAAyD 434
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------IDGEDILEEVLD-Q 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 435 FRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEA---------YDGTLLFVSHDRYF 505
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllkseKNLTVILTTNDEKD 128
|
....*...
gi 2526491659 506 INRFATRI 513
Cdd:smart00382 129 LGPALLRR 136
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-235 |
7.21e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 2 IEIQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGrrvglisqipvyPAG 81
Cdd:PRK11247 11 TPLLLNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA------------PLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 CTVEDVlRSAF--ARL---ESLAEEM----------RALEARMAAGESD-----PAilkrygtlserfeafggydtdvav 141
Cdd:PRK11247 78 EAREDT-RLMFqdARLlpwKKVIDNVglglkgqwrdAALQALAAVGLADranewPA------------------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 142 nkianglsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD-LHATEwLEEYIRSF---HG-TVVTISH 216
Cdd:PRK11247 133 -------------------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRIE-MQDLIESLwqqHGfTVLLVTH 192
|
250 260
....*....|....*....|..
gi 2526491659 217 DryfLDRTVT---RVIEIQDGK 235
Cdd:PRK11247 193 D---VSEAVAmadRVLLIEEGK 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
332-521 |
7.36e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLK-----VEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTG-----PQVKEAYLPQI- 400
Cdd:PRK13634 5 FQKVEHRYQYKTPFERRALYdvnvsIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitAGKKNKKLKPLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 ----IRFDHPDWNLVENMMA-------AKKGLSAQSARnRLAAYDFR----GEDVFK--PVSvLSGGEQSRLRLC--MLM 461
Cdd:PRK13634 85 kkvgIVFQFPEHQLFEETVEkdicfgpMNFGVSEEDAK-QKAREMIElvglPEELLArsPFE-LSGGQMRRVAIAgvLAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 462 DDEInfLILDEPTNHLDIDSREWIEEAVEAY----DGTLLFVSHDRYFINRFATRIWELADGTI 521
Cdd:PRK13634 163 EPEV--LVLDEPTAGLDPKGRKEMMEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
326-485 |
8.27e-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: 52.43 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 326 GDEVLGIRNVSKsygdKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK------TGPQVKEA---- 395
Cdd:cd03215 1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgkpvTRRSPRDAirag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 396 --YLPQIiRFDH---PDWNLVENMMAAkkglsaqsarnrlaaydfrgedvfkpvSVLSGGEQSRLRLCMLMDDEINFLIL 470
Cdd:cd03215 77 iaYVPED-RKREglvLDLSVAENIALS---------------------------SLLSGGNQQKVVLARWLARDPRVLIL 128
|
170
....*....|....*
gi 2526491659 471 DEPTNHLDIDSREWI 485
Cdd:cd03215 129 DEPTRGVDVGAKAEI 143
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-523 |
9.01e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 53.64 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 333 RNVSKSYG--DKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-----KTGPQVKEAYLPQI----- 400
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghDLALADPAWLRRQVgvvlq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 401 --IRFDHpdwNLVENMMAAKKGLSAQS--ARNRLA-AYDF-----RGED--VFKPVSVLSGGEQSRLRLCMLMDDEINFL 468
Cdd:cd03252 84 enVLFNR---SIRDNIALADPGMSMERviEAAKLAgAHDFiselpEGYDtiVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 469 ILDEPTNHLDIDSREWIEEAVEAY-DG-TLLFVSHdRYFINRFATRIWELADGTITD 523
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAH-RLSTVKNADRIIVMEKGRIVE 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-218 |
9.36e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.34 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 8 NLVKSFevGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQgrrvglisqipvypagctvED 86
Cdd:PRK11432 11 NITKRF--GSNtVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG-------------------ED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 87 VL-RSAFARLESLAEEMRALEARMAAGESDPAILKRYGTLSERFEAfggydtdvavnKIANGLSIPDSQ--RSQLFDSLS 163
Cdd:PRK11432 70 VThRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQ-----------RVKEALELVDLAgfEDRYVDQIS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 164 GGEKTRVNLGR-LILEdTDILLLDEPTNHLDLHATEWLEEYIR----SFHGTVVTISHDR 218
Cdd:PRK11432 139 GGQQQRVALARaLILK-PKVLLFDEPLSNLDANLRRSMREKIRelqqQFNITSLYVTHDQ 197
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-235 |
9.69e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.43 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 24 TFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGRRVGLISQIPVypAGCTVEDVLrsaFARLeslaeem 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPV--SMLFQENNL---FSHL------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 103 rALEARMAAGeSDPAiLKrygtLSErfeafggyDTDVAVNKIANGLSIpDSQRSQLFDSLSGGEKTRVNLGRLILEDTDI 182
Cdd:PRK10771 87 -TVAQNIGLG-LNPG-LK----LNA--------AQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 183 LLLDEPTNHLD--LHAT--EWLEEYIRSFHGTVVTISHDryfLD---RTVTRVIEIQDGK 235
Cdd:PRK10771 151 LLLDEPFSALDpaLRQEmlTLVSQVCQERQLTLLMVSHS---LEdaaRIAPRSLVVADGR 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-217 |
1.20e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 52.05 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 5 QVNNLVksfevGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVglisqipvypAGCTV 84
Cdd:cd03215 6 EVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-GKPV----------TRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVLRSAFARLeslAEEmraleaRmaagesdpailKRYGTLSERfeafggydtDVAVNkiangLSIPDSqrsqlfdsLSG 164
Cdd:cd03215 70 RDAIRAGIAYV---PED------R-----------KREGLVLDL---------SVAEN-----IALSSL--------LSG 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 165 GEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HGT-VVTISHD 217
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGKaVLLISSE 163
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
329-474 |
1.61e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQVKEAYLPQIIRFD--- 404
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfDGKDITDWQTAKIMREAvai 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 HPDWNLVENMMAAKKGLSAQSARNRLAAYDFRGEDVF-----------KPVSVLSGGEQSRLRLCMLMDDEINFLILDEP 473
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYelfprlherriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
.
gi 2526491659 474 T 474
Cdd:PRK11614 165 S 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-189 |
1.67e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 21 DGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV-VVGQG---------RRVGLISQipvypagctvedvlrs 90
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPvdagdiatrRRVGYMSQ---------------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 91 AFarleSLAEEM--R---ALEAR---MAAGESDPAIlkryGTLSERFEAfggydTDVAvnkianglsipdsqrSQLFDSL 162
Cdd:NF033858 347 AF----SLYGELtvRqnlELHARlfhLPAAEIAARV----AEMLERFDL-----ADVA---------------DALPDSL 398
|
170 180
....*....|....*....|....*..
gi 2526491659 163 SGGEKTRVNLGRLILEDTDILLLDEPT 189
Cdd:NF033858 399 PLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-247 |
1.73e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqgRRVGLISQIPvYPAGCTVED-VLRSAFARL 95
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--RSIAYVPQQA-WIMNATVRGnILFFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 96 ESLAEEMRALEArmaagESDPAILKrygtlserfeafGGYDTDVAVNKIanglsipdsqrsqlfdSLSGGEKTRVNLGRL 175
Cdd:PTZ00243 750 ARLADAVRVSQL-----EADLAQLG------------GGLETEIGEKGV----------------NLSGGQKARVSLARA 796
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 176 ILEDTDILLLDEPTNHLDLHATEWL-EEYIR-SFHG-TVVTISHDRYFLDRTvTRVIEIQDGKAEFySGNYSFYA 247
Cdd:PTZ00243 797 VYANRDVYLLDDPLSALDAHVGERVvEECFLgALAGkTRVLATHQVHVVPRA-DYVVALGDGRVEF-SGSSADFM 869
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
338-521 |
1.81e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.08 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 338 SYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELyPDDGRIK-TGPQVKEAYLPQIIRfdHPDW-------- 408
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKiNGIELRELDPESWRK--HLSWvgqnpqlp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 409 --NLVENMMAAKKGLSAQSARNRLA---AYDF-----RGEDVfkPVS----VLSGGEQSRLRLCMLMDDEINFLILDEPT 474
Cdd:PRK11174 436 hgTLRDNVLLGNPDASDEQLQQALEnawVSEFlpllpQGLDT--PIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2526491659 475 NHLDIDSREWIEEAVEAY--DGTLLFVSHDRYFINRFATrIWELADGTI 521
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQWDQ-IWVMQDGQI 561
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
332-478 |
2.15e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI---------KTGPQVKE-AYLPQII 401
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfSKTPSDKAiRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 RFDHPDWNL------VENMMAAKK---GLSAQSARN-------RLAAYDFrgEDVFkPVSvLSGGEQSRL---RLCMlMD 462
Cdd:PRK11124 85 GMVFQQYNLwphltvQQNLIEAPCrvlGLSKDQALAraeklleRLRLKPY--ADRF-PLH-LSGGQQQRVaiaRALM-ME 159
|
170
....*....|....*.
gi 2526491659 463 DEInfLILDEPTNHLD 478
Cdd:PRK11124 160 PQV--LLFDEPTAALD 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-217 |
2.30e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.45 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGR-----------RVGLISQIPVYP-AGCTVE-D 86
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklrkHIGIVFQNPDNQfVGSIVKyD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 87 VlrsAFArleslaeemraLEARMAAGESDPAILKRygTLSErfeafggydtdvaVNKIANGLSIPDSqrsqlfdsLSGGE 166
Cdd:PRK13648 105 V---AFG-----------LENHAVPYDEMHRRVSE--ALKQ-------------VDMLERADYEPNA--------LSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF----HGTVVTISHD 217
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHD 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-218 |
2.79e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGrrvglISQIPVYpagc 82
Cdd:PRK11607 20 LEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVD-----LSHVPPY---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 83 tvedvlrsafARLESLAEEMRALEARMAAgesdpailkrygtlsERFEAFGGYDTDVAVNKIANG----LSIPDSQR--S 156
Cdd:PRK11607 90 ----------QRPINMMFQSYALFPHMTV---------------EQNIAFGLKQDKLPKAEIASRvnemLGLVHMQEfaK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 157 QLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD--LHATEWLE--EYIRSFHGTVVTISHDR 218
Cdd:PRK11607 145 RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-198 |
2.95e-07 |
|
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: 52.55 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 15 VGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGtvVVGQGRRVGLISQIPVYPAGCTVEDVLRSAFA- 93
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHSGRISFSSQFSWIMPGTIKENIIFGVSYd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 94 --RLESLAEEMRALEARMAAGESDPAILKRYGTlserfeafggydtdvavnkianglsipdsqrsqlfdSLSGGEKTRVN 171
Cdd:cd03291 126 eyRYKSVVKACQLEEDITKFPEKDNTVLGEGGI------------------------------------TLSGGQRARIS 169
|
170 180
....*....|....*....|....*..
gi 2526491659 172 LGRLILEDTDILLLDEPTNHLDLhATE 198
Cdd:cd03291 170 LARAVYKDADLYLLDSPFGYLDV-FTE 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-482 |
2.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEG-----ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQV-----KEAYLPQII 401
Cdd:PRK13649 5 LQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 R-----FDHPDWNLVENMMAAKKGLSAQS-----------ARNRLA----AYDFRGEDVFKpvsvLSGGEQSRLRLCMLM 461
Cdd:PRK13649 85 KkvglvFQFPESQLFEETVLKDVAFGPQNfgvsqeeaealAREKLAlvgiSESLFEKNPFE----LSGGQMRRVAIAGIL 160
|
170 180
....*....|....*....|.
gi 2526491659 462 DDEINFLILDEPTNHLDIDSR 482
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGR 181
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
3.18e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.17 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEVG---KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRV-------G 70
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD-GVPVtgpgadrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQI-PVYPAGCTVEDVlrsAFA-RLESLAEEMRALEARmaagesdpAILKRYGtlserfeafggydtdvavnkiangl 148
Cdd:COG4525 80 VVFQKdALLPWLNVLDNV---AFGlRLRGVPKAERRARAE--------ELLALVG------------------------- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 149 sIPDSQRSQLFdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYI----RSFHGTVVTISHD 217
Cdd:COG4525 124 -LADFARRRIW-QLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHS 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-64 |
3.33e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 3.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 7 NNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVG 64
Cdd:PRK11288 8 DGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID 64
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-216 |
3.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTT----LFKIL---TGEL---DYDEGTVVVGQGRRVglISQIPVYPagctvedVL 88
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVeleKGRImidDCDVAKFGLTDLRRV--LSIIPQSP-------VL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 89 RSAFAR--LESLAEEMRAlearmaagesdpailkrygtlsERFEAFGGYDTDVAVNKIANGLsipDSQRSQLFDSLSGGE 166
Cdd:PLN03232 1322 FSGTVRfnIDPFSEHNDA----------------------DLWEALERAHIKDVIDRNPFGL---DAEVSEGGENFSVGQ 1376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 167 KTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIR-SFHG-TVVTISH 216
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIReEFKScTMLVIAH 1428
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
327-502 |
3.89e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.06 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSY-GDKHL-FEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-----KTGPQVKEAYLPQ 399
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 I-IRFDHPDWNLVENMMAAKkglSAQSARNRLAAYDFRGEDVFKPVS-------------VLSGGEQSRLRLCMLMDDEI 465
Cdd:PRK13648 85 IgIVFQNPDNQFVGSIVKYD---VAFGLENHAVPYDEMHRRVSEALKqvdmleradyepnALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2526491659 466 NFLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSHD 502
Cdd:PRK13648 162 SVIILDEATSMLDPDARQnlldLVRKVKSEHNITIISITHD 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-228 |
4.03e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFE-VGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIPVYPAGC 82
Cdd:TIGR01257 1938 LRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 83 TVEDVLRSAFARLESLaeemrALEARMAagesdpailkryGTLSERFEafggydtdvavnKIAN------GLSIpdsQRS 156
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHL-----YLYARLR------------GVPAEEIE------------KVANwsiqslGLSL---YAD 2065
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 157 QLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISHDRYFLDRTVTRV 228
Cdd:TIGR01257 2066 RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRL 2140
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
161-194 |
4.80e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 4.80e-07
10 20 30
....*....|....*....|....*....|....
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL 194
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-235 |
4.89e-07 |
|
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: 51.49 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 24 TFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGLISqipvypagctvedvlrsafarleslAEEMR 103
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID-GQDIAAMS-------------------------RKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 104 ALearmaagesdpailkRYGTLSERFEAFGGYDTDVAVNKIANGLSI---PDSQR-----------------SQLFDSLS 163
Cdd:cd03294 98 EL---------------RRKKISMVFQSFALLPHRTVLENVAFGLEVqgvPRAEReeraaealelvglegweHKYPDELS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLD-LHATEWLEEYIR---SFHGTVVTISHDryfLD---RTVTRVIEIQDGK 235
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDpLIRREMQDELLRlqaELQKTIVFITHD---LDealRLGDRIAIMKDGR 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
332-501 |
6.48e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.19 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIK----MIvgELYPD---DGRiktgpqvkeaylpqiIRFD 404
Cdd:COG1117 14 VRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrMN--DLIPGarvEGE---------------ILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 405 -----HPDWNLVEN----MMAAKK--------------GLSAQSARNRlAAYDFRGEDVFK--------------PVSVL 447
Cdd:COG1117 77 gediyDPDVDVVELrrrvGMVFQKpnpfpksiydnvayGLRLHGIKSK-SELDEIVEESLRkaalwdevkdrlkkSALGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 448 SGGEQsrLRLC----MLMDDEInfLILDEPTNHLDIDSREWIEEAVEA----YdgTLLFVSH 501
Cdd:COG1117 156 SGGQQ--QRLCiaraLAVEPEV--LLMDEPTSALDPISTAKIEELILElkkdY--TIVIVTH 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
8.79e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEVGKnVLDGLTFQVDQGERVGLLGRNGAGKTTLFKIL------------TGELDYDEGTV----VVG 64
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIfkmdVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 65 QGRRVGLISQIP-VYPAGCTVEDVlrSAFARLESLAEEMRALEARmaagesdpailkrygtLSERFEAFGGYDtdvavnK 143
Cdd:PRK14247 80 LRRRVQMVFQIPnPIPNLSIFENV--ALGLKLNRLVKSKKELQER----------------VRWALEKAQLWD------E 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 144 IANGLSIPDSqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISH 216
Cdd:PRK14247 136 VKDRLDAPAG-------KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-193 |
9.00e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSF---EVGKNVldglTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRrvglISQIPv 77
Cdd:PRK11000 1 MASVTLRNVTKAYgdvVISKDI----NLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR----MNDVP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 78 yPAGCTVEDVLRS-AFARLESLAEEMrALEARMAaGESDPAILKRygtlserfeafggydtdvaVNKIANGLsipdsQRS 156
Cdd:PRK11000 72 -PAERGVGMVFQSyALYPHLSVAENM-SFGLKLA-GAKKEEINQR-------------------VNQVAEVL-----QLA 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2526491659 157 QLFD----SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK11000 125 HLLDrkpkALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-222 |
1.08e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 30 GERVGLLGRNGAGKTTLFKILTGELDYDegtvvvgqgrrVGLISQIPVYpagctvEDVLRsAFArleslAEEMRALEARM 109
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPN-----------LGKFDDPPDW------DEILD-EFR-----GSELQNYFTKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 110 AAGESDPAILKRY---------GTLSERFEAfggYDTDVAVNKIANGLSIpDSQRSQLFDSLSGGEKTRVNLGRLILEDT 180
Cdd:cd03236 83 LEGDVKVIVKPQYvdlipkavkGKVGELLKK---KDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2526491659 181 DILLLDEPTNHLD----LHATEWLEEYIRSfHGTVVTISHDRYFLD 222
Cdd:cd03236 159 DFYFFDEPSSYLDikqrLNAARLIRELAED-DNYVLVVEHDLAVLD 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-217 |
1.10e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 21 DGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQ-------------IPVYPAGCTVEDV 87
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiarmgvvrtfqhVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 88 LRSAFARLES--LAEEMRALEARMAAGESdpaiLKRYGTLSERfeafggydtdVAVNKIANglsipdsqRSQlfDSLSGG 165
Cdd:PRK11300 102 LVAQHQQLKTglFSGLLKTPAFRRAESEA----LDRAATWLER----------VGLLEHAN--------RQA--GNLAYG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 166 EKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYI---RSFHG-TVVTISHD 217
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelRNEHNvTVLLIEHD 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-235 |
1.58e-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: 50.48 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVD---QGERV-GLLGRNGAGKTTLFKILTGELDYDEGTVVVG--------QG-------RRVGLISQ----IP 76
Cdd:COG4148 11 RGGFTLDVDftlPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsaRGiflpphrRRIGYVFQearlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 VYpagcTVEDVLR------SAFARLESLAE--EMRALEArmaagesdpaILKRYgtlserfeafggydtdvavnkiangl 148
Cdd:COG4148 91 HL----SVRGNLLygrkraPRAERRISFDEvvELLGIGH----------LLDRR-------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 149 siPDSqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHA----TEWLEEYIRSFHGTVVTISHDRYFLDRT 224
Cdd:COG4148 131 --PAT--------LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHSLDEVARL 200
|
250
....*....|.
gi 2526491659 225 VTRVIEIQDGK 235
Cdd:COG4148 201 ADHVVLLEQGR 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
326-501 |
1.96e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 326 GDEVLGIRNVSKSYGD------KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLP 398
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QIIR------FDHPDWNLV------------ENMmaakkGLSAQSARNR-------LAAYDFRGEdvfkPVSVLSGGEQS 453
Cdd:PRK13633 81 WDIRnkagmvFQNPDNQIVativeedvafgpENL-----GIPPEEIRERvdeslkkVGMYEYRRH----APHLLSGGQKQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 454 RLRLCMLMDDEINFLILDEPTNHLDIDSRE----WIEEAVEAYDGTLLFVSH 501
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRRevvnTIKELNKKYGITIILITH 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
330-377 |
2.19e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 2.19e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2526491659 330 LGIRNVSKSYGDKHL-FEGISLKVEGGERIALIGDNGTGKSTLIKMIVG 377
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG 52
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
160-235 |
2.41e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 160 DSLSGGEKTRVNLG-RLILEDT-----DILLLDEPTNHLDL-HATEWLEEYIRS----FHGTVVTISHDRYFLDR--TVT 226
Cdd:cd03240 114 GRCSGGEKVLASLIiRLALAETfgsncGILALDEPTTNLDEeNIEESLAEIIEErksqKNFQLIVITHDEELVDAadHIY 193
|
....*....
gi 2526491659 227 RVIEIQDGK 235
Cdd:cd03240 194 RVEKDGRQK 202
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
329-377 |
2.71e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 2.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVG 377
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
329-477 |
2.75e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSY-GDKHLfEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK--------TGPQVKEAYLPQ 399
Cdd:PRK10762 4 LLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevtfNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIrfdHPDWNLVENMMAAKKGLSAQSARNRLAAYD----FRGEDVF-----------KPVSVLSGGEQSRLRLCMLMDDE 464
Cdd:PRK10762 83 II---HQELNLIPQLTIAENIFLGREFVNRFGRIDwkkmYAEADKLlarlnlrfssdKLVGELSIGEQQMVEIAKVLSFE 159
|
170
....*....|...
gi 2526491659 465 INFLILDEPTNHL 477
Cdd:PRK10762 160 SKVIIMDEPTDAL 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-386 |
3.09e-06 |
|
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: 50.07 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVG---KNVLDGLTFQVDQGERVGLLGRNGAGKT----TLFKILTGELDYDEGTVVV-GQ---------- 65
Cdd:COG4172 7 LSVEDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFdGQdllglserel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 66 ----GRRVGLISQ------IPVYpagcTVEDVLRsafarlESLA--EEMRALEARMAAGEsdpaILKRYGtlserfeafg 133
Cdd:COG4172 87 rrirGNRIAMIFQepmtslNPLH----TIGKQIA------EVLRlhRGLSGAAARARALE----LLERVG---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 134 gydtdvavnkianglsIPDSQRsqLFDS----LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDlhAT------EWLEEY 203
Cdd:COG4172 143 ----------------IPDPER--RLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALD--VTvqaqilDLLKDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 204 IRSFHGTVVTISHD----RYFLDRtvtrVIEIQDGKAEfysgnysfyavekerryqermkqyekEQAKIAQLEKAAEQlr 279
Cdd:COG4172 203 QRELGMALLLITHDlgvvRRFADR----VAVMRQGEIV--------------------------EQGPTAELFAAPQH-- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 280 vwafmgmdkTYRRAI---SMERRIERMRTTAKPtkarkmdarfssaefhgdeVLGIRNVSKSY-GDKHLF---------- 345
Cdd:COG4172 251 ---------PYTRKLlaaEPRGDPRPVPPDAPP-------------------LLEARDLKVWFpIKRGLFrrtvghvkav 302
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2526491659 346 EGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPDDGRI 386
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEI 342
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-271 |
3.75e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ----------------GRRVGLISQIPVYpagct 83
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrlRKEIGLVFQFPEY----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 vedvlrsafarleSLAEEmrALEARMAAGesdPAILkrygtlserfeafgGYDTDVAVNKIANGL---SIPD--SQRSQL 158
Cdd:PRK13645 102 -------------QLFQE--TIEKDIAFG---PVNL--------------GENKQEAYKKVPELLklvQLPEdyVKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 159 fdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATE----WLEEYIRSFHGTVVTISHDRYFLDRTVTRVIEIQDG 234
Cdd:PRK13645 150 --ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 2526491659 235 KAEFYSGNYSFYAvekerrYQERMKQYEKEQAKIAQL 271
Cdd:PRK13645 228 KVISIGSPFEIFS------NQELLTKIEIDPPKLYQL 258
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-234 |
3.90e-06 |
|
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: 48.48 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGtvvvgqgrRVGLISQIPVYPAGCT 83
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--------KVHWSNKNESEPSFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VEDVLRSAFARLESLAEEMRA-LEARMAAGEsdPAILKRYGTLSERFEAfgGYDTDVavnkianglsIPDSQRSQLFD-- 160
Cdd:cd03290 73 TRSRNRYSVAYAAQKPWLLNAtVEENITFGS--PFNKQRYKAVTDACSL--QPDIDL----------LPFGDQTEIGErg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 161 -SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLE-----EYIRSFHGTVVTISHDRYFLDRTvTRVIEIQDG 234
Cdd:cd03290 139 iNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYLPHA-DWIIAMKDG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
327-502 |
4.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 327 DEVLGIRNVSKSY---GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKT-GPQVKEAYLPQIIR 402
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 403 -----FDHPDWNLV------------ENMMAAKKGLSAQSARNRLAA--YDFRGEDVFKpvsvLSGGEQSRLRLCMLMDD 463
Cdd:PRK13642 82 kigmvFQNPDNQFVgatveddvafgmENQGIPREEMIKRVDEALLAVnmLDFKTREPAR----LSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2526491659 464 EINFLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHD 502
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRqeimRVIHEIKEKYQLTVLSITHD 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-216 |
6.47e-06 |
|
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: 49.36 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRRVGLISQIP-----------VYPAgcTV 84
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPymtlgtlrdqiIYPD--SS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVLRSAF--ARLESLAEEMRaLEArmaagesdpaILKRYGTLSerfeafggydtdvavnkianglSIPDSQrsqlfDSL 162
Cdd:TIGR00954 542 EDMKRRGLsdKDLEQILDNVQ-LTH----------ILEREGGWS----------------------AVQDWM-----DVL 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 163 SGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGTVVTISH 216
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-193 |
6.76e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.79 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV-GQGrrvglISQIP------ 76
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQD-----ITHVPaenrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 --------VYPAGCTVEDVlrsAFA-RLESLAE---EMRALEA-RMAagesdpailkrygtlseRFEAFGGydtdvavNK 143
Cdd:PRK09452 89 ntvfqsyaLFPHMTVFENV---AFGlRMQKTPAaeiTPRVMEAlRMV-----------------QLEEFAQ-------RK 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526491659 144 IANglsipdsqrsqlfdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK09452 142 PHQ---------------LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
359-502 |
7.32e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 359 ALIGDNGTGKSTLIKmivgelypddgriktgpqvkeaylpQIIrfdhpdWNLVENMMAAKKGLSAQSARNR-LAAYDFRG 437
Cdd:cd03227 25 IITGPNGSGKSTILD-------------------------AIG------LALGGAQSATRRRSGVKAGCIVaAVSAELIF 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 438 EdvfkpVSVLSGGEQSRLRLCMLM----DDEINFLILDEPTNHLDIDSREWIEEAVEAY---DGTLLFVSHD 502
Cdd:cd03227 74 T-----RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHL 140
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-485 |
7.32e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 349 SLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQVKEAYLPQIirfDHPDWN---LVEN--MM 415
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQS---EEVDWSfpvLVEDvvMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 416 A------------AKKGLSAQSARNRLAAYDFRgedvFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSRE 483
Cdd:PRK15056 104 GryghmgwlrrakKRDRQIVTAALARVDMVEFR----HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
..
gi 2526491659 484 WI 485
Cdd:PRK15056 180 RI 181
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-216 |
8.32e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 8.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG----TVVTISH 216
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-522 |
8.52e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLISQIPVYPAGCT 83
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 84 VedvlrsAFARLeSLAEEMRALEaRMAAGEsdpailkrygTLSERFEAFGGYDTDVAVNKIANGLSIPDSQRS--QLFDS 161
Cdd:PRK09700 84 I------IYQEL-SVIDELTVLE-NLYIGR----------HLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDldEKVAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG---TVVTISHDRYFLDRTVTRVIEIQDGkAEF 238
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDG-SSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 239 YSGNYSfyavekerryqermkqyekeqakiaqlekaaeqlrvwafmgmdktyrrAISMERRIERMrttakptKARKMDAR 318
Cdd:PRK09700 225 CSGMVS------------------------------------------------DVSNDDIVRLM-------VGRELQNR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 319 FSS-----AEFHGDEVLGIRNVSKSygDKHLFEGISLKVEGGERIALIGDNGTGKSTLI-------KMIVGELYPDDGRI 386
Cdd:PRK09700 250 FNAmkenvSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMnclfgvdKRAGGEIRLNGKDI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 387 K-TGP--QVKE--AYLPQIIRFD--HPDWNLVENMMAAK-------KGL-----------SAQSARNRLAaydFRGEDVF 441
Cdd:PRK09700 328 SpRSPldAVKKgmAYITESRRDNgfFPNFSIAQNMAISRslkdggyKGAmglfhevdeqrTAENQRELLA---LKCHSVN 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 442 KPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVE--AYDG-TLLFVSHDRYFINRFATRIWELAD 518
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRqlADDGkVILMVSSELPEIITVCDRIAVFCE 484
|
....
gi 2526491659 519 GTIT 522
Cdd:PRK09700 485 GRLT 488
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-251 |
1.04e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELD-YDEGTVVVGQ----------------GRRVGLISQIP-VY 78
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKvlyfgkdifqidaiklRKEVGMVFQQPnPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 79 PAGCTVEDVlrsAFARLESLAEEMRALEARMAAGesdpaiLKRYGTLSErfeafggydtdvavnkIANGLSIPDSQrsql 158
Cdd:PRK14246 103 PHLSIYDNI---AYPLKSHGIKEKREIKKIVEEC------LRKVGLWKE----------------VYDRLNSPASQ---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 159 fdsLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISHDRYFLDRTVTRVIEIQDGK- 235
Cdd:PRK14246 154 ---LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEl 230
|
250
....*....|....*.
gi 2526491659 236 AEFYSGNYSFYAVEKE 251
Cdd:PRK14246 231 VEWGSSNEIFTSPKNE 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-193 |
1.30e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVL----------DGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYdEGTVVVgQGRRVGLIS 73
Cdd:COG4172 276 LEARDLKVWFPIKRGLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRF-DGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 74 QipvypagctvedvlrsafarleslaEEMRALEARMAAGESDPailkrYGTLSERFeafggydtDVAvNKIANGLSI--- 150
Cdd:COG4172 354 R-------------------------RALRPLRRRMQVVFQDP-----FGSLSPRM--------TVG-QIIAEGLRVhgp 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 151 --PDSQRSQLFDSL------------------SGGEKTRVNLGR-LILEdTDILLLDEPTNHLD 193
Cdd:COG4172 395 glSAAERRARVAEAleevgldpaarhryphefSGGQRQRIAIARaLILE-PKLLVLDEPTSALD 457
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
330-523 |
1.35e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSYGDKHLFEG-ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI-----KTGPQVKEAYLpQIIRF 403
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkPVTAEQPEDYR-KLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 404 DHPDWNLVENMMaAKKGLSAQSA-----------RNRLAAYDFRGEDVfkpvsVLSGGEQSRLRLCMLMDDEINFLILDE 472
Cdd:PRK10522 402 VFTDFHLFDQLL-GPEGKPANPAlvekwlerlkmAHKLELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 473 PTnhLDID---SREWIEE---AVEAYDGTLLFVSH-DRYFINrfATRIWELADGTITD 523
Cdd:PRK10522 476 WA--ADQDphfRREFYQVllpLLQEMGKTIFAISHdDHYFIH--ADRLLEMRNGQLSE 529
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
348-524 |
1.64e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVK----EAYLP-QIIRFDHPDWNLVeNMMAAKKGLS 422
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSviaiSAGLSgQLTGIENIEFKML-CMGFKRKEIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 423 AQSArnRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDI----DSREWIEEAVEAyDGTLLF 498
Cdd:PRK13546 122 AMTP--KIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQtfaqKCLDKIYEFKEQ-NKTIFF 198
|
170 180
....*....|....*....|....*.
gi 2526491659 499 VSHDRYFINRFATRIWELADGTITDY 524
Cdd:PRK13546 199 VSHNLGQVRQFCTKIAWIEGGKLKDY 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
161-229 |
1.97e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 1.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD----LHATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVI 229
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
349-522 |
1.99e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 349 SLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQ-------------VKEAYL------------------ 397
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFShitrlsfeqlqklVSDEWQrnntdmlspgeddtgrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 398 PQIIRFDHPDWNLVEnMMAAKKGLSAQSARNrlaaydfrgedvFKpvsVLSGGEQSRLRLCMLMDDEINFLILDEPTNHL 477
Cdd:PRK10938 103 AEIIQDEVKDPARCE-QLAQQFGITALLDRR------------FK---YLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 478 DIDSREWIEEAVEAYDG---TLLFVshdryfINRF------ATRIWELADGTIT 522
Cdd:PRK10938 167 DVASRQQLAELLASLHQsgiTLVLV------LNRFdeipdfVQFAGVLADCTLA 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-258 |
2.23e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.76 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQG-------------RRVG 70
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 71 LISQIPvypagctvEDVLRSAfarleSLAEEMRALEARMAAGESDpaILKRYGTLSERfeafggydTDVAvnkianglsi 150
Cdd:PRK13636 86 MVFQDP--------DNQLFSA-----SVYQDVSFGAVNLKLPEDE--VRKRVDNALKR--------TGIE---------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 151 pdSQRSQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHAT----EWLEEYIRSFHGTVVTISHDRYFLDRTVT 226
Cdd:PRK13636 133 --HLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVseimKLLVEMQKELGLTIIIATHDIDIVPLYCD 210
|
250 260 270
....*....|....*....|....*....|....
gi 2526491659 227 RVIEIQDGKAEFYSGNYSFYAvEKE--RRYQERM 258
Cdd:PRK13636 211 NVFVMKEGRVILQGNPKEVFA-EKEmlRKVNLRL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-523 |
2.53e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 23 LTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ------GRRVGLISQIpvypAGCTVEDVLRSAFARLe 96
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrSRQVIELSEQ----SAAQMRHVRGADMAMI- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 97 sLAEEMRALEARMAAGESDPAILKRYgtlserfEAFGGYDTDVAVNKIANGLSIPDSQR--SQLFDSLSGGEKTRVNLGR 174
Cdd:PRK10261 110 -FQEPMTSLNPVFTVGEQIAESIRLH-------QGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 175 LILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHGT----VVTISHDRYFLDRTVTRVIEIQDGKA-EFYSGNYSFYAve 249
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmsmgVIFITHDMGVVAEIADRVLVMYQGEAvETGSVEQIFHA-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 250 kerryqermKQYEKEQAKIAQLEkaaeqlRVWAFMGMDKTYRRA-ISMERRIERMRTTAKPT--------KARKMDARFS 320
Cdd:PRK10261 260 ---------PQHPYTRALLAAVP------QLGAMKGLDYPRRFPlISLEHPAKQEPPIEQDTvvdgepilQVRNLVTRFP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 321 SAEfhgdevlGIRNVSKSygDKHLFEGISLKVEGGERIALIGDNGTGKST-------LIKMIVGELYPDDGRIKTGPQVK 393
Cdd:PRK10261 325 LRS-------GLLNRVTR--EVHAVEKVSFDLWPGETLSLVGESGSGKSTtgrallrLVESQGGEIIFNGQRIDTLSPGK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 394 EAYLPQIIRFDHPD------------WNLVENMMAAKKgLSAQSARNRLA----AYDFRGEDVFKPVSVLSGGEqsRLRL 457
Cdd:PRK10261 396 LQALRRDIQFIFQDpyasldprqtvgDSIMEPLRVHGL-LPGKAAAARVAwlleRVGLLPEHAWRYPHEFSGGQ--RQRI 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 458 CMLMDDEIN--FLILDEPTNHLDIDSREWI--------EEAVEAYdgtlLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK10261 473 CIARALALNpkVIIADEAVSALDVSIRGQIinllldlqRDFGIAY----LFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-235 |
3.89e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLvkSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTtlfkiLT--GELDYDEGTVVVGQGRRvgLISQIPVYPA- 80
Cdd:PRK10418 5 IELRNI--ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS-----LTcaAALGILPAGVRQTAGRV--LLDGKPVAPCa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 --GCTVEDVL---RSAFARLESLAEEmrALEARMAAGESDPAilkryGTLSERFEAFGgydtdvavnkianglsIPDSQR 155
Cdd:PRK10418 76 lrGRKIATIMqnpRSAFNPLHTMHTH--ARETCLALGKPADD-----ATLTAALEAVG----------------LENAAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 156 -SQLFD-SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDL----HATEWLEEYIRSFHGTVVTISHDRYFLDRTVTRVI 229
Cdd:PRK10418 133 vLKLYPfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVA 212
|
....*.
gi 2526491659 230 EIQDGK 235
Cdd:PRK10418 213 VMSHGR 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-193 |
3.97e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGelDYDEG--TVVVGQGRRVGlisqipvypAG 81
Cdd:PRK10938 261 IVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysNDLTLFGRRRG---------SG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 82 CTVEDVLRSAFARLESLaeemrALEARMAAGESDpAILKRYgtlserFEAFGGYD--TDvAVNKIANG----LSIPDSQR 155
Cdd:PRK10938 329 ETIWDIKKHIGYVSSSL-----HLDYRVSTSVRN-VILSGF------FDSIGIYQavSD-RQQKLAQQwldiLGIDKRTA 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 2526491659 156 SQLFDSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK10938 396 DAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-235 |
4.78e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 17 KNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQGRrVGLISQIP-VYPAgcTVED--VLRSAF- 92
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT-VAYVPQVSwIFNA--TVRDniLFGSPFd 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 93 -ARLEslaeemRALEArmAAGESDPAILKrygtlserfeafGGYDTDVAvnkiANGLSIpdsqrsqlfdslSGGEKTRVN 171
Cdd:PLN03130 707 pERYE------RAIDV--TALQHDLDLLP------------GGDLTEIG----ERGVNI------------SGGQKQRVS 750
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 172 LGRLILEDTDILLLDEPTNHLDLH-ATEWLEEYIRS--FHGTVVTISHDRYFLDRtVTRVIEIQDGK 235
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDelRGKTRVLVTNQLHFLSQ-VDRIILVHEGM 816
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-216 |
5.31e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 16 GKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGQ------------------GRRVGLISQIP 76
Cdd:PRK14267 15 GSNhVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEvrlfgrniyspdvdpievRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 -VYPAGCTVEDVlrsafarleslaeemralearmAAGESDPAILKRYGTLSERFEAfggydtdvAVNKIAnglsIPDSQR 155
Cdd:PRK14267 95 nPFPHLTIYDNV----------------------AIGVKLNGLVKSKKELDERVEW--------ALKKAA----LWDEVK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 156 SQLFD---SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSFHG--TVVTISH 216
Cdd:PRK14267 141 DRLNDypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
359-521 |
6.63e-05 |
|
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: 46.16 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 359 ALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQI-----------IRFDHpdWNLVENMM--AAKKGLSAQS 425
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVrqslgmcpqhnILFHH--LTVAEHILfyAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 426 ARNRLAA-------YDFRGEDVfkpvSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDG--TL 496
Cdd:TIGR01257 1038 AQLEMEAmledtglHHKRNEEA----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTI 1113
|
170 180
....*....|....*....|....*
gi 2526491659 497 LFVSHDRYFINRFATRIWELADGTI 521
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
332-386 |
7.41e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.45 E-value: 7.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDK----HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVG-ELyPDDGRI 386
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlER-PTSGSV 62
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
330-513 |
8.38e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 330 LGIRNVSKSY----GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGEL------YPDdGRIKTGPQ----VKEA 395
Cdd:PRK15134 6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvvYPS-GDIRFHGEsllhASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 396 YLPQI------IRFDHPDWNL-----VENMMAA----KKGLSAQSAR----------------NRLAAYDFRgedvfkpv 444
Cdd:PRK15134 85 TLRGVrgnkiaMIFQEPMVSLnplhtLEKQLYEvlslHRGMRREAARgeilncldrvgirqaaKRLTDYPHQ-------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526491659 445 svLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWI----EEAVEAYDGTLLFVSHDRYFINRFATRI 513
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIlqllRELQQELNMGLLFITHNLSIVRKLADRV 227
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
161-223 |
8.69e-05 |
|
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: 43.47 E-value: 8.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTD--ILLLDEPTNHLDLHATEWLEEYIRSF---HGTVVTISHDRYFLDR 223
Cdd:cd03238 87 TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLSS 154
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-216 |
9.52e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKT----TLFKIL---TGEL---DYDEGTVVVGQGRRV-GLISQIPVYPAGcTVEDV 87
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIVeleRGRIlidGCDISKFGLMDLRKVlGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 88 LrSAFARlESLAEEMRALEArmaagesdpAILKrygtlserfeafggydtDVaVNKIANGLsipDSQRSQLFDSLSGGEK 167
Cdd:PLN03130 1333 L-DPFNE-HNDADLWESLER---------AHLK-----------------DV-IRRNSLGL---DAEVSEAGENFSVGQR 1380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 168 TRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIR-SFHG-TVVTISH 216
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIReEFKScTMLIIAH 1431
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-166 |
9.75e-05 |
|
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: 43.77 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 10 VKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTG--ELDYDEGTVVV-GQG------RRVGLISQIPVYPA 80
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILInGRPldknfqRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 81 GCTVEDVLR-SAFARLESLAEEMR---ALEarMAAgesDPAILkrygtlserF--EAFGGYDTDVA------VNKIAN-G 147
Cdd:cd03232 93 NLTVREALRfSALLRGLSVEQRKRltiGVE--LAA---KPSIL---------FldEPTSGLDSQAAynivrfLKKLADsG 158
|
170 180
....*....|....*....|....*....
gi 2526491659 148 LSI------PDSQRSQLFDSL----SGGE 166
Cdd:cd03232 159 QAIlctihqPSASIFEKFDRLlllkRGGK 187
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
348-524 |
9.88e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 348 ISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIktgpQVK-EAYLPQIIRFDHPDWNLVEN------MMAAKKG 420
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----DIKgSAALIAISSGLNGQLTGIENielkglMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 421 lSAQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPtnhLDIDSREWIEEAVEAYD------G 494
Cdd:PRK13545 119 -KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQTFTKKCLDKMNefkeqgK 194
|
170 180 190
....*....|....*....|....*....|
gi 2526491659 495 TLLFVSHDRYFINRFATRIWELADGTITDY 524
Cdd:PRK13545 195 TIFFISHSLSQVKSFCTKALWLHYGQVKEY 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-242 |
9.98e-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: 45.17 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 12 SFEVGknVLDgLTFQvdQGERVGLLGRNGAGKTTLFKILTGeLdY--DEGTVVVGqgrrvglisqipvypaGCTVEDVLR 89
Cdd:COG4615 345 GFTLG--PID-LTIR--RGELVFIVGGNGSGKSTLAKLLTG-L-YrpESGEILLD----------------GQPVTADNR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 90 SAFARLES-------LAEEMRALEarmaaGESDPAILKRYgtLsERFEafggydtdvavnkIANGLSIPDSQRSQLfdSL 162
Cdd:COG4615 402 EAYRQLFSavfsdfhLFDRLLGLD-----GEADPARAREL--L-ERLE-------------LDHKVSVEDGRFSTT--DL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 163 SGGEKTRVNLGRLILEDTDILLLDEPTNHLDLH-----ATEWLEEyIRSFHGTVVTISHD-RYF--LDrtvtRVIEIQDG 234
Cdd:COG4615 459 SQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELLPE-LKARGKTVIAISHDdRYFdlAD----RVLKMDYG 533
|
....*...
gi 2526491659 235 KAEFYSGN 242
Cdd:COG4615 534 KLVELTGP 541
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
329-499 |
1.07e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVG--ELYPDDGRIKTGPQVKEAYLPQ------- 399
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEdragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 400 IIRFDHP-DWNLVENMMAAKKGLSA------QSARNRLAAYDFRGEDV----------FKPVSV-LSGGEQSRLRLCMLM 461
Cdd:PRK09580 81 FMAFQYPvEIPGVSNQFFLQTALNAvrsyrgQEPLDRFDFQDLMEEKIallkmpedllTRSVNVgFSGGEKKRNDILQMA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2526491659 462 DDEINFLILDEPTNHLDIDSREWIEEAVEAY-DGTLLFV 499
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLrDGKRSFI 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
79-217 |
1.13e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 79 PAGCTVEDVLRsAFARLESLAEEMRAlEARMA-------AGESDPA-ILKRYGTLSER---FE-------AFG----GY- 135
Cdd:PRK14243 44 PSGCGKSTILR-CFNRLNDLIPGFRV-EGKVTfhgknlyAPDVDPVeVRRRIGMVFQKpnpFPksiydniAYGarinGYk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 136 -DTDVAVNKIANGLSIPDSQRSQLFDS---LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYIRSF--HG 209
Cdd:PRK14243 122 gDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQY 201
|
....*...
gi 2526491659 210 TVVTISHD 217
Cdd:PRK14243 202 TIIIVTHN 209
|
|
| Miro1 |
cd01893 |
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ... |
357-382 |
1.32e-04 |
|
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.
Pssm-ID: 206680 [Multi-domain] Cd Length: 168 Bit Score: 43.09 E-value: 1.32e-04
10 20
....*....|....*....|....*.
gi 2526491659 357 RIALIGDNGTGKSTLIKMIVGELYPD 382
Cdd:cd01893 4 RIVLIGDEGVGKSSLIMSLVSEEFPE 29
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
332-386 |
1.47e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.41 E-value: 1.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 332 IRNVSKSY----GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-235 |
1.49e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 24 TFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVGLISQipvypagCTVEDVLRSAFArlesLAEEMR 103
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKISD-------AELREVRRKKIA----MVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 104 ALEARMAAGESDPAILKRYGT-LSERFEAFGGYDTDVAVNKIANGLSipdsqrsqlfDSLSGGEKTRVNLGRLILEDTDI 182
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYP----------DELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 183 LLLDEPTNHLD-LHATEWLEEYIR---SFHGTVVTISHDRYFLDRTVTRVIEIQDGK 235
Cdd:PRK10070 186 LLMDEAFSALDpLIRTEMQDELVKlqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-193 |
1.49e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 1 MIEIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVGqGRRVGLISqiP---- 76
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIG-GRVVNELE--Padrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 77 ---------VYPAgCTVEDvlrsafarleslaeemraleaRMAAGesdpaiLKRYGTLSERFEAfggydtdvAVNKIANG 147
Cdd:PRK11650 78 iamvfqnyaLYPH-MSVRE---------------------NMAYG------LKIRGMPKAEIEE--------RVAEAARI 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2526491659 148 LSIpdsqrSQLFD----SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK11650 122 LEL-----EPLLDrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
329-381 |
1.57e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 329 VLGIRNVSKSY-GDKHLfEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYP 381
Cdd:NF040905 1 ILEMRGITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYP 52
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
332-386 |
1.86e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.71 E-value: 1.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2526491659 332 IRNVSKSY-GDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
327-386 |
1.96e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 1.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 327 DEVLGIRNVSKSYGDKH-LF--------EGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI 386
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-193 |
2.00e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELD---YDEGTVVVGQG-------RRVGLISQIPVYPAGCTVEDVL 88
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRpldssfqRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 89 R-SAFARLE---SLAEEMRALEARMAAGEsdpaiLKRYgtlserfeafggydTDVAVNKIANGLSIpdSQRSqlfdslsg 164
Cdd:TIGR00956 858 RfSAYLRQPksvSKSEKMEYVEEVIKLLE-----MESY--------------ADAVVGVPGEGLNV--EQRK-------- 908
|
170 180 190
....*....|....*....|....*....|
gi 2526491659 165 gektRVNLG-RLILEDTDILLLDEPTNHLD 193
Cdd:TIGR00956 909 ----RLTIGvELVAKPKLLLFLDEPTSGLD 934
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
332-411 |
2.46e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRIK-TGPQV-----KEAyLPQIIRFDH 405
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIdfkssKEA-LENGISMVH 79
|
....*.
gi 2526491659 406 PDWNLV 411
Cdd:PRK10982 80 QELNLV 85
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-61 |
2.91e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.99 E-value: 2.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 5 QVNNLVKSFEVGKNvLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV 61
Cdd:PRK11701 8 SVRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-55 |
2.98e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 42.25 E-value: 2.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 1 MIEIQVNNLVKSFEVGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELD 55
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE 58
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-52 |
5.32e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 5.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2526491659 8 NLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTG 52
Cdd:NF040905 6 GITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
332-501 |
5.52e-04 |
|
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: 41.71 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 332 IRNVSKSYGD--KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYPDDGRI--------KTGPQV---KEAYLP 398
Cdd:cd03244 5 FKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdisKIGLHDlrsRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 399 QI-------IRFD------HPD---WNLVENM------MAAKKGLSAQSARNrlaaydfrGEDvfkpvsvLSGGEQSRLR 456
Cdd:cd03244 85 QDpvlfsgtIRSNldpfgeYSDeelWQALERVglkefvESLPGGLDTVVEEG--------GEN-------LSVGQRQLLC 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2526491659 457 LCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAY--DGTLLFVSH 501
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-61 |
9.04e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 9.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTV 61
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
556-635 |
1.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 556 AAERPQRGNKAQQAARRQLTICER---------DIARAEERIAALEADMEAAACDYEKLNELVGQKDAAQAELDALYERW 626
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
....*....
gi 2526491659 627 EQLSEEAEG 635
Cdd:COG4913 709 DELKGEIGR 717
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-523 |
1.59e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 334 NVSKSYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKM-------IVGELYPDD----GR-IKTGPQVKEAYLPQII 401
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGDvllgGRsIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 402 RFDHPD---WNLVENMMAAKKGLS----------AQSARNRLAAYDFRGEDVFKPVSVLSGGEQSRLRLCMLMDDEINFL 468
Cdd:PRK14271 106 LFQRPNpfpMSIMDNVLAGVRAHKlvprkefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2526491659 469 ILDEPTNHLDIDSREWIEEAVEAYDG--TLLFVSHDRYFINRFATRIWELADGTITD 523
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-400 |
1.89e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 338 SYGDKHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYP-DDGRIKTGPQVkeAYLPQI 400
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTV--AYVPQV 687
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-62 |
2.19e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526491659 4 IQVNNLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDY--DEGTVV 62
Cdd:PRK09580 2 LSIKDLHVSVE-DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVE 61
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
161-196 |
2.84e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.84e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2526491659 161 SLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHA 196
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA 426
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-63 |
2.87e-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: 38.51 E-value: 2.87e-03
10 20 30
....*....|....*....|....*....|....*
gi 2526491659 29 QGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVV 63
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-106 |
3.34e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 19 VLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRVG------------LISQIPVYPAGCTVED 86
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV-NGREIGayglrelrrqfsMIPQDPVLFDGTVRQN 1403
|
90 100
....*....|....*....|.
gi 2526491659 87 VlrSAFarLE-SLAEEMRALE 106
Cdd:PTZ00243 1404 V--DPF--LEaSSAEVWAALE 1420
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
10-192 |
3.55e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 10 VKSFEVgKNV--LDGLTFQVDQGERVGLL-GRNGAGKTTLFKI----LTGEL----DYDEGTVVVGQGRRVGLISQIPVY 78
Cdd:COG3950 3 IKSLTI-ENFrgFEDLEIDFDNPPRLTVLvGENGSGKTTLLEAialaLSGLLsrldDVKFRKLLIRNGEFGDSAKLILYY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 79 PAGCTVED--------VLRSAFARLESLAE------EMRALEARMAAGESDpAILKRYGTLSERFEAF------------ 132
Cdd:COG3950 82 GTSRLLLDgplkklerLKEEYFSRLDGYDSlldedsNLREFLEWLREYLED-LENKLSDELDEKLEAVrealnkllpdfk 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 133 -----GGYDTDVAVNKiaNGLSIPdsqrsqlFDSLSGGEKTRVNL-GRLI------------LEDTD-ILLLDEPTNHL 192
Cdd:COG3950 161 diridRDPGRLVILDK--NGEELP-------LNQLSDGERSLLALvGDLArrlaelnpalenPLEGEgIVLIDEIDLHL 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-69 |
3.67e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 3.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 8 NLVKSFEvGKNVLDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV 69
Cdd:PRK10982 3 NISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-QGKEI 62
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-216 |
3.86e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.63 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 4 IQVNNLvkSFEVGKN-VLDGLTFQVDQGERVGLLGRNGAGKTTLFKIL------------TGE--LD----YDEGTVVVG 64
Cdd:COG1117 12 IEVRNL--NVYYGDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarvEGEilLDgediYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 65 QGRRVGLISQIP-----------VYPA---GCT--------VEDVLRSAfarleSLAEEmraLEARmaagesdpaiLKRY 122
Cdd:COG1117 90 LRRRVGMVFQKPnpfpksiydnvAYGLrlhGIKskseldeiVEESLRKA-----ALWDE---VKDR----------LKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 123 GTlserfeafggydtdvavnkianglsipdsqrsqlfdSLSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEE 202
Cdd:COG1117 152 AL------------------------------------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEE 195
|
250
....*....|....*.
gi 2526491659 203 YIRSFHG--TVVTISH 216
Cdd:COG1117 196 LILELKKdyTIVIVTH 211
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
359-523 |
4.45e-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: 39.68 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 359 ALIGDNGTGKSTLIKMIVGELYPDDGRIKTGPQVKEAYLPQIIRFdhpDWNLVENMMAAKKGLSAQSARNRLAAYDFRGE 438
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPS---LLNGIDPKEPIEFEISEFLEDGVRYRYGLDLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 439 --DVFKPVSVLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSREWIEEAVEAYDgTLLFVSHDRYFINRFATRIWEL 516
Cdd:pfam13304 80 reDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELS-DLISGLLLLSIISPLSFLLLLD 158
|
....*..
gi 2526491659 517 ADGTITD 523
Cdd:pfam13304 159 EGLLLED 165
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
162-233 |
4.92e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.45 E-value: 4.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526491659 162 LSGGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYI---RSFHGTVVTISHdryfldrTVTRVIEIQD 233
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNKTVFVITH-------TMEHVLEVAD 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-217 |
5.19e-03 |
|
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: 38.99 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 20 LDGLTFQVDQGERVGLLGRNGAGKTTLFKILTGELDYDEGTVVVgQGRRV--------------GLISQIPVYP-AGCTV 84
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQItepgpdrmvvfqnySLLPWLTVREnIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 85 EDVLRSA-FARLESLAEEMRALEARMAAGESDPailkrygtlserfeafggydtdvavnkianglsipdsqrsqlfDSLS 163
Cdd:TIGR01184 80 DRVLPDLsKSERRAIVEEHIALVGLTEAADKRP-------------------------------------------GQLS 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526491659 164 GGEKTRVNLGRLILEDTDILLLDEPTNHLDLHATEWLEEYI----RSFHGTVVTISHD 217
Cdd:TIGR01184 117 GGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
442-508 |
6.19e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.07 E-value: 6.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526491659 442 KPVSVLSGGEQSRLRLCMLMDDEI--NFLILDEPTNHLD-IDSREWIEEAVEAYD--GTLLFVSHDRYFINR 508
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHqQDINQLLEVIKGLIDlgNTVILIEHNLDVLSS 154
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
160-193 |
6.21e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2526491659 160 DSLSGGEKT------RVNLGRLILEDTDILLLDEPTNHLD 193
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD 839
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
343-381 |
7.06e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 7.06e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2526491659 343 HLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGELYP 381
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-217 |
7.32e-03 |
|
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: 37.72 E-value: 7.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526491659 157 QLFDSLSGGEKTRVNLgRLIL-----EDTDILLLDEPTNHLDLHATEWLEEYIRSF--HG-TVVTISHD 217
Cdd:cd03227 73 FTRLQLSGGEKELSAL-ALILalaslKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGaQVIVITHL 140
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
329-513 |
7.34e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 39.28 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 329 VLGIRNVSKSYGD----KHLFEGISLKVEGGERIALIGDNGTGKSTLIKMIVGeLYPDDGRIKTG---------PQVKEA 395
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILR-LLPDPAAHPSGsilfdgqdlLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526491659 396 YLPQiIR-------FDHPDWNL-----VENMMA----AKKGLSAQSAR----------------NRLAAYDFRgedvfkp 443
Cdd:COG4172 85 ELRR-IRgnriamiFQEPMTSLnplhtIGKQIAevlrLHRGLSGAAARaralellervgipdpeRRLDAYPHQ------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526491659 444 vsvLSGGEQSRLRLCMLMDDEINFLILDEPTNHLDIDSR----EWIEEAVEAYDGTLLFVSHDRYFINRFATRI 513
Cdd:COG4172 157 ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQaqilDLLKDLQRELGMALLLITHDLGVVRRFADRV 227
|
|
| |
