|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-556 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1182.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 1 MAQYVYTMNRVGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPEL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 81 NPEHTVRQSVEEGLGAVFNAKQRLDEVYAAYAEPDADFDALAAEQAELEAVIAAAASsgaDDIEHQMEIAADALRLPPWD 160
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADA---WDLDSQLEIAMDALRCPPWD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 161 AMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYG 240
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 241 IPWKGNYSSWLEQKEDRLKQEEATESARQKTIKKELEWVRQNPKGRQAKAKARIARFEELSSYEYQKRNETQEIFIPVGD 320
Cdd:PRK11819 239 IPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 321 RLGNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDS 400
Cdd:PRK11819 319 RLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:PRK11819 399 LDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 481 ETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEGDSQVVFFDGNYQEYEADKKHRLGEEGAKPKRLRYKAL 556
Cdd:PRK11819 479 ETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKL 554
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-556 |
0e+00 |
|
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: 1096.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 2 AQYVYTMNRVGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPELN 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 82 PEHTVRQSVEEGLGAVFNAKQRLDEVYAAYAEPDADFDALAAEQAELEAVIAAAASSgadDIEHQMEIAADALRLPPWDA 161
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAW---DLDSQLEIAMDALRCPPWDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 162 MVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGI 241
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 242 PWKGNYSSWLEQKEDRLKQEEATESARQKTIKKELEWVRQNPKGRQAKAKARIARFEELSSYEYQKRNETQEIFIPVGDR 321
Cdd:TIGR03719 238 PWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 322 LGNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSL 401
Cdd:TIGR03719 318 LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE 481
Cdd:TIGR03719 398 DPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 482 TLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEGDSQVVFFDGNYQEYEADKKHRLGEEGAKPKRLRYKAL 556
Cdd:TIGR03719 478 TLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-536 |
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: 717.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 8 MNRVGKIVPpKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPELNPEHTVR 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLGAVFNAKQRLDEVYAAYAEPDADFDALAAEQAELEAVIAaaassgaDDIEHQMEIAADALRLP--PWDAMVGK 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGG-------WEAEARAEEILSGLGFPeeDLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGIPWKG 245
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 246 NYSSWLEQKEDRLKQEEATESARQKTIKKELEWVRQN-PKGRQAK-AKARIARFEELSSYEYQKRNETQEIFIPVGDRLG 323
Cdd:COG0488 233 NYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFrAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSLEG 403
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 404 NKTVFDAVADGADlltvGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETL 483
Cdd:COG0488 393 DKTVLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 484 RALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgDSQVVFFDGNYQEYEAD 536
Cdd:COG0488 469 EALEEALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-532 |
2.28e-105 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 329.60 E-value: 2.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 31 PGAKIGVLGLNGSGKSTLLKIMAGvdkEI---EGEAIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGAVFNAKQR---- 103
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNG---EVlldDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQAEYLKRyhdi 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 104 LDEVYAAYAEpdADFDALAAEQAELEAVIAAAassgaddIEHQMEIAADALRLPPwDAMVGKLSGGEKRRVALCRLLLSK 183
Cdd:PRK11147 105 SHLVETDPSE--KNLNELAKLQEQLDHHNLWQ-------LENRINEVLAQLGLDP-DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 184 PDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGIPWKGNYSSWLEQKEDRLKQEEA 263
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 264 TESARQKTIKKELEWVRQNPKGRQAKAKARIARFEELSSYEYQKRNE--TQEIFIPVGDRLGNEVIEFNHVSKAYGDRLL 341
Cdd:PRK11147 255 QNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVmgTAKMQVEEASRSGKIVFEMENVNYQIDGKQL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSLEGNKTVFDAVADGADLLTVG 421
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVN 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 422 KFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVIS 501
Cdd:PRK11147 415 GRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVS 494
|
490 500 510
....*....|....*....|....*....|.
gi 489917580 502 HDRWFLDRIATHILAFEGDSQVVFFDGNYQE 532
Cdd:PRK11147 495 HDRQFVDNTVTECWIFEGNGKIGRYVGGYHD 525
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-537 |
1.73e-80 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 261.75 E-value: 1.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGAVFNAKQRL 104
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTELWEVKQER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 105 DevyAAYAEPDA-DFDALAAeqAELEAVIAaaassgaddiehQM-----EIAADALRLP---PWDAMVGKLSG---GEKR 172
Cdd:PRK15064 100 D---RIYALPEMsEEDGMKV--ADLEVKFA------------EMdgytaEARAGELLLGvgiPEEQHYGLMSEvapGWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGIPWKGNYSSWLE 252
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 253 ---QKEDRLkqeeATESARQKTIKKEL-EWVRQ----NPKGRQAKAKARiaRFEELSSYEYqKRNETQEIFI--PVGDRL 322
Cdd:PRK15064 243 aatQARERL----LADNAKKKAQIAELqSFVSRfsanASKAKQATSRAK--QIDKIKLEEV-KPSSRQNPFIrfEQDKKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 323 GNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQ-SRDSL 401
Cdd:PRK15064 316 HRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGNKTVFDAVA----DGADLLTVgkfempsRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSND 477
Cdd:PRK15064 396 ENDLTLFDWMSqwrqEGDDEQAV-------RGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 478 LDVETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEGDsQVVFFDGNYQEYEADK 537
Cdd:PRK15064 469 MDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPD-GVVDFSGTYEEYLRSQ 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-549 |
1.37e-71 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 241.23 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvDKEIEGEAIPMPG-LNIGYLPQE-PELnpEHTVRQSVEEGLGA 96
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGGSYTFPGnWQLAWVNQEtPAL--PQPALEYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VFNAKQRLDEvyaayAEPDADFDALAAEQAELEAVIAAAASSGADDIEHQMEIAADALRLPpwdamVGKLSGGEKRRVAL 176
Cdd:PRK10636 91 YRQLEAQLHD-----ANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERP-----VSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGIPWKGNYSSWLEQKED 256
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 257 RLKQEEATESARQKTIKKELEWV-RQNPKGRQAK-AKARIARFEELSSYEYQKRNETQEIFIPVGDRLGNEVIEFNHVSK 334
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIdRFRAKATKAKqAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 335 AYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSR-DSLEGNKTVFDAVAD 413
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 414 GADLLTvgkfEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF 493
Cdd:PRK10636 401 LAPQEL----EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 494 PGSVMVISHDRWFLdRIATHILAFEGDSQVVFFDG---NYQEYEADKKHRLGEEGAKPK 549
Cdd:PRK10636 477 EGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGdleDYQQWLSDVQKQENQTDEAPK 534
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
329-541 |
1.18e-66 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 224.94 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 329 FNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSrDSLEGNKTVF 408
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 409 DAVADG--------------------------------ADLLTVGKFEMPSRA--YLGRFNFKGGDQNKIVGQLSGGERG 454
Cdd:COG0488 80 DTVLDGdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWEAEARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 455 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgDSQVVFFDGNYQEYE 534
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD-RGKLTLYPGNYSAYL 238
|
....*..
gi 489917580 535 ADKKHRL 541
Cdd:COG0488 239 EQRAERL 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
327-520 |
2.78e-59 |
|
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: 193.43 E-value: 2.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQsrdslegnkt 406
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 407 vfdavadgadlltvgkfempsraylgrfnfkggdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL 486
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....
gi 489917580 487 EDALLEFPGSVMVISHDRWFLDRIATHILAFEGD 520
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-534 |
1.74e-53 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 193.54 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdKEIEGeaIPMpglNIGYLPQEPEL-NPEHTVRQSVeegLGAV 97
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAM--HAIDG--IPK---NCQILHVEQEVvGDDTTALQCV---LNTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 FNAKQRL-DEVYAAYAEPDADFDALAAEQ--AELEAVIAAAASSGADDIEHQME-IAADALRLPPWDAMVG--------- 164
Cdd:PLN03073 260 IERTQLLeEEAQLVAQQRELEFETETGKGkgANKDGVDKDAVSQRLEEIYKRLElIDAYTAEARAASILAGlsftpemqv 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 ----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYG 240
Cdd:PLN03073 340 katkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 241 IPWKGNYSSWLEQKEDRLKQE----EATESARQKtIKKELEWVRQNPKgRQAKAKARIARFEELSSYEYQKRNETQEIFI 316
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQqkafESNERSRSH-MQAFIDKFRYNAK-RASLVQSRIKALDRLGHVDAVVNDPDYKFEF 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 317 PV-GDRLGNEVIEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYV 394
Cdd:PLN03073 498 PTpDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRdslegnktvfdavADGADLLTV----------GKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PLN03073 578 SQHH-------------VDGLDLSSNpllymmrcfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHDRWFLDRiATHILAFEGDSQVVFFDGNYQEYE 534
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG-SVDELWVVSEGKVTPFHGTFHDYK 713
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-238 |
1.64e-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: 173.02 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQepelnpehtvrqsveeglgav 97
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 fnakqrldevyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdamvgkLSGGEKRRVALC 177
Cdd:cd03221 71 --------------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 178 RLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-515 |
2.26e-42 |
|
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: 158.91 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV--------------DKEIEGEAIPMPGLNIGYLPQEPE--LNP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphggrisgevlldGRDLLELSEALRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 eHTVRQSVEEGLgavfnakqRLDEVyaayaePDADFDALAAEQAEleaviaaaassgaddiehQMEIAADALRLPpwdam 162
Cdd:COG1123 99 -VTVGDQIAEAL--------ENLGL------SRAEARARVLELLE------------------AVGLERRLDRYP----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 163 vGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:COG1123 141 -HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 239 ygipwkgnysswleqkedrlkqeEATESARQKTIKKELEWVRQNPKGRQAKAKARIARfeelssyeyqkrnetqeifipv 318
Cdd:COG1123 220 -----------------------RIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAA---------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 319 gdRLGNEVIEFNHVSKAY-----GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--- 389
Cdd:COG1123 255 --AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLtkl 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 ----------KLAYVDQS-RDSLEGNKTVFDAVADGADLLTVGKF-EMPSRAY--LGRFNFKGGDQNKIVGQLSGGERGR 455
Cdd:COG1123 333 srrslrelrrRVQMVFQDpYSSLNPRMTVGDIIAEPLRLHGLLSRaERRERVAelLERVGLPPDLADRYPHELSGGQRQR 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 456 LHLAKTLIAGGNVLLLDEPSNDLDVET----LRALEDALLEFPGSVMVISHDRWFLDRIATHIL 515
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
327-515 |
2.77e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.58 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTV---------KLAYVDQ 396
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SrDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:COG1131 81 E-PALYPDLTVRENLRFFARLYGLPRKEARERIdeLLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 475 SNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHIL 515
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVA 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-515 |
2.23e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-----KLAYVDQSRD 399
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 SlegNK----TVFDAVADGAdLLTVGKFEMPSRAY-------LGRFN---FKggdqNKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:COG1121 86 V---DWdfpiTVRDVVLMGR-YGRRGLFRRPSRADreavdeaLERVGledLA----DRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHIL 515
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVL 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
326-516 |
1.85e-36 |
|
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: 136.33 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYV 394
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRDSLEGNkTVFDAVAdgadlltvgkfempsrayLGRFNFKGG-------DQNKI----------------VGQLSGG 451
Cdd:COG1120 81 PQEPPAPFGL-TVRELVA------------------LGRYPHLGLfgrpsaeDREAVeealertglehladrpVDELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 452 ERGRLHLAKTLIAGGNVLLLDEPSNDLD----VETLRALEDALLEFPGSVMVISHDrwfLD---RIATHILA 516
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLVL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
327-515 |
2.88e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYVD 395
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QSRDSLEGnkTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPS 475
Cdd:COG4619 81 QEPALWGG--TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 476 NDLDVETLRALEDALLEFP----GSVMVISHDRWFLDRIATHIL 515
Cdd:COG4619 159 SALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVL 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-238 |
4.92e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNIGYLPQEPELNPEH--TVRQS 89
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPptsgtvRLFGKPPRRARRRIGYVPQRAEVDWDFpiTVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEEGLGAVFNAKQRLDEVyaayaepdadfDALAAEQAeLEaviaaaassgaddiehQMEIAADAlrlppwDAMVGKLSGG 169
Cdd:COG1121 98 VLMGRYGRRGLFRRPSRA-----------DREAVDEA-LE----------------RVGLEDLA------DRPIGELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-234 |
8.97e-35 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 129.91 E-value: 8.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGL----NIGYLPQEPELNPEHTVRQ 88
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpsagevLWNGEPIRDAREdyrrRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEeglgavfnakqrldeVYAAYAEPDADFDALAAeqaeleaviaaaassgaddiehqmeiAADALRLPP-WDAMVGKLS 167
Cdd:COG4133 95 NLR---------------FWAALYGLRADREAIDE--------------------------ALEAVGLAGlADLPVRQLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTHDRYFLDNAAEWILE 234
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARVLDLG 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
327-515 |
1.20e-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: 128.67 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTVKLAYVDQSRDslegnk 405
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIKKEPEEVKRR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 tvFDAVADGADL---LTVgkfempsRAYLgrfnfkggdqnkivgQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 482
Cdd:cd03230 75 --IGYLPEEPSLyenLTV-------RENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 483 LRALEDALLEF---PGSVMVISHDRWFLDRIATHIL 515
Cdd:cd03230 131 RREFWELLRELkkeGKTILLSSHILEEAERLCDRVA 166
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
326-515 |
3.25e-34 |
|
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: 129.59 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV--------KLGQTVK--LAYVD 395
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREARrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 Q-----SRDSLEGNKTVFDAVADGADLLTVGKFEMpsraYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:COG4555 81 DerglyDRLTVRENIRYFAELYGLFDEELKKRIEE----LIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489917580 471 LDEPSNDLDVETLRALEDALLEF---PGSVMVISHDRWFLDRIATHIL 515
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-238 |
4.32e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 4.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------AIPMPGL--NIGYLPQEPELNPEhtvr 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEiyldgkplsAMPPPEWrrQVAYVPQEPALWGG---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 qSVEEGLGAVFNAKQRldevyaayaepdaDFDALAAEQAeLEaviaaaassgaddiehQMEIAADALrlppwDAMVGKLS 167
Cdd:COG4619 89 -TVRDNLPFPFQLRER-------------KFDRERALEL-LE----------------RLGLPPDIL-----DKPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
342-476 |
7.33e-34 |
|
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: 125.45 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYVDQSrDSLEGNKTVFDA 410
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLtdderkslrkEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 411 VADGADLLTVGKFEMPSRAYLGRFNFKGGDQNK-----IVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSN 476
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
328-518 |
8.66e-34 |
|
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: 125.82 E-value: 8.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 328 EFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLgqtvklayvdqsrdslegnktv 407
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 408 fdavaDGADLLTVGKFEMpsRAYLGrfnfkggdqnkIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALE 487
Cdd:cd00267 59 -----DGKDIAKLPLEEL--RRRIG-----------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....
gi 489917580 488 DALLEFPG---SVMVISHDRWFLDRIATHILAFE 518
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-231 |
1.14e-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: 128.62 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIP-MPGL----NIGYLPQEPELNPEHT 85
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpssgevLLDGRDLAsLSRRelarRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGAVFNAKQRLDEVyaayaepdadfDALAAEQAeLEaviaaaassgaddiehQMEIAADALRLppwdamVGK 165
Cdd:COG1120 92 VRELVALGRYPHLGLFGRPSAE-----------DREAVEEA-LE----------------RTGLEHLADRP------VDE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEQF--LHKFPG-TVVAVTHDryfLDNAAEW 231
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLELLrrLARERGrTVVMVLHD---LNLAARY 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-238 |
2.31e-33 |
|
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: 126.43 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQepelnpeHTVRQSVeeglGAV 97
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGE-VLVDGKDLTKLSL-------KELRRKV----GLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 F-NAKQRL------DEVyaayaepdadfdALAAEQAELEAviaaaassgaDDIEHQMEIAADALRLPPW-DAMVGKLSGG 169
Cdd:cd03225 81 FqNPDDQFfgptveEEV------------AFGLENLGLPE----------EEIEERVEEALELVGLEGLrDRSPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
328-527 |
2.60e-33 |
|
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: 126.11 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 328 EFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-----KLAYVDQSRDSL 401
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EG-NKTVFDAVADGAdLLTVGKFEMPSRAY----------LGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:cd03235 81 RDfPISVRDVVLMGL-YGHKGLFRRLSKADkakvdealerVGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 471 LDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHILAFEGDsqVVFFD 527
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRT--VVASG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
328-518 |
3.32e-33 |
|
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: 125.66 E-value: 3.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 328 EFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYV 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLtklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 473 EPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHILAFE 518
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-194 |
6.97e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 122.76 E-value: 6.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-----------AIPMPGLNIGYLPQEPELNPEHTVRQSV 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEGLGAVFNAKQRLDEvyaayaepdadfdalaaeqaeleaviaaaassgaddiehQMEIAADALRLP-----PWDAMVGK 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDA---------------------------------------RAEEALEKLGLGdladrPVGERPGT 121
|
170 180
....*....|....*....|....*....
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTN 194
Cdd:pfam00005 122 LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
326-503 |
6.92e-32 |
|
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: 122.20 E-value: 6.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK---------LAYVD 395
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdaredyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QsRDSLEGNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPS 475
Cdd:COG4133 82 H-ADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 476 NDLDVETLRALEDALLEFP---GSVMVISHD 503
Cdd:COG4133 160 TALDAAGVALLAELIAAHLargGAVLLTTHQ 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
327-511 |
4.91e-31 |
|
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: 119.93 E-value: 4.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------KLAYVDQS 397
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 rDSLEGNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFK-GGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSN 476
Cdd:cd03259 81 -YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGlEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489917580 477 DLDVET---LRALEDALLEFPGSVMV-ISHDR----WFLDRIA 511
Cdd:cd03259 160 ALDAKLreeLREELKELQRELGITTIyVTHDQeealALADRIA 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
328-519 |
7.64e-31 |
|
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: 118.31 E-value: 7.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 328 EFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYVDQ 396
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRDSLegnktvfdavaDGADLLtvgkfempsraylgrfnfkggdqNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSN 476
Cdd:cd03214 81 ALELL-----------GLAHLA-----------------------DRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489917580 477 DLDV-------ETLRALEDallEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:cd03214 127 HLDIahqiellELLRRLAR---ERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-238 |
1.06e-30 |
|
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: 118.79 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLN-------IGYLPQEPELNPEH--TVRQS 89
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS-IRVFGKPlekerkrIGYVPQRRSIDRDFpiSVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEEGLGAVFNAKQRLDEvyaayaepdADFDAlaAEQAeLEaviaaaassgaddiehQMEIAADALRLppwdamVGKLSGG 169
Cdd:cd03235 91 VLMGLYGHKGLFRRLSK---------ADKAK--VDEA-LE----------------RVGLSELADRQ------IGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQfLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
327-492 |
2.13e-30 |
|
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: 118.34 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR----LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL------GQTVKLAYVDQ 396
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 sRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKGGdQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:cd03293 81 -QDALLPWLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170
....*....|....*...
gi 489917580 475 SNDLDVETLRALEDALLE 492
Cdd:cd03293 159 FSALDALTREQLQEELLD 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-238 |
2.76e-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: 118.20 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA----IPMPGLN-------IGYLPQepelNPEH 84
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgKDITKKNlrelrrkVGLVFQ----NPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 -----TVRqsveeglgavfnakqrlDEVyaayaepdadfdALAAEQAELEAviaaaassgaDDIEHQMEIAADALRLPPW 159
Cdd:COG1122 87 qlfapTVE-----------------EDV------------AFGPENLGLPR----------EEIRERVEEALELVGLEHL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 160 -DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILEL 235
Cdd:COG1122 128 aDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVL 207
|
...
gi 489917580 236 DRG 238
Cdd:COG1122 208 DDG 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
326-503 |
3.40e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.04 E-value: 3.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY----GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK-----LAYVD 395
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPVTgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QSrDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKGgDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:COG1116 87 QE-PALLPWLTVLDNVALGLELRGVPKAERRERAreLLELVGLAG-FEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190
....*....|....*....|....*....|....
gi 489917580 474 PSNDLDVETLRALEDALL----EFPGSVMVISHD 503
Cdd:COG1116 165 PFGALDALTRERLQDELLrlwqETGKTVLFVTHD 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
327-519 |
4.39e-30 |
|
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: 115.94 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRL--LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV-----------KLAY 393
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQsrdslegNKTVFDAvadgadllTVgkfempsraylgRFNFkggdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:cd03228 81 VPQ-------DPFLFSG--------TI------------RENI-----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489917580 474 PSNDLDVETLRALEDALLEFPG--SVMVISHdRWFLDRIATHILAFEG 519
Cdd:cd03228 123 ATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-238 |
8.90e-30 |
|
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: 124.18 E-value: 8.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------AIPMPGL--NIGYLPQEPELNPEhTVRQS 89
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlrQIDPASLrrQIGVVLQDVFLFSG-TIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VeeglgavfnakqrldevyaAYAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalRLPP-WDAMVG-- 164
Cdd:COG2274 569 I-------------------TLGDPDATDEEIieAARLAGLH-----------DFIE----------ALPMgYDTVVGeg 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 --KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHDRYFLDNaAEWILELDRG 238
Cdd:COG2274 609 gsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-279 |
1.59e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.50 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAI----PMPGLNIGYLPQEPELNPEHTVR 87
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVrkepREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEeglgavFNAkqrldevyAAYAEPDADFDALAaeqaeleaviaaaassgaDDIEHQMEIAADAlrlppwDAMVGKLS 167
Cdd:COG4555 93 ENIR------YFA--------ELYGLFDEELKKRI------------------EELIELLGLEEFL------DRRVGELS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF---PGTVVAVTHDRYFLDNAAEWILELDRGygipwk 244
Cdd:COG4555 135 TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKG------ 208
|
250 260 270
....*....|....*....|....*....|....*
gi 489917580 245 gnysswleqkedRLKQEEATESARQKTIKKELEWV 279
Cdd:COG4555 209 ------------KVVAQGSLDELREEIGEENLEDA 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-238 |
3.06e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.55 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGL----NIGYLPQEPELNPEHTVR 87
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsgevRVLGEDVARDPAevrrRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEeglgavFNAKqrldevyaAYAEPDADFDALAAEqaeleaviaaaassgaddiehqmeiAADALRLPPW-DAMVGKL 166
Cdd:COG1131 92 ENLR------FFAR--------LYGLPRKEARERIDE-------------------------LLELFGLTDAaDRKVGTL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDryfLDNA---AEWILELDRG 238
Cdd:COG1131 133 SGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY---LEEAerlCDRVAIIDKG 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-238 |
4.74e-29 |
|
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: 114.51 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGL-----------NIGYLPQEPELNP 82
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtDISKLsekelaafrrrHIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVEegLGAVFNAKQRLDevyaayaepdadfdalAAEQAE--LEAViaaaassgadDIEHQMeiaadalrlppwD 160
Cdd:cd03255 96 DLTALENVE--LPLLLAGVPKKE----------------RRERAEelLERV----------GLGDRL------------N 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 161 AMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAVTHDRyFLDNAAEWILELD 236
Cdd:cd03255 136 HYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELR 214
|
..
gi 489917580 237 RG 238
Cdd:cd03255 215 DG 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-255 |
7.76e-29 |
|
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: 120.64 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA----IPMPGLN-------IGYLPQEPelnpeHTVR 87
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggVDLRDLDeddlrrrIAVVPQRP-----HLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLgavfnakqRLdevyaayAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalRLPP-WDAMVG 164
Cdd:COG4987 423 TTLRENL--------RL-------ARPDATDEELwaALERVGLG-----------DWLA----------ALPDgLDTWLG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 ----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEQFLHKFPG-TVVAVTHDRYFLDNAAEwILELDRG 238
Cdd:COG4987 467 eggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR-ILVLEDG 545
|
250
....*....|....*..
gi 489917580 239 yGIPWKGNYSSWLEQKE 255
Cdd:COG4987 546 -RIVEQGTHEELLAQNG 561
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-514 |
1.12e-28 |
|
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: 113.37 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTvklaYVDQSRDSLEGN 404
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY----SIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 KTV---FDAVADGadlLTV-----------GKFEMPSRA----YLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIAGG 466
Cdd:cd03263 77 LGYcpqFDALFDE---LTVrehlrfyarlkGLPKSEIKEevelLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489917580 467 NVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDRIATHI 514
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-519 |
1.31e-28 |
|
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: 114.13 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG----DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KL 391
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVtrrrrkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQ-SRDSLEGNKTVFDAVADGadLLTVGKFEMPSR------------AYLGRFnfkggdqnkiVGQLSGGERGRLHL 458
Cdd:COG1124 82 QMVFQdPYASLHPRHTVDRILAEP--LRIHGLPDREERiaelleqvglppSFLDRY----------PHQLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 459 AKTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-238 |
1.38e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.18 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpmpglnigYLPQEPELNPEHTVRQSVeeglga 96
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEELRRRI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 vfnakqrldevyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdAMVGKLSGGEKRRVAL 176
Cdd:cd00267 76 ----------------------------------------------------------------GYVPQLSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
327-532 |
1.66e-28 |
|
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: 119.48 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV-----------KLAYV 394
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQS----RDSLEGNKTVFDAVADGADLLTVGKfempsRAYLGRF--------NFKGGDQNKivgQLSGGERGRLHLAKTL 462
Cdd:COG4988 417 PQNpylfAGTIRENLRLGRPDASDEELEAALE-----AAGLDEFvaalpdglDTPLGEGGR---GLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 463 IAGGNVLLLDEPSNDLDVETLRALEDALLEFPGS--VMVISHdRWFLDRIATHILAFEgDSQVVFFdGNYQE 532
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITH-RLALLAQADRILVLD-DGRIVEQ-GTHEE 557
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
327-518 |
2.00e-28 |
|
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: 112.58 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD----RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------------ 389
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 --KLAYVDQSRdSLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:cd03255 81 rrHIGFVFQSF-NLLPDLTALENVELPLLLAGVPKKERRERAEelLERVGL-GDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPG----SVMVISHDRwFLDRIATHILAFE 518
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP-ELAEYADRIIELR 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
327-532 |
2.11e-28 |
|
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: 113.20 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSLeG- 403
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKV-Gl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 404 ----------NKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKG-GDQNkiVGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:COG1122 80 vfqnpddqlfAPTVEEDVAFGPENLGLPREEIRERVeeALELVGLEHlADRP--PHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 471 LDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHILAFEgDSQVVfFDGNYQE 532
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD-DGRIV-ADGTPRE 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-511 |
2.91e-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: 118.37 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVD--KEIEGEAI--------------------PMPGLNIGYLPQE 77
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpskvgePCPVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 78 PEL-NPEHTVRQSVEEGLG-------AVFNAKQRLDEVYAAYaePDADFDALAAEQAELEAVIAAaassgadDIEHQM-E 148
Cdd:TIGR03269 94 VDFwNLSDKLRRRIRKRIAimlqrtfALYGDDTVLDNVLEAL--EEIGYEGKEAVGRAVDLIEMV-------QLSHRItH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 149 IAADalrlppwdamvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEW----LEQFLHKFPGTVVAVTHDRYF 224
Cdd:TIGR03269 165 IARD-------------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 225 LDNAAEwileldrgygipwkgnYSSWLEQKEdrLKQEEATESArqktikkelewvrqnpkgrqakakarIARFEELSSyE 304
Cdd:TIGR03269 232 IEDLSD----------------KAIWLENGE--IKEEGTPDEV--------------------------VAVFMEGVS-E 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 305 YQKRNETQeifipvgdrLGNEVIEFNHVSKAYG--DRLLI---DDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD 379
Cdd:TIGR03269 267 VEKECEVE---------VGEPIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 380 SGE--VKLGQ----TVKLAYVDQSRD-----------SLEGNKTVFDAVAD--GADLltvgKFEMPSRAYLGRFNFKGGD 440
Cdd:TIGR03269 338 SGEvnVRVGDewvdMTKPGPDGRGRAkryigilhqeyDLYPHRTVLDNLTEaiGLEL----PDELARMKAVITLKMVGFD 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 441 Q-------NKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALL----EFPGSVMVISHDRWFL-- 507
Cdd:TIGR03269 414 EekaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVld 493
|
....*.
gi 489917580 508 --DRIA 511
Cdd:TIGR03269 494 vcDRAA 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
327-557 |
6.65e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 118.13 E-value: 6.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQS--RDsLEGn 404
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRN-VEG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 kTVFDAVADG----ADLLT--------VGkfEMPSRAYLGRF---------------------NFK--GGDQNKIVGQLS 449
Cdd:PRK11147 82 -TVYDFVAEGieeqAEYLKryhdishlVE--TDPSEKNLNELaklqeqldhhnlwqlenrineVLAqlGLDPDAALSSLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 450 GGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgDSQVVFFDGN 529
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD-RGKLVSYPGN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489917580 530 YQEY----------------EADKKhrLGEE------GAKPKRL----RYKALK 557
Cdd:PRK11147 238 YDQYllekeealrveelqnaEFDRK--LAQEevwirqGIKARRTrnegRVRALK 289
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
327-514 |
7.29e-28 |
|
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: 110.77 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTVKLAYVDQSR------- 398
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRigaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 DSLEGNKTVFDAVADGADLLTVGKFEMPSraYLGRFNFKGGDQNKiVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL 478
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDE--VLDVVGLKDSAKKK-VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 489917580 479 D---VETLRALEDALLEFPGSVMVISHDRWFLDRIATHI 514
Cdd:cd03268 158 DpdgIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
327-518 |
8.73e-28 |
|
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: 109.58 E-value: 8.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------------KLAY 393
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLtdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQsRDSLEGNKTVFDAVADGadlltvgkfempsraylgrfnfkggdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:cd03229 81 VFQ-DFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 474 PSNDLDVETLRALEDALL----EFPGSVMVISHDRWFLDRIATHILAFE 518
Cdd:cd03229 127 PTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-291 |
1.09e-27 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 117.36 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 9 NRVGKIV---------PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQ-EP 78
Cdd:PRK11147 313 SRSGKIVfemenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 79 ELNPEHTVRQSVEEGLGAV-FNAKQRldevyaayaepdadfdalaaeqaeleaviaaaassgaddieHQMEIAADALrLP 157
Cdd:PRK11147 393 ELDPEKTVMDNLAEGKQEVmVNGRPR-----------------------------------------HVLGYLQDFL-FH 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 158 PWDAM--VGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAE--WIL 233
Cdd:PRK11147 431 PKRAMtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTecWIF 510
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 234 ELDrgygipwkGNYSSWLEQKEDRLKQEEATESARQKTIKKELEWVRQNPKGRQAKAK 291
Cdd:PRK11147 511 EGN--------GKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-238 |
2.49e-27 |
|
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: 116.01 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPGL-------NIGYLPQEPELnPEH 84
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSilinGVDLSDLdpaswrrQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVeeglgavfnakqRLdevyaayAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalRLPP-WDA 161
Cdd:COG4988 426 TIRENL------------RL-------GRPDASDEELeaALEAAGLD-----------EFVA----------ALPDgLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 162 MVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHDRYFLDNaAEWILEL 235
Cdd:COG4988 466 PLGeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVL 544
|
...
gi 489917580 236 DRG 238
Cdd:COG4988 545 DDG 547
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-238 |
2.70e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 108.25 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGL----NIGYLPQEPELNPEHTVR 87
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpdsgeiKVLGKDIKKEPEevkrRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVeeglgavfnakqrldevyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdamvgKLS 167
Cdd:cd03230 92 ENL--------------------------------------------------------------------------KLS 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF---PGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03230 98 GGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-519 |
2.85e-27 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 116.06 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 31 PGAKIGVLGLNGSGKSTLLKIMAGvdkeiegEAIPmpglNIG----------------------YL-------------P 75
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSG-------ELIP----NLGdyeeepswdevlkrfrgtelqnYFkklyngeikvvhkP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 76 QEPELNPEhTVRQSVEEGLGAVfNAKQRLDEVyaayaepdadfdalaAEQAELEaviaaaassgaddiehqmeiaadalr 155
Cdd:PRK13409 167 QYVDLIPK-VFKGKVRELLKKV-DERGKLDEV---------------VERLGLE-------------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 156 lPPWDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVEWLEQflHKfpgTVVAVTHDRYFLDNA 228
Cdd:PRK13409 204 -NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrlnvARLIRELAE--GK---YVLVVEHDLAVLDYL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 229 AEWILELdrgYGIPwkGNYSswleqkedrlkqeeatesarqktikkelewVRQNPKGrqakakARIARFEELSSY----- 303
Cdd:PRK13409 278 ADNVHIA---YGEP--GAYG------------------------------VVSKPKG------VRVGINEYLKGYlpeen 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 304 --------EYQKRNETQEIFIPVgdrlgneVIEFNHVSKAYGDrlliddLSFKVPAGAI-----VGIIGPNGAGKSTLFR 370
Cdd:PRK13409 317 mrirpepiEFEERPPRDESERET-------LVEYPDLTKKLGD------FSLEVEGGEIyegevIGIVGPNGIGKTTFAK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 371 MLAGREQPDSGEVKlgQTVKLAYVDQ--SRDSlegNKTVFDAVADGADLLTVGKF--EMPSRAYLGRFNfkggDQNkiVG 446
Cdd:PRK13409 384 LLAGVLKPDEGEVD--PELKISYKPQyiKPDY---DGTVEDLLRSITDDLGSSYYksEIIKPLQLERLL----DKN--VK 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 447 QLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE----TLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
327-527 |
7.79e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 108.74 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-------------KLA 392
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 YVDQSR---DSLegnkTVFDAVAdgadLLTVGKFEMPSRAYLGRFNFK------GGDQNKIVGQLSGGERGRLHLAKTLI 463
Cdd:cd03261 81 MLFQSGalfDSL----TVFENVA----FPLREHTRLSEEEIREIVLEKleavglRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALL----EFPGSVMVISHDRWFLDRIATHIlAFEGDSQVVFFD 527
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRI-AVLYDGKIVAEG 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-519 |
8.35e-27 |
|
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: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 31 PGAKIGVLGLNGSGKSTLLKIMAGvdkeiegEAIPmpglNIGYLPQEP------------ELNP------EHTVR----- 87
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG-------ELKP----NLGDYDEEPswdevlkrfrgtELQDyfkklaNGEIKvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEgLGAVFNAKQRldEVYAAYAEPDAdfdalaaeqaeleaviaaaassgADDIehqmeiaADALRLPP-WDAMVGKL 166
Cdd:COG1245 167 QYVDL-IPKVFKGTVR--ELLEKVDERGK-----------------------LDEL-------AEKLGLENiLDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVewleQFLHKFPGTVVAVTHDRYFLDNAAEWILELdrgY 239
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlnvARLI----RELAEEGKYVLVVEHDLAILDYLADYVHIL---Y 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 240 GIPwkGNYSSWLEQKEDR------LKQEEATESARqktikkelewVRQNPkgrqakakariARFEELSSYEYQKRNEtqe 313
Cdd:COG1245 287 GEP--GVYGVVSKPKSVRvginqyLDGYLPEENVR----------IRDEP-----------IEFEVHAPRREKEEET--- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 314 ifipvgdrlgneVIEFNHVSKAYGD-RLLIDdlSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLgqTVKLA 392
Cdd:COG1245 341 ------------LVEYPDLTKSYGGfSLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKIS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 YVDQ--SRDSlegNKTVFDAvadgadLLTVGKFEMPSRAY----LGRFNFKggdqnKI----VGQLSGGERGRLHLAKTL 462
Cdd:COG1245 405 YKPQyiSPDY---DGTVEEF------LRSANTDDFGSSYYkteiIKPLGLE-----KLldknVKDLSGGELQRVAIAACL 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 463 IAGGNVLLLDEPSNDLDVE----TLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-221 |
1.52e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.64 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVEE 92
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 GLgavfnakqRLDEVYAAYAEPDADfDALaaEQAELEAviaaaassgaddiehqmeiAADALrlpPWDamvgkLSGGEKR 172
Cdd:COG1116 104 GL--------ELRGVPKAERRERAR-ELL--ELVGLAG-------------------FEDAY---PHQ-----LSGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDA---ESV-EWLEQFLHKFPGTVVAVTHD 221
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDAltrERLqDELLRLWQETGKTVLFVTHD 198
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
326-532 |
2.23e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 107.76 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTV-------------KL 391
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDItglsekelyelrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQSR---DSLegnkTVFDAVAdgadlltvgkF------EMPSRAYLGRFNFK------GGDQNKIVGQLSGGERGRL 456
Cdd:COG1127 85 GMLFQGGalfDSL----TVFENVA----------FplrehtDLSEAEIRELVLEKlelvglPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 457 HLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE----FPGSVMVISHDRWFLDRIATHIlAFEGDSQVVfFDGNYQE 532
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRV-AVLADGKII-AEGTPEE 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
325-511 |
2.52e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 325 EVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAY 393
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLnGRPLAdwspaelarrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQS----------------RDSLEGNKTVFDAVADGAdLLTVGKFEMPSRAYLgrfnfkggdqnkivgQLSGGERGRLH 457
Cdd:PRK13548 81 LPQHsslsfpftveevvamgRAPHGLSRAEDDALVAAA-LAQVDLAHLAGRDYP---------------QLSGGEQQRVQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 458 LAKTLI------AGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHD-----RWfLDRIA 511
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-221 |
3.08e-26 |
|
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: 106.79 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVEEG 93
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDNVALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 LGAVFNAKQRLDEVYAAYaepdadfdalaAEQAELEaviaaaassgadDIEHQMeiaadalrlpPWDamvgkLSGGEKRR 173
Cdd:cd03293 98 LELQGVPKAEARERAEEL-----------LELVGLS------------GFENAY----------PHQ-----LSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489917580 174 VALCRLLLSKPDMLLLDEPTNHLDA---ESV-EWLEQFLHKFPGTVVAVTHD 221
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
331-523 |
3.30e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 106.19 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG--------QTVKLAYVDQSRDSL 401
Cdd:cd03226 4 NISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakeRRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGNKTVFDAVADGADLLTVGKFEmpSRAYLGRFN-FKGGDQNKIvgQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:cd03226 84 LFTDSVREELLLGLKELDAGNEQ--AETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489917580 481 ETLRALEDALLEFPG---SVMVISHDRWFLDRIATHILAFEGDSQV 523
Cdd:cd03226 160 KNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
327-503 |
4.71e-26 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 112.62 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR--LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAY 393
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDLRqidpaslrrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQS----RDSLEGNKTVFDAVADGADLLTVGKfempsRAYLGRF--NFKGGDQNKIV---GQLSGGERGRLHLAKTLIA 464
Cdd:COG2274 554 VLQDvflfSGTIRENITLGDPDATDEEIIEAAR-----LAGLHDFieALPMGYDTVVGeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHD 503
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
327-503 |
5.39e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 106.11 E-value: 5.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG-----REQPDSGEVKL-GQTV----------- 389
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -KLAYVDQSRDSLEGnkTVFDAVADGADLLTVGKFEMP--------SRAYLgrfnFKGGDQNKIVGQLSGGERGRLHLAK 460
Cdd:cd03260 81 rRVGMVFQKPNPFPG--SIYDNVAYGLRLHGIKLKEELderveealRKAAL----WDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 461 TLIAGGNVLLLDEPSNDLDVETLRALEDALLEF--PGSVMVISHD 503
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-238 |
5.64e-26 |
|
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: 106.81 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGL-----NIGYLPQEPE--LNPEH 84
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwsgevTFDGRPVTRRRRkafrrRVQMVFQDPYasLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEEGLGA--VFNAKQRLDEvyaayaepdadfdalAAEQAELeaviaaaassgaddiehqmeiAADAL-RLPpwda 161
Cdd:COG1124 97 TVDRILAEPLRIhgLPDREERIAE---------------LLEQVGL---------------------PPSFLdRYP---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 162 mvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDR 237
Cdd:COG1124 137 --HQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
.
gi 489917580 238 G 238
Cdd:COG1124 215 G 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
337-546 |
6.00e-26 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 112.19 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSLEgnKTVFDAVADG-- 414
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP--QPALEYVIDGdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 415 -------------------------ADLLTVGKFEMPSRA--YLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGN 467
Cdd:PRK10636 90 eyrqleaqlhdanerndghaiatihGKLDAIDAWTIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 468 VLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgdSQVVF-FDGNYQEYEADKKHRLGEEGA 546
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE--QQSLFeYTGNYSSFEVQRATRLAQQQA 247
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-229 |
6.18e-26 |
|
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: 104.44 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPqepelnpehtvrqsveeglga 96
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE-ILLDGKDLASLS--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 vfnAKQRLDEVyaAYAEpdadfdalaaeQAeLEaviaaaassgaddiehQMEIAADALRLppwdamVGKLSGGEKRRVAL 176
Cdd:cd03214 68 ---PKELARKI--AYVP-----------QA-LE----------------LLGLAHLADRP------FNELSGGERQRVLL 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDryfLDNAA 229
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD---LNLAA 162
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
335-503 |
9.92e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 9.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 335 AYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQ-SR--DSLEgnKTVFDAV 411
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrSEvpDSLP--LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 412 ADG-------------ADLLTVGkfEMPSRAYLGRFnfkggdQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL 478
Cdd:NF040873 79 AMGrwarrglwrrltrDDRAAVD--DALERVGLADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 489917580 479 DVETLRALEDALLEFPG---SVMVISHD 503
Cdd:NF040873 151 DAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
326-519 |
1.17e-25 |
|
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: 105.36 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDR----LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKL----AYVDQ 396
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRD--------SLEGNKTVFDAVADGADLLTVGKFEMPSRAY-LGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGN 467
Cdd:cd03258 81 RRRigmifqhfNLLSSRTVFENVALPLEIAGVPKAEIEERVLeLLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 468 VLLLDEPSNDLDVETLRALEDALL----EFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
327-532 |
1.46e-25 |
|
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: 110.63 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY--GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG---------QTV--KLAY 393
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQS----RDSLEGNKTVFDAVADGADLLTVGKfempsRAYLGRFnFKGGDQ--NKIVG----QLSGGERGRLHLAKTLI 463
Cdd:COG4987 414 VPQRphlfDTTLRENLRLARPDATDEELWAALE-----RVGLGDW-LAALPDglDTWLGeggrRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALLE-FPG-SVMVISHDRWFLDRiATHILAFEgDSQVVfFDGNYQE 532
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEaLAGrTVLLITHRLAGLER-MDRILVLE-DGRIV-EQGTHEE 555
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
327-526 |
2.46e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.78 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYVD 395
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QSrDSLEGNKTVFDAVAdgadlltvgkfempsrayLGRFNFKGG-----DQNKI----------------VGQLSGGERG 454
Cdd:COG4604 82 QE-NHINSRLTVRELVA------------------FGRFPYSKGrltaeDREIIdeaiayldledladryLDELSGGQRQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 455 RLHLAKTLIAGGNVLLLDEPSNDLD----VETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgDSQVVFF 526
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMK-DGRVVAQ 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
327-538 |
3.49e-25 |
|
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: 104.06 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG-------------------- 386
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglppheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 387 -QTVKLAyvdqsrdsleGNKTVFDAVADGADLLTVGKF----------EMPSRA--YLGRFNFkGGDQNKIVGQLSGGER 453
Cdd:cd03219 81 fQIPRLF----------PELTVLENVMVAAQARTGSGLllararreerEARERAeeLLERVGL-ADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 454 GRLHLAKTLIAGGNVLLLDEPS---NDLDVETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFegDSQVVFFDGNY 530
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL--DQGRVIAEGTP 227
|
....*...
gi 489917580 531 QEYEADKK 538
Cdd:cd03219 228 DEVRNNPR 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
327-515 |
4.06e-25 |
|
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: 103.13 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTV------KLAYVDQSRd 399
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLdiaarnRIGYLPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 SLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSND 477
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIdeWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 478 LDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHIL 515
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVL 199
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
326-546 |
6.44e-25 |
|
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: 103.97 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV----------------KLG--- 386
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditglpphriaRLGiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 387 --QTVKLAyvdqsrdsleGNKTVFDAVADGADLLTVGKF---------------EMPSRAY--LGRFNFkGGDQNKIVGQ 447
Cdd:COG0411 84 tfQNPRLF----------PELTVLENVLVAAHARLGRGLlaallrlprarreerEARERAEelLERVGL-ADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 448 LSGGERGRLHLAKTLIAGGNVLLLDEP--------SNDLdVETLRALEDallEFPGSVMVISHDRWFLDRIATHILAFeg 519
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLRD---ERGITILLIEHDMDLVMGLADRIVVL-- 226
|
250 260 270
....*....|....*....|....*....|
gi 489917580 520 DSQVVFFDGNYQEYEADKKHR---LGEEGA 546
Cdd:COG0411 227 DFGRVIAEGTPAEVRADPRVIeayLGEEAA 256
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-221 |
7.22e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPELNPEH--TVRQSVEEGL 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 GAVFNAKQRLDEvyAAYAEPDADFDALAAeqAELEaviaaaassgaddiehqmeiaadalrlppwDAMVGKLSGGEKRRV 174
Cdd:NF040873 83 WARRGLWRRLTR--DDRAAVDDALERVGL--ADLA------------------------------GRQLGELSGGQRQRA 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL---HKFPGTVVAVTHD 221
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLaeeHARGATVVVVTHD 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
327-504 |
8.55e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.61 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVklAYVDQS-RDS----- 400
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD--LFTNLPpRERrvgfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 -----LEGNKTVFDAVADGadlLTVGKfemPSRA--------YLGRFNFKG-GDQnkIVGQLSGGERGRLHLAKTLIAGG 466
Cdd:COG1118 81 fqhyaLFPHMTVAENIAFG---LRVRP---PSKAeirarveeLLELVQLEGlADR--YPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 467 NVLLLDEPSNDLDVETLRALEDALL----EFPGSVMVISHDR 504
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQ 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
327-511 |
9.19e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.57 E-value: 9.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------KLAYVDQS 397
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdGRDVtglppekrNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 rDSLEGNKTVFDAVADGADLLTVGKFEMPSRA-----------YLGRFnfkggdqnkiVGQLSGGERGRLHLAKTLIAGG 466
Cdd:COG3842 86 -YALFPHLTVAENVAFGLRMRGVPKAEIRARVaellelvglegLADRY----------PHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 467 NVLLLDEP-SNdLDVET-------LRALEDALlefpG--SVMViSHDR----WFLDRIA 511
Cdd:COG3842 155 RVLLLDEPlSA-LDAKLreemreeLRRLQREL----GitFIYV-THDQeealALADRIA 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-254 |
1.39e-24 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 107.28 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPElnpehtvrqsveeglgAV 97
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHA----------------YD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 FNAKQRLDEVYAAYAEPDADFDALAAEQAELeaviaaaaSSGADDIEHQmeiaadalrlppwdamVGKLSGGEKRRVALC 177
Cdd:PRK15064 395 FENDLTLFDWMSQWRQEGDDEQAVRGTLGRL--------LFSQDDIKKS----------------VKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 178 RLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGIPWKGNYSSWLEQK 254
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
326-493 |
2.02e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.65 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQ------SR 398
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 dSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSN 476
Cdd:COG4152 81 -GLYPKMKVGEQLVYLARLKGLSKAEAKRRAdeWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170
....*....|....*..
gi 489917580 477 DLDVETLRALEDALLEF 493
Cdd:COG4152 159 GLDPVNVELLKDVIREL 175
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-221 |
3.91e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 105.76 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIP-MPGL-------NIGYLPQEPE-- 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsiLFDGKDLTkLSRRslrelrrRVQMVFQDPYss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 LNPEHTVRQSVEEGLGA--VFNAKQRLDEVYAayaepdadfdalAAEQAELEaviaaaassgaddiehqmeiaADALRLP 157
Cdd:COG1123 355 LNPRMTVGDIIAEPLRLhgLLSRAERRERVAE------------LLERVGLP---------------------PDLADRY 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 158 PWDamvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:COG1123 402 PHE-----LSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDLQRELGLTYLFISHD 464
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
324-502 |
4.46e-24 |
|
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: 101.31 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV------KLGQTV------KL 391
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDvwelrkRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQS-RDSLEGNKTVFDAVADGA-DllTVGKFEMPS-------RAYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTL 462
Cdd:COG1119 81 GLVSPAlQLRFPRDETVLDVVLSGFfD--SIGLYREPTdeqreraRELLELLGL-AHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 463 IAGGNVLLLDEPSNDLDV---ETLRALEDALLEFPGSVMV-ISH 502
Cdd:COG1119 158 VKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
289-486 |
4.53e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.37 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 289 KAKARIA-RFEELSSYEYQKRNETQEIFIPVGDrLGNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKST 367
Cdd:PRK13536 4 RAVAEEApRRLELSPIERKHQGISEAKASIPGS-MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 368 LFRMLAGREQPDSGEVK-LGQTV---------KLAYVDQSrDSLEGNKTVFDavadgaDLLTVGKF----------EMPS 427
Cdd:PRK13536 83 IARMILGMTSPDAGKITvLGVPVpararlaraRIGVVPQF-DNLDLEFTVRE------NLLVFGRYfgmstreieaVIPS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 428 RAYLGRFNFKGgdqNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV-------ETLRAL 486
Cdd:PRK13536 156 LLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhliwERLRSL 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-238 |
5.82e-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: 98.61 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGL-----NIGYLPQEPELnpehtVR 87
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDptsgeiLIDGVDLRDLDLeslrkNIAYVPQDPFL-----FS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLgavfnakqrldevyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdamvgkLS 167
Cdd:cd03228 90 GTIRENI-----------------------------------------------------------------------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHdRYFLDNAAEWILELDRG 238
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-238 |
6.30e-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: 99.97 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGL------------NIGYLPQEPELnpehtvrqs 89
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSG-SVLLDGTdirqldpadlrrNIGYVPQDVTL--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 veeglgavFNAKQRlDEVyaAYAEPDADfDALAAEQAELEAviaaaassgaddiehqmeiAADALRLPP--WDAMVGK-- 165
Cdd:cd03245 90 --------FYGTLR-DNI--TLGAPLAD-DERILRAAELAG-------------------VTDFVNKHPngLDLQIGErg 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 166 --LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHdRYFLDNAAEWILELDRG 238
Cdd:cd03245 139 rgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-222 |
7.01e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.92 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGE----AIPMPGLNIGYLPQEPELNPEHTV 86
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRdlftNLPPRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGLgavfnaKQRldevyaayAEPDADFDALAAEQAELeaviaaaassgaddieHQMEIAADalRLPpwdamvGKL 166
Cdd:COG1118 93 AENIAFGL------RVR--------PPSKAEIRARVEELLEL----------------VQLEGLAD--RYP------SQL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSV-----EWLEQFLHKFPGTVVAVTHDR 222
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-474 |
8.60e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 8.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DK---EIEGEAIPMPG------LNIGYLPQEPELNPEHTVRQS 89
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVyqpDSgeiLLDGEPVRFRSprdaqaAGIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VeeGLGAVFNAKQRLD--EVYAAYAEpdadfdALAaeqaELEaviaaaassgaddiehqmeiaadaLRLPPwDAMVGKLS 167
Cdd:COG1129 100 I--FLGREPRRGGLIDwrAMRRRARE------LLA----RLG------------------------LDIDP-DTPVGDLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHdryFLDnaaEwILEL-DR------ 237
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH---RLD---E-VFEIaDRvtvlrd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 238 GygipwkgnysswleQKEDRLKQEEATEsarqktikkelewvrqnpkgrqakakARIARF---EELSSYEYQKRNETqei 314
Cdd:COG1129 216 G--------------RLVGTGPVAELTE--------------------------DELVRLmvgRELEDLFPKRAAAP--- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 315 fipvgdrlGNEVIEFNHVSKAYGdrllIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK--- 390
Cdd:COG1129 253 --------GEVVLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRirs 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 --------LAYV--DQSRDSLEGNKTV--------FDAVADGAdLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGE 452
Cdd:COG1129 321 prdairagIAYVpeDRKGEGLVLDLSIrenitlasLDRLSRGG-LLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
490 500
....*....|....*....|..
gi 489917580 453 RGRLHLAKTLIAGGNVLLLDEP 474
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEP 421
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
327-511 |
1.11e-23 |
|
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: 99.37 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGE--------VKLGQTVK--LAYVDQ 396
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRrrIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRdSLEGNKTVFDAVADGADLLTVGKFEMPSRA-----YLGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIAGGNVLLL 471
Cdd:cd03265 81 DL-SVDDELTGWENLYIHARLYGVPGAERRERIdelldFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489917580 472 DEPSNDLDVET----LRALEDALLEFPGSVMVISHD----RWFLDRIA 511
Cdd:cd03265 156 DEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYmeeaEQLCDRVA 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-238 |
1.17e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-AIPmPGLNIGYLPQEPELnPEHTVRQSVeegl 94
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARP-AGARVLFLPQRPYL-PLGTLREAL---- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 gavfnakqrldevyaAYAEPDADFD--ALAA--EQAELeaviaaaassgaDDIEHQMEIAADalrlppWDAMvgkLSGGE 170
Cdd:COG4178 447 ---------------LYPATAEAFSdaELREalEAVGL------------GHLAERLDEEAD------WDQV---LSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL-EQFLHKFPG-TVVAVTHdRYFLDNAAEWILELDRG 238
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALyQLLREELPGtTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
326-519 |
1.50e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-------------K 390
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 LAYVDQsrD-SLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGN 467
Cdd:COG2884 81 IGVVFQ--DfRLLPDRTVYENVALPLRVTGKSRKEIRRRVRevLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 468 VLLLDEPSNDLDVETLRALEDALLEF--PG-SVMVISHDRWFLDRIATHILAFEG 519
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLELED 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
327-503 |
2.41e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.42 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYVD 395
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLnGRPLaawspwelarRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QS----------------RDSLEGNKTVFDAVADGAdLLTVGKFEMPSRAYLgrfnfkggdqnkivgQLSGGERGRLHLA 459
Cdd:COG4559 82 QHsslafpftveevvalgRAPHGSSAAQDRQIVREA-LALVGLAHLAGRSYQ---------------TLSGGEQQRVQLA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 460 KTLI-------AGGNVLLLDEPSNDLDV----ETLRALEDaLLEFPGSVMVISHD 503
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQ-LARRGGGVVAVLHD 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
327-518 |
2.49e-23 |
|
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: 98.25 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------KLAYVDQS- 397
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 ----RDS-LEGNKTVFDAVADGADLLTVGKFEMPSR--AYLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:cd03292 81 gvvfQDFrLLPDRNVYENVAFALEVTGVPPREIRKRvpAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 471 LDEPSNDLDVETLRALEDALLEFP---GSVMVISHDRWFLDRIATHILAFE 518
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALE 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-221 |
2.98e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.19 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLN-----------IGYLPQEPELNP 82
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqDISSLSerelarlrrrhIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVEegLGAVFNAKQRldevyaayAEPDADFDALaaeqaeLEAViaaaassgadDIEHQMeiaadalrlppwDAM 162
Cdd:COG1136 100 ELTALENVA--LPLLLAGVSR--------KERRERAREL------LERV----------GLGDRL------------DHR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 163 VGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEQF--LHKFPG-TVVAVTHD 221
Cdd:COG1136 142 PSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKtGEEVLELLreLNRELGtTIVMVTHD 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
327-504 |
3.23e-23 |
|
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: 103.14 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR-LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYV 394
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQS----RDSLEGNKTVFDAVADGADLLtvgkfEMPSRAYLGRF-NFKGGDQNKIVGQ----LSGGERGRLHLAKTLIAG 465
Cdd:TIGR02857 402 PQHpflfAGTIAENIRLARPDASDAEIR-----EALERAGLDEFvAALPQGLDTPIGEggagLSGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDR 504
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
326-479 |
5.13e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-KLAYVDQSR----- 398
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpSRARHARQRvgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 --DSLEGNKTVFDavadgaDLLTVGKF----------EMPSRAYLGRFNFKGGDQnkiVGQLSGGERGRLHLAKTLIAGG 466
Cdd:PRK13537 87 qfDNLDPDFTVRE------NLLVFGRYfglsaaaaraLVPPLLEFAKLENKADAK---VGELSGGMKRRLTLARALVNDP 157
|
170
....*....|...
gi 489917580 467 NVLLLDEPSNDLD 479
Cdd:PRK13537 158 DVLVLDEPTTGLD 170
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
324-524 |
6.46e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.42 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLL----IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------- 389
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDIsslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -----KLAYVDQSR---DSLegnkTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkGGDQNKIVGQLSGGERGRLHLA 459
Cdd:COG1136 82 rlrrrHIGFVFQFFnllPEL----TALENVALPLLLAGVSRKERRERAreLLERVGL-GDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 460 KTLIAGGNVLLLDEPSNDLDVET----LRALEDALLEFPGSVMVISHDRwFLDRIATHILAFEgDSQVV 524
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLR-DGRIV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-221 |
7.90e-23 |
|
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: 96.60 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSF-FPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------------IPMPGLNIGYLPQEPELN 81
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 82 PEHTVRQSVEEGLGAVFNAKQRLdevyaayaEPDADFDALAAEQAEleaviaaaassgaddiehqmeiaadalrlppwDA 161
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRI--------SVDELLDLLGLDHLL--------------------------------NR 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 162 MVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHK----FPGTVVAVTHD 221
Cdd:cd03297 128 YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
327-502 |
9.13e-23 |
|
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: 94.80 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAyvdqsrdslegnk 405
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 TVFDAVADGadlltVGkfempsraylgrfnfkggdqnkIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV----- 480
Cdd:cd03216 68 SPRDARRAG-----IA----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPaever 120
|
170 180
....*....|....*....|....*
gi 489917580 481 --ETLRALEDAllefpG-SVMVISH 502
Cdd:cd03216 121 lfKVIRRLRAQ-----GvAVIFISH 140
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-222 |
1.07e-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: 96.43 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------AIPMPGLNIGYLPQEPELNPEHTVRQSV 90
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEGLgavfnaKQRLdevyaayaEPDADFDALAAEQAELeaviaaaassgaddiehqMEIAADALRLPpwdamvGKLSGGE 170
Cdd:cd03259 94 AFGL------KLRG--------VPKAEIRARVRELLEL------------------VGLEGLLNRYP------HELSGGQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL---HKFPG-TVVAVTHDR 222
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREELkelQRELGiTTIYVTHDQ 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
327-512 |
1.12e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.78 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAYV 394
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdGVDIRdltleslrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQS----RDSLEGNKTVFDAVADGADLLTVGKfempsRAYLGRF--NFKGG-DQnkIVGQ----LSGGERGRLHLAKTLI 463
Cdd:COG1132 420 PQDtflfSGTIRENIRYGRPDATDEEVEEAAK-----AAQAHEFieALPDGyDT--VVGErgvnLSGGQRQRIAIARALL 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALLEFPGS--VMVISHdrwfldRIAT 512
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH------RLST 537
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
327-492 |
1.14e-22 |
|
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: 96.92 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------KLAYVDQS 397
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDItnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RdSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPS 475
Cdd:cd03300 81 Y-ALFPHLTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170
....*....|....*..
gi 489917580 476 NDLDVEtLRalEDALLE 492
Cdd:cd03300 159 GALDLK-LR--KDMQLE 172
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-238 |
2.61e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.59 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 14 IVPP--KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------------------DKEIEGEaipmpglNIGY 73
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwpptagsvrldgadlsqwDREELGR-------HIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 74 LPQEPELNPEhTVRQSVeeglgAVFnakqrldevyaayaePDADFDAL--AAEQAELeaviaaaassgaddieHQMeIaa 151
Cdd:COG4618 411 LPQDVELFDG-TIAENI-----ARF---------------GDADPEKVvaAAKLAGV----------------HEM-I-- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 152 daLRLPP-WDAMVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF---PGTVVAVTHDRY 223
Cdd:COG4618 451 --LRLPDgYDTRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPS 528
|
250
....*....|....*
gi 489917580 224 FLdNAAEWILELDRG 238
Cdd:COG4618 529 LL-AAVDKLLVLRDG 542
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
327-502 |
2.86e-22 |
|
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: 95.76 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAYV 394
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIRevtldslrraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQsrDSLEGNKTVFDAVADGAdlLTVGKFEMPSRAYLGRF-----NFKGGdQNKIVGQ----LSGGERGRLHLAKTLIAG 465
Cdd:cd03253 81 PQ--DTVLFNDTIGYNIRYGR--PDATDEEVIEAAKAAQIhdkimRFPDG-YDTIVGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPGS--VMVISH 502
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-221 |
3.00e-22 |
|
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: 95.27 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMP--------------GLNIGYLPQEP--ELN 81
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirRKEIQMVFQDPmsSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 82 PEHTVRQSVEEGLGAVFNakqrldevyaayaePDADFDALAAEQAELEaviaaaassgaddiehQMEIAADALRLPPwda 161
Cdd:cd03257 97 PRMTIGEQIAEPLRIHGK--------------LSKKEARKEAVLLLLV----------------GVGLPEEVLNRYP--- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 162 mvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSVEW--LEQFLH---KFPGTVVAVTHD 221
Cdd:cd03257 144 --HELSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQAqiLDLLKKlqeELGLTLLFITHD 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
327-486 |
3.30e-22 |
|
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: 95.48 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG---------QTVKLAYVDQS 397
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RdSLEGNKTVFDAVADGadLLTVGKFEMPSRAYLGR-----FNFKGGD--QNKIVGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:cd03296 83 Y-ALFRHMTVFDNVAFG--LRVKPRSERPPEAEIRAkvhelLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170
....*....|....*.
gi 489917580 471 LDEPSNDLDVETLRAL 486
Cdd:cd03296 160 LDEPFGALDAKVRKEL 175
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
327-528 |
6.21e-22 |
|
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: 94.13 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------------KLAY 393
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQSRDsLEGNKTVFDAVADGadLLTVGKfeMP-------SRAYLGRFNFKggDQ-NKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:cd03262 81 VFQQFN-LFPHLTVLENITLA--PIKVKG--MSkaeaeerALELLEKVGLA--DKaDAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFP--GSVMVI-SHDRWFLDRIATHilafegdsqVVFFDG 528
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAeeGMTMVVvTHEMGFAREVADR---------VIFMDD 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
327-479 |
8.88e-22 |
|
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: 93.86 E-value: 8.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------KLAYVDQS 397
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlppkdrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RdSLEGNKTVFDAVADGADLLTVGKFEMPSR-----------AYLGRFnfkggdqnkiVGQLSGGERGRLHLAKTLIAGG 466
Cdd:cd03301 81 Y-ALYPHMTVYDNIAFGLKLRKVPKDEIDERvrevaellqieHLLDRK----------PKQLSGGQRQRVALGRAIVREP 149
|
170
....*....|...
gi 489917580 467 NVLLLDEPSNDLD 479
Cdd:cd03301 150 KVFLMDEPLSNLD 162
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
327-527 |
1.18e-21 |
|
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: 92.38 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG--DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRdslegn 404
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 ktvfdavadgaDLLTVgkfeMPSRAYLgrfnFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLR 484
Cdd:cd03247 75 -----------SLISV----LNQRPYL----FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 485 ALEDALLEF--PGSVMVISHdrwfldriatHILAFEGDSQVVFFD 527
Cdd:cd03247 136 QLLSLIFEVlkDKTLIWITH----------HLTGIEHMDKILFLE 170
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
342-503 |
1.30e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.94 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK--------------------LGQTVKLAYVDQSRDSL 401
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrrkkflrrigvvFGQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGNKTVFDA--------VADGADLLTVGKF-EMPSRaylgrfnfkggdqnkivgQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:cd03267 117 YLLAAIYDLpparfkkrLDELSELLDLEELlDTPVR------------------QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 473 EPSNDLDV---ETLRA-LEDALLEFPGSVMVISHD 503
Cdd:cd03267 179 EPTIGLDVvaqENIRNfLKEYNRERGTTVLLTSHY 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
327-541 |
1.39e-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: 93.79 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG----QTVKLAYVDQSRD-- 399
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 -------SLEGNKTVFDAVADGAdLLTVGKFempsRAYLGRFN-------FKGGDQ-------NKIVGQLSGGERGRLHL 458
Cdd:cd03256 81 gmifqqfNLIERLSVLENVLSGR-LGRRSTW----RSLFGLFPkeekqraLAALERvglldkaYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 459 AKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFP---GSVMVIS-HDRWFLDRIATHILAFEgDSQVVfFDGNYQEYE 534
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQVDLAREYADRIVGLK-DGRIV-FDGPPAELT 233
|
....*..
gi 489917580 535 ADKKHRL 541
Cdd:cd03256 234 DEVLDEI 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
327-502 |
1.91e-21 |
|
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: 91.51 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLgqtvklayvdqsrdslegn 404
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 ktvfdavaDGADLLTVGkfempsRAYLGRFN---------FKGGDQNKIvgqLSGGERGRLHLAKTLIAGGNVLLLDEPS 475
Cdd:cd03246 62 --------DGADISQWD------PNELGDHVgylpqddelFSGSIAENI---LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|
gi 489917580 476 NDLDVETLRALEDALLEFP---GSVMVISH 502
Cdd:cd03246 125 SHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
326-515 |
1.96e-21 |
|
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: 92.95 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLL----IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQtvKLAYVDQSRDS 400
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGK--DLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNK----------------TVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGD----QNKIVGQLSGGERGRLHLAK 460
Cdd:cd03257 79 IRRKEiqmvfqdpmsslnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeevLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 461 TLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHDRWFLDRIATHIL 515
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
327-485 |
2.28e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.53 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------KLAYVDQS 397
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 rDSLEGNKTVFD------------------AVADGADLLTVGkfempsrAYLGRFnfkggdqnkiVGQLSGGERGRLHLA 459
Cdd:COG3839 84 -YALYPHMTVYEniafplklrkvpkaeidrRVREAAELLGLE-------DLLDRK----------PKQLSGGQRQRVALG 145
|
170 180
....*....|....*....|....*..
gi 489917580 460 KTLIAGGNVLLLDEP-SNdLDVEtLRA 485
Cdd:COG3839 146 RALVREPKVFLLDEPlSN-LDAK-LRV 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-238 |
2.83e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.42 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 8 MNRVGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI------------PMPGL--NIGY 73
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlkrrEIPYLrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 74 LPQEPELNPEHTVRQSVeeglgavfnakqrldevyaayaepdadfdALAAEQAELEAviaaaassgaDDIEHQMEiaaDA 153
Cdd:COG2884 84 VFQDFRLLPDRTVYENV-----------------------------ALPLRVTGKSR----------KEIRRRVR---EV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 154 LRlppW-------DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEQF--LHKFPGTVVAVTHDRY 223
Cdd:COG2884 122 LD---LvglsdkaKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIMELLeeINRRGTTVLIATHDLE 198
|
250
....*....|....*
gi 489917580 224 FLDNAAEWILELDRG 238
Cdd:COG2884 199 LVDRMPKRVLELEDG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-238 |
4.43e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.77 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMA-------------GVD-KEIEGEAipmpgL--NIGYLPQEPE 79
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDiRDLTLES-----LrrQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 LnpehtvrqsveeglgavFNakqrlDEVYA--AYAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalR 155
Cdd:COG1132 425 L-----------------FS-----GTIREniRYGRPDATDEEVeeAAKAAQAH-----------EFIE----------A 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 156 LPP-WDAMVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTH-------- 220
Cdd:COG1132 462 LPDgYDTVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAHrlstirna 541
|
250
....*....|....*...
gi 489917580 221 DRyfldnaaewILELDRG 238
Cdd:COG1132 542 DR---------ILVLDDG 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-237 |
5.20e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.59 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPGLN-------IGYLPQEPELnPEH 84
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavnGVPLADADadswrdqIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVeeglgavfnakqrldevyaAYAEPDADFDAL--AAEQAELeaviaaaassgaddiehqMEIAADalrLPP-WDA 161
Cdd:TIGR02857 411 TIAENI-------------------RLARPDASDAEIreALERAGL------------------DEFVAA---LPQgLDT 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 162 MVGK----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEQFLHKFPG-TVVAVTHDRyfldnaaEWILEL 235
Cdd:TIGR02857 451 PIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRL-------ALAALA 523
|
..
gi 489917580 236 DR 237
Cdd:TIGR02857 524 DR 525
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-238 |
5.49e-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: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNI---------GYLPQEPELNP-EHT 85
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS-ILLNGKPIkakerrksiGYVMQDVDYQLfTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGAVFNAKQRLDEVyaayaepdadfdalaaeqaeLEAviaaaassgaddiehqMEIAADALRLPpWDamvgk 165
Cdd:cd03226 89 VREELLLGLKELDAGNEQAETV--------------------LKD----------------LDLYALKERHP-LS----- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVE----WLEQfLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03226 127 LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMErvgeLIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
327-510 |
5.80e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.50 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL------------------- 385
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlrrnigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 386 -GQTVKLAYvdqsrDSLEGNKTVFDAVADGADLLTVGKFempsrayLGRFNFKGGDQNKI---VG----QLSGGERGRLH 457
Cdd:cd03245 83 vPQDVTLFY-----GTLRDNITLGAPLADDERILRAAEL-------AGVTDFVNKHPNGLdlqIGergrGLSGGQRQAVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFL---DRI 510
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
327-504 |
8.11e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 8.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------KLAYVDQS 397
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RdSLEGNKTVFDAVADGadlLTV-GKFEMPSRAYLGRFNFKGGDQ-------NKIVGQLSGGERGRLHLAKTLIAGGNVL 469
Cdd:PRK10851 83 Y-ALFRHMTVFDNIAFG---LTVlPRRERPNAAAIKAKVTQLLEMvqlahlaDRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 470 LLDEPSNDLDVET-------LRALEDAlLEFPgSVMViSHDR 504
Cdd:PRK10851 159 LLDEPFGALDAQVrkelrrwLRQLHEE-LKFT-SVFV-THDQ 197
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
327-515 |
1.00e-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: 90.72 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGaIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK---------LAYVDQ 396
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 sRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:cd03264 80 -EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVdeVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 475 SNDLDVETLRALEDALLEFPGSVMVIshdrwfldrIATHIL 515
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVI---------LSTHIV 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-492 |
1.20e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.63 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVdQSRD--- 399
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSI-QQRDicm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 -----SLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:PRK11432 83 vfqsyALFPHMSLGENVGYGLKMLGVPKEERKQRVkeALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180
....*....|....*....|
gi 489917580 473 EPSNDLDVETLRALEDALLE 492
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRE 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
333-519 |
1.45e-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: 90.93 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 333 SKAYGD-RLLIDDLSFKvpAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLgQTVKLAYVDQ--SRDSlEGnkTVFD 409
Cdd:cd03237 7 KKTLGEfTLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQyiKADY-EG--TVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 410 AVAD-GADLLTVGKFE-------MPSRAYlgrfnfkggDQNkiVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE 481
Cdd:cd03237 81 LLSSiTKDFYTHPYFKteiakplQIEQIL---------DRE--VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 482 ----TLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:cd03237 150 qrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
331-474 |
2.82e-20 |
|
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: 89.91 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQT------------VKLAYVDQsR 398
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLPQ-E 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 399 DSLEGNKTVFDAVADGADLLTVGKFEMPSR--AYLGRFNFKGGDQNKiVGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKleELLEEFHITHLRKSK-ASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
331-474 |
5.20e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.32 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK-----------LAYVDQSR 398
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 dSLEGNKTVFD---AVadgADLLTVGKFEMPSR--AYLGRFNF------KGgdqnkivGQLSGGERGRLHLAKTLIAGGN 467
Cdd:COG1137 88 -SIFRKLTVEDnilAV---LELRKLSKKEREERleELLEEFGIthlrksKA-------YSLSGGERRRVEIARALATNPK 156
|
....*..
gi 489917580 468 VLLLDEP 474
Cdd:COG1137 157 FILLDEP 163
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
330-519 |
8.33e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.46 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 330 NHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLaGREQPDS-GEVKLGQTV-----------KLAYVDQS 397
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDAQPleswsskafarKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RDSLEGnKTVFDAVAdgadlltVGKFemPSRAYLGRFNFKGGDQ--------------NKIVGQLSGGERGRLHLAKTLI 463
Cdd:PRK10575 94 LPAAEG-MTVRELVA-------IGRY--PWHGALGRFGAADREKveeaislvglkplaHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 464 AGGNVLLLDEPSNDLD----VETLrALEDALLEFPG-SVMVISHDRWFLDRIATHILAFEG 519
Cdd:PRK10575 164 QDSRCLLLDEPTSALDiahqVDVL-ALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRG 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
344-525 |
8.85e-20 |
|
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: 88.12 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKVPAGaIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------------KLAYVDQSRdSLEGNKTVF 408
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQY-ALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 409 DAVADGADLLTVGKFEMPSRAYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET----LR 484
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 485 ALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgDSQVVF 525
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME-DGRLQY 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
326-502 |
9.47e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAyvdQSRDSLE-- 402
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIR---SPRDAIAlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 -----------GNKTVFDAVADGADLLTVGKFEMPS-----RAYLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIAGG 466
Cdd:COG3845 82 igmvhqhfmlvPNLTVAENIVLGLEPTKGGRLDRKAarariRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 467 NVLLLDEP--------SNDLdVETLRALEDAllefpG-SVMVISH 502
Cdd:COG3845 161 RILILDEPtavltpqeADEL-FEILRRLAAE-----GkSIIFITH 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
327-515 |
1.14e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.27 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSL---E 402
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLTALPPAERPVSMlfqE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 GN----KTVFDAVADG--ADL-LTVGKFEMPSRAyLGRFNFKGGDQNKiVGQLSGGERGRLHLAKTLIAGGNVLLLDEPS 475
Cdd:COG3840 80 NNlfphLTVAQNIGLGlrPGLkLTAEQRAQVEQA-LERVGLAGLLDRL-PGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489917580 476 NDLD----VETLRALEDALLEFPGSVMVISHDrwfLD---RIATHIL 515
Cdd:COG3840 158 SALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVL 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
337-502 |
1.25e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 87.16 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVklayVDQSRDSLE----------GNKT 406
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP----LDFQRDSIArgllylghapGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 407 VFDAVAD----GADLLTVGKFEMPSRAYLGRFnfkggdQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 482
Cdd:cd03231 87 TLSVLENlrfwHADHSDEQVEEALARVGLNGF------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 489917580 483 LRALEDAL---LEFPGSVMVISH 502
Cdd:cd03231 161 VARFAEAMaghCARGGMVVLTTH 183
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-222 |
1.64e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEaiPMPGL-----NIGYLPQEPELNPEHTVRQ 88
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdsgriLLDGR--DVTGLppekrNVGMVFQDYALFPHLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEEGLgavfnaKQRldevyaayAEPDADFDALAAEQAELeaviaaaassgaddiehqMEIAADALRLPpwdamvGKLSG 168
Cdd:COG3842 97 NVAFGL------RMR--------GVPKAEIRARVAELLEL------------------VGLEGLADRYP------HQLSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDA---ESV-EWLEQFLHKFPGTVVAVTHDR 222
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
327-490 |
1.81e-19 |
|
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: 87.04 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR----LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGevklgqTVKLAYVDQSRDSLE 402
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 ---------GNKTVFDAVADGADLLTVGKFE-MPSRAYLGRFNfKGGDQ-------NKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:cd03266 76 arrrlgfvsDSTGLYDRLTARENLEYFAGLYgLKGDELTARLE-ELADRlgmeellDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180
....*....|....*....|....*
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDAL 490
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFI 179
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-238 |
1.95e-19 |
|
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: 87.95 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIP-------MP----GLNIGYLPQEPELNPEHTVR 87
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhgLSrrarARRVALVEQDSDTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGlgavfnakqRLDEVYAAYAEPDADFDALAAEQAeleaviaaaassgaddiehQMEIAADALRlpPWDAmvgkLS 167
Cdd:TIGR03873 94 DVVALG---------RIPHRSLWAGDSPHDAAVVDRALA-------------------RTELSHLADR--DMST----LS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:TIGR03873 140 GGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGG 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
336-533 |
2.04e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 91.49 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 336 YGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSLEgNKTVFDAV---- 411
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFE-EFTVLDTVimgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 412 ---------------------ADG---ADLltVGKF-EM-----PSRAylGRFNFKGG---DQ-NKIVGQLSGGERGRLH 457
Cdd:PRK15064 90 telwevkqerdriyalpemseEDGmkvADL--EVKFaEMdgytaEARA--GELLLGVGipeEQhYGLMSEVAPGWKLRVL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFE-GDSQVvfFDGNYQEY 533
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDyGELRV--YPGNYDEY 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
326-528 |
2.41e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 87.36 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------------KLA 392
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdGEDLtdskkdinklrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 YVDQSRdSLEGNKTVFDAVADGadLLTVGKfeMP-------SRAYLGRFnfkG-GDQ-NKIVGQLSGGERGRLHLAKTLI 463
Cdd:COG1126 81 MVFQQF-NLFPHLTVLENVTLA--PIKVKK--MSkaeaeerAMELLERV---GlADKaDAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 464 AGGNVLLLDEPSNDLDVET----LRALEDALLEfpGSVMVishdrwfldrIATHILAFEGD--SQVVFFDG 528
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELvgevLDVMRDLAKE--GMTMV----------VVTHEMGFAREvaDRVVFMDG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
326-503 |
2.64e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQsrdslegnK 405
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ--------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 TVFDAVADgadlLTVGKFEMPsraylgRFNFKGGD-------------QNKIVGQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:PRK09544 76 LYLDTTLP----LTVNRFLRL------RPGTKKEDilpalkrvqaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 473 EPSNDLDVETLRALEDAL----LEFPGSVMVISHD 503
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIdqlrRELDCAVLMVSHD 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-193 |
2.65e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 86.72 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIP------MPGLNIGYLPQEPELNPEHTVR 87
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPprsgsiRFDGRDITglppheRARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLGAVFNA--KQRLDEVYAAyaepdadFDALAaeqaeleaviaaaassgaddiehQMeiaadalrlppWDAMVGK 165
Cdd:cd03224 94 ENLLLGAYARRRAkrKARLERVYEL-------FPRLK-----------------------ER-----------RKQLAGT 132
|
170 180
....*....|....*....|....*...
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPT 193
Cdd:cd03224 133 LSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
337-488 |
2.80e-19 |
|
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: 86.07 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGR--EQPDSGEVKL-GQTVKL-------AYVDQSrDSLEGNKT 406
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLInGRPLDKrsfrkiiGYVPQD-DILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 407 VFDAVADGADLltvgkfempsraylgrfnfKGgdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD------- 479
Cdd:cd03213 99 VRETLMFAAKL-------------------RG---------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssalqv 150
|
....*....
gi 489917580 480 VETLRALED 488
Cdd:cd03213 151 MSLLRRLAD 159
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-236 |
3.99e-19 |
|
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: 84.51 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGL-NIGYLPQEPELnPEHTVRQSVeegl 94
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR-IGMPEGeDLLFLPQRPYL-PLGTLREQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 gavfnakqrldevyaAYaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlpPWDAMvgkLSGGEKRRV 174
Cdd:cd03223 85 ---------------IY----------------------------------------------PWDDV---LSGGEQQRL 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHdRYFLDNAAEWILELD 236
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
326-515 |
4.02e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 90.35 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY--GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD---SGEVKLGQT-----------V 389
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFKG-GDQNkiVGQLSGGERGRLHLAKTLIAGG 466
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLelLEAVGLERrLDRY--PHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 467 NVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHDRWFLDRIATHIL 515
Cdd:COG1123 162 DLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
331-544 |
4.31e-19 |
|
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: 86.56 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK-----------LAYVDQS- 397
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGYLPQEa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 ----RDSLEGNktvFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKiVGQLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:TIGR04406 86 sifrKLTVEEN---IMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNK-AMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 474 PSNDLD---VETLRALEDALLEFPGSVMVISHD-RWFLDRIATHILAFEGDsqvVFFDGNYQEYEADKKHR---LGEE 544
Cdd:TIGR04406 162 PFAGVDpiaVGDIKKIIKHLKERGIGVLITDHNvRETLDICDRAYIISDGK---VLAEGTPAEIVANEKVRrvyLGEQ 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-238 |
4.67e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 90.48 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 14 IVPP--KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAI-----PMPGLNIGYLPQEPEL 80
Cdd:TIGR01842 324 IVPPggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPptsgsvRLDGADLkqwdrETFGKHIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 81 NPeHTVRQSVeeglgavfnakQRLDEvyaaYAEPDADFDALAAEQAeleaviaaaassgaddieHQMeiaadALRLPP-W 159
Cdd:TIGR01842 404 FP-GTVAENI-----------ARFGE----NADPEKIIEAAKLAGV------------------HEL-----ILRLPDgY 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 160 DAMVGK----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQF---LHKFPGTVVAVTHdRYFLDNAAEWI 232
Cdd:TIGR01842 445 DTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAikaLKARGITVVVITH-RPSLLGCVDKI 523
|
....*.
gi 489917580 233 LELDRG 238
Cdd:TIGR01842 524 LVLQDG 529
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
327-475 |
4.99e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 85.95 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG----------QTVK--LAYV 394
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpphERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRDsLEGNKTVFDAVADGADLLTVGKF-EMPSRAY-----LGRFnfkggdQNKIVGQLSGGERGRLHLAKTLIAGGNV 468
Cdd:cd03224 81 PEGRR-IFPELTVEENLLLGAYARRRAKRkARLERVYelfprLKER------RKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
....*..
gi 489917580 469 LLLDEPS 475
Cdd:cd03224 154 LLLDEPS 160
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
324-521 |
5.34e-19 |
|
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: 85.95 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAY-----GDRLL--IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL---GQTVKLA- 392
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 ---------------YVDQ-----SRDS---------LEGNKTVFDAVADGADLLTvgKFEMPSR---AYLGRFnfkggd 440
Cdd:COG4778 82 aspreilalrrrtigYVSQflrviPRVSaldvvaeplLERGVDREEARARARELLA--RLNLPERlwdLPPATF------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 441 qnkivgqlSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFP--GSVMV-ISHDRWFLDRIATHILAF 517
Cdd:COG4778 154 --------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGTAIIgIFHDEEVREAVADRVVDV 225
|
....
gi 489917580 518 EGDS 521
Cdd:COG4778 226 TPFS 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
330-503 |
6.16e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 330 NHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSR----DS-LEGN 404
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqDArLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 KTVFDAVADG----------ADLLTVGkfeMPSRAylgrfnfkggdqNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:PRK11247 96 KKVIDNVGLGlkgqwrdaalQALAAVG---LADRA------------NEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 489917580 475 SNDLD----VETLRALEDALLEFPGSVMVISHD 503
Cdd:PRK11247 161 LGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-243 |
6.17e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkEIEGEA--IPMPGLNI------------GYLPQEPELNPE 83
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG---ELSPDSgeVRLNGRPLadwspaelarrrAVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 HTVRQSVEEGLGAVFNAKQRLDEVYAAYAEpDADFDALAAeqaeleaviaaaassgaddiehqmeiaadalRLPPwdamv 163
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAAALA-QVDLAHLAG-------------------------------RDYP----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 164 gKLSGGEKRRVALCRLL--LSKPDM----LLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDryfLDNAAEW-- 231
Cdd:PRK13548 134 -QLSGGEQQRVQLARVLaqLWEPDGpprwLLLDEPTSALDlahqHHVLRLARQLAHERGLAVIVVLHD---LNLAARYad 209
|
250
....*....|....*..
gi 489917580 232 -ILELDRG----YGIPW 243
Cdd:PRK13548 210 rIVLLHQGrlvaDGTPA 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-220 |
6.51e-19 |
|
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: 85.35 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI--------PMPGLN-IGYLPQEPELNPEHTVRQ 88
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqkNIEALRrIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEEGLGAVFNAKQRLDEVyaayaepdadfdalaaeqaeLEAVIAaaassgaDDIEHQMeiaadalrlppwdamVGKLSG 168
Cdd:cd03268 92 NLRLLARLLGIRKKRIDEV--------------------LDVVGL-------KDSAKKK---------------VKGFSL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTH 220
Cdd:cd03268 130 GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSH 184
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
327-518 |
6.68e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKlayvDQSRDSLEGN 404
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR----TVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 -KTVF-DA------VADGadlLTVGK--------FEMPSRAYLGRFNFKGGDQ-NKIVG----QLSGGERGRLHLAKTLI 463
Cdd:PRK13657 411 iAVVFqDAglfnrsIEDN---IRVGRpdatdeemRAAAERAQAHDFIERKPDGyDTVVGergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALLEfpgsVM------VISHdRWFLDRIATHILAFE 518
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDE----LMkgrttfIIAH-RLSTVRNADRILVFD 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
327-503 |
6.70e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.11 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGqTVKLAYVDQSRDS----- 400
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRrrvsv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNKTVFDAV-----------ADGADLLtvgkfEMPSRAYLGRF--NFKGGDQNKIVG---QLSGGERGRLHLAKTLIA 464
Cdd:TIGR02868 414 CAQDAHLFDTTvrenlrlarpdATDEELW-----AALERVGLADWlrALPDGLDTVLGEggaRLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDALLE-FPG-SVMVISHD 503
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAaLSGrTVVLITHH 529
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-221 |
8.15e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.58 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLP----------QEPELNPEHTVRQSVeeGL 94
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGR-ILWNGQDLTALPpaerpvsmlfQENNLFPHLTVAQNI--GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 GavFNAKQRLDevyaayaepdadfdalAAEQAELEaviaaaassgadDIEHQMEIAADALRLPpwdamvGKLSGGEKRRV 174
Cdd:COG3840 95 G--LRPGLKLT----------------AEQRAQVE------------QALERVGLAGLLDRLP------GQLSGGQRQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-238 |
8.87e-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: 84.16 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-------------AIPMPGLNIGYLPQEPELNPEH 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEEGLgavfnakqrldevyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdamvg 164
Cdd:cd03229 92 TVLENIALGL---------------------------------------------------------------------- 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 klSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVEWLEQFLHKFPG-TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03229 102 --SGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-221 |
8.98e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DKEIEGE---------AIPMPGLNIGYLPQEPELNPEHTV 86
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEvllngrrltALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGLGAVFNAKQRLDEVYAAYAEpdADFDALAaeqaeleaviaaaassgaddiehqmeiaadalrlppwDAMVGKL 166
Cdd:COG4136 94 GENLAFALPPTIGRAQRRARVEQALEE--AGLAGFA-------------------------------------DRDPATL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQF----LHKFPGTVVAVTHD 221
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHD 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
327-487 |
9.01e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVklayvdQSRDSLEGNK 405
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDV------EALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 TVFDAVADGA-----DLLTVgkFEMPSRAYLGRFNFKGGDQNKIVGQ-----------------LSGGERGRLHLAKTLI 463
Cdd:PRK09536 78 RVASVPQDTSlsfefDVRQV--VEMGRTPHRSRFDTWTETDRAAVERamertgvaqfadrpvtsLSGGERQRVLLARALA 155
|
170 180
....*....|....*....|....*
gi 489917580 464 AGGNVLLLDEPSNDLDV-ETLRALE 487
Cdd:PRK09536 156 QATPVLLLDEPTASLDInHQVRTLE 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
326-492 |
1.03e-18 |
|
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: 85.18 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGD---RLLI-DDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------- 389
Cdd:COG4181 8 IIELRGLTKTVGTgagELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 ---KLAYVDQSRdSLEGNKTVFDAVADGADLLTVGKFEMPSRAYLGRfnfkggdqnkiVG----------QLSGGERGRL 456
Cdd:COG4181 88 rarHVGFVFQSF-QLLPTLTALENVMLPLELAGRRDARARARALLER-----------VGlghrldhypaQLSGGEQQRV 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 457 HLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE 492
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
327-502 |
1.22e-18 |
|
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: 89.39 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG--DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG----QTVKL-------AY 393
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLaslrrqvAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQsrDSLEGNKTVFDAVADGAdLLTVGKFEMPS---RAYLGRF---NFKGGDQNkiVGQ----LSGGERGRLHLAKTLI 463
Cdd:TIGR02203 411 VSQ--DVVLFNDTIANNIAYGR-TEQADRAEIERalaAAYAQDFvdkLPLGLDTP--IGEngvlLSGGQRQRLAIARALL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALLEF-PG-SVMVISH 502
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
327-503 |
1.23e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV-----------KLAYVD 395
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QSRDSLEGnKTVFDAVADGADlltvgkfemPSRAYLGRFNfkGGDQ----------------NKIVGQLSGGERGRLHLA 459
Cdd:PRK11231 83 QHHLTPEG-ITVRELVAYGRS---------PWLSLWGRLS--AEDNarvnqameqtrinhlaDRRLTDLSGGQRQRAFLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 460 KTLIAGGNVLLLDEPSNDLD----VETLRALEDalLEFPG-SVMVISHD 503
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDinhqVELMRLMRE--LNTQGkTVVTVLHD 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-221 |
1.34e-18 |
|
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: 88.96 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPGLN-------IGYLPQEPELNpEH 84
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEvtldGVPVSSLDqdevrrrVSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVeeglgavfnakqRLdevyaayAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalRLPP-WDA 161
Cdd:TIGR02868 424 TVRENL------------RL-------ARPDATDEELwaALERVGLA-----------DWLR----------ALPDgLDT 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 162 MVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEQFLHKFPG-TVVAVTHD 221
Cdd:TIGR02868 464 VLGeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
327-527 |
1.40e-18 |
|
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: 85.04 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAYV 394
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRdSLEGNKTVFDAVADGADLLTVGKFEMPSRAY-------LGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIAGGN 467
Cdd:cd03295 81 IQQI-GLFPHMTVEENIALVPKLLKWPKEKIRERADellalvgLDPAEFA----DRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 468 VLLLDEPSNDLDVETLRALEDALL----EFPGSVMVISHDRWFLDRIATHIlAFEGDSQVVFFD 527
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKrlqqELGKTIVFVTHDIDEAFRLADRI-AIMKNGEIVQVG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-220 |
1.73e-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: 84.97 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDK---EIEGEAIPMPGLN-----IGYLPQEpelnpeh 84
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLlfrFYDVSSgsiLIDGQDIREVTLDslrraIGVVPQD------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVrqsveeglgaVFNakqrlDEVYA--AYAEPDADFDAL--AAEQAELEaviaaaassgaDDIehqmeiaadaLRLPP-W 159
Cdd:cd03253 84 TV----------LFN-----DTIGYniRYGRPDATDEEVieAAKAAQIH-----------DKI----------MRFPDgY 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 160 DAMVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTH 220
Cdd:cd03253 128 DTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-199 |
2.09e-18 |
|
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: 83.78 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAkIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLN----IGYLPQEPELNPEHTV 86
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPpssgtiRIDGQDVLKQPQKlrrrIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEeglgavfnakqrldevYAAYAE--PDADFDALAAEQAELeaviaaaassgADDIEHQmeiaadalrlppwDAMVG 164
Cdd:cd03264 90 REFLD----------------YIAWLKgiPSKEVKARVDEVLEL-----------VNLGDRA-------------KKKIG 129
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE 199
Cdd:cd03264 130 SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
327-502 |
2.22e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 84.59 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLAY 393
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQsrDSLEGNKTVFDAVADGADLLTVGKFEMPSR-AYLGRF--NFKGGDQNKIV---GQLSGGERGRLHLAKTLIAGGN 467
Cdd:cd03251 81 VSQ--DVFLFNDTVAENIAYGRPGATREEVEEAARaANAHEFimELPEGYDTVIGergVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 489917580 468 VLLLDEPSNDLDVETLRALEDAL--LEFPGSVMVISH 502
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALerLMKNRTTFVIAH 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
337-502 |
2.49e-18 |
|
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: 83.18 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQT----VKLAYVDQS-----RDSLEGNKTV 407
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeQRDEPHENIlylghLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 408 ------FDAVADGADLltvgkfeMPSRAyLGRFNFKGGdQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD-- 479
Cdd:TIGR01189 91 lenlhfWAAIHGGAQR-------TIEDA-LAAVGLTGF-EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDka 161
|
170 180
....*....|....*....|....
gi 489917580 480 -VETLRALEDALLEFPGSVMVISH 502
Cdd:TIGR01189 162 gVALLAGLLRAHLARGGIVLLTTH 185
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
326-523 |
2.52e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY---GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KL 391
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQsrDSLEGNKTVFDAVADGADLLTvgKFEMPSRAYL-GRFNFKGGDQNKI---VG----QLSGGERGRLHLAKTLI 463
Cdd:TIGR00958 558 ALVGQ--EPVLFSGSVRENIAYGLTDTP--DEEIMAAAKAaNAHDFIMEFPNGYdteVGekgsQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHdRWFLDRIATHILAFEGDSQV 523
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVV 692
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-220 |
3.28e-18 |
|
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: 82.98 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGE----AIPMPGLN----IGYLPQEPELNPEHTVR 87
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEvlinGRPLDKRSfrkiIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEeglgavFNAKQRldevyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdamvgKLS 167
Cdd:cd03213 101 ETLM------FAAKLR-------------------------------------------------------------GLS 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTH 220
Cdd:cd03213 114 GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtgrTIICSIH 169
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-245 |
3.51e-18 |
|
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: 83.71 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK----EIEGEAIPMPGL----------NIGYLPQEPELNPEH 84
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgEVLIDGEDISGLseaelyrlrrRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEeglgavFNAKQRLDEvyaayaePDADFDALAAEQAELeaviaaaassgaddiehqMEIAADALRLPpwdamvG 164
Cdd:cd03261 93 TVFENVA------FPLREHTRL-------SEEEIREIVLEKLEA------------------VGLRGAEDLYP------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD---AESVEWLEQFLHKFPG-TVVAVTHDRYFLDNAAEWILELDRGyG 240
Cdd:cd03261 136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDG-K 214
|
....*
gi 489917580 241 IPWKG 245
Cdd:cd03261 215 IVAEG 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-238 |
3.54e-18 |
|
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: 82.90 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGlNIGYLPQEPELNPEhTVRQSVEegLGAVFNa 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGS-VSVPG-SIAYVSQEPWIQNG-TIRENIL--FGKPFD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 101 KQRLDEVYAAYAEpDADFDALAAeqaeleaviaaaassgADDIEhqmeiaadalrlppwdamVGK----LSGGEKRRVAL 176
Cdd:cd03250 94 EERYEKVIKACAL-EPDLEILPD----------------GDLTE------------------IGEkginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAESVEWLeqFLH------KFPGTVVAVTHDRYFLDNaAEWILELDRG 238
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHI--FENcilgllLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-200 |
3.57e-18 |
|
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: 87.95 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEAIPMPGLNIGYLPQEpelnpehtvrqSVEEGLGA 96
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-YDVTSGRILIDGQDIRDVTQA-----------SLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 V------FNakqrlDEVYA--AYAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalRLPP-WDAMVG- 164
Cdd:COG5265 437 VpqdtvlFN-----DTIAYniAYGRPDASEEEVeaAARAAQIH-----------DFIE----------SLPDgYDTRVGe 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 489917580 165 ---KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 200
Cdd:COG5265 491 rglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
327-511 |
4.37e-18 |
|
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: 83.54 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLiDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------KLAYVDQS 397
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RdSLEGNKTVFDAVADGADLLTVGKFEMPSRAyLGRFNFKGGDQ--NKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPS 475
Cdd:cd03299 80 Y-ALFPHMTVYKNIAYGLKKRKVDKKEIERKV-LEIAEMLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 476 NDLDVET----LRALEDALLEFPGSVMVISHD----RWFLDRIA 511
Cdd:cd03299 158 SALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-221 |
4.49e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.54 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGE---AIPMPGLNIGYLPQEPELNPEHTVRQSVEE 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEdatDVPVQERNVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 GLgAVFNAKQRldevyaayaEPDADFDALAAEQAELEaviaaaassgaddiehQMEIAADalRLPPwdamvgKLSGGEKR 172
Cdd:cd03296 98 GL-RVKPRSER---------PPEAEIRAKVHELLKLV----------------QLDWLAD--RYPA------QLSGGQRQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-192 |
8.58e-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: 82.59 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI---------PM---PGLNIGYLPQEPELnpeht 85
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditklPMhkrARLGIGYLPQEASI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQ-SVEEGLGAVfnakqrLDEVYAAYAEPDADFDALAAEQaeleaviaaaassgadDIEHqmeiaadaLRlppwDAMVG 164
Cdd:cd03218 87 FRKlTVEENILAV------LEIRGLSKKEREEKLEELLEEF----------------HITH--------LR----KSKAS 132
|
170 180
....*....|....*....|....*...
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEP 192
Cdd:cd03218 133 SLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
324-384 |
9.26e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAY------GDRLL----------------IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSG 381
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepSRSLKelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
...
gi 489917580 382 EVK 384
Cdd:COG1134 82 RVE 84
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-222 |
1.02e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGL----------NIGYLPQEPELNPEHTVR 87
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH-IRFHGTdvsrlhardrKVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLgAVFNAKQRldevyaayaePDADfdALAAEQAELEAVIaaaassgaddiehQMEIAADalRLPpwdamvGKLS 167
Cdd:PRK10851 93 DNIAFGL-TVLPRRER----------PNAA--AIKAKVTQLLEMV-------------QLAHLAD--RYP------AQLS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEQfLH---KFpgTVVAVTHDR 222
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQ-LHeelKF--TSVFVTHDQ 197
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
327-482 |
1.04e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.36 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY----GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------------ 389
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdGVDLtalserelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -KLAYVDQSrDSLEGNKTVFDAVA-----DGadlltVGKFEMPSRA--YLgrfnfkggdqnKIVG----------QLSGG 451
Cdd:COG1135 82 rKIGMIFQH-FNLLSSRTVAENVAlpleiAG-----VPKAEIRKRVaeLL-----------ELVGlsdkadaypsQLSGG 144
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 452 ERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 482
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-221 |
1.28e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 82.23 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 9 NRVGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG-----------VDKEI---EGEAIPMPGLNIGYL 74
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvliDGTDInklKGKALRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 75 PQEPELNPEHTVRQSVEEGLGAVFNAKQRLDEVYaayaePDADF-DALAAeqaeLEaviaaaassgaddiehQMEIAADA 153
Cdd:cd03256 84 FQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLF-----PKEEKqRALAA----LE----------------RVGLLDKA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 154 LRlppwdaMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD---AESV-EWLEQFLHKFPGTVVAVTHD 221
Cdd:cd03256 139 YQ------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVmDLLKRINREEGITVIVSLHQ 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
337-514 |
1.30e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQS------RDSLEGNKTVFD 409
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPDVAEAchylghRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 410 AVADGADLLtvGKFEMPSRAYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDA 489
Cdd:PRK13539 93 NLEFWAAFL--GGEELDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
170 180
....*....|....*....|....*...
gi 489917580 490 L---LEFPGsvMVIshdrwfldrIATHI 514
Cdd:PRK13539 170 IrahLAQGG--IVI---------AATHI 186
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-239 |
1.37e-17 |
|
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: 81.42 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNI-------GYLPQEPELNPEH 84
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiIIDGLKLTDDKKNInelrqkvGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEEGLGAVFNakqrldevyaayaEPDADFDALAAEqaELEaviaaaassgaddiehQMEIAADAlrlppwDAMVG 164
Cdd:cd03262 92 TVLENITLAPIKVKG-------------MSKAEAEERALE--LLE----------------KVGLADKA------DAYPA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLE--QFLHKFPGTVVAVTHDRYFLDNAAEWILELDRGY 239
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgEVLDvmKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-221 |
1.51e-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: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI-------PMP--GLNIGYLPQEPELNPEHTVRQSVEE 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditNLPpeKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 GLGAVFNAKQRLDEvyaayaepdadfdalaaeqaeleaviaaaassGADDIEHQMEIAADALRLPpwdamvGKLSGGEKR 172
Cdd:cd03299 95 GLKKRKVDKKEIER--------------------------------KVLEIAEMLGIDHLLNRKP------ETLSGGEQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTHD 221
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
327-503 |
1.61e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK-----LAYVDQSrDS 400
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEgpgaeRGVVFQN-EG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKGGDQNKIvGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL 478
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAhqMLKKVGLEGAEKRYI-WQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*....
gi 489917580 479 DVETLRALEDALL----EFPGSVMVISHD 503
Cdd:PRK11248 160 DAFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-220 |
1.66e-17 |
|
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: 82.05 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------------DKEIEGEAIPmpGL--NIGYLpqEPELNPEH 84
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygndvrlfGERRGGEDVW--ELrkRIGLV--SPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEE----GLgavfnakqrldevYAA---YAEPDADFDALAAEQAELeaviaaaassgaddiehqMEIAADAlrlp 157
Cdd:COG1119 92 PRDETVLDvvlsGF-------------FDSiglYREPTDEQRERARELLEL------------------LGLAHLA---- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 158 pwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTH 220
Cdd:COG1119 137 --DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-528 |
1.91e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPG------LNIGYLPQEPELNPEHTVRQS 89
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKPVRIRSprdaiaLGIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEegLGAVFNAKQRLDevyaayaepdadfdaLAAEQAELEaviaaaassgaddiehqmEIAAD-ALRLPPwDAMVGKLSG 168
Cdd:COG3845 101 IV--LGLEPTKGGRLD---------------RKAARARIR------------------ELSERyGLDVDP-DAKVEDLSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDryfLDnaaEwILEL-DR------G 238
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHK---LR---E-VMAIaDRvtvlrrG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 239 ygipwkgnysswleQKEDRLKQEEATEsarqktikKEL-EW-VrqnpkGRQAKAKARIARFEelssyeyqkrnetqeifi 316
Cdd:COG3845 218 --------------KVVGTVDTAETSE--------EELaELmV-----GREVLLRVEKAPAE------------------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 317 pvgdrLGNEVIEFNHVS-KAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----- 389
Cdd:COG3845 253 -----PGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdGEDItglsp 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 ------KLAYV--DQSRDSLEGNKTVFD-AVADGADLLTVGKFEMPSRAYL--------GRFNFKGGDQNKIVGQLSGGE 452
Cdd:COG3845 328 rerrrlGVAYIpeDRLGRGLVPDMSVAEnLILGRYRRPPFSRGGFLDRKAIrafaeeliEEFDVRTPGPDTPARSLSGGN 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 453 RGRLHLAKTLIAGGNVLLLDEPSNDLDV-------ETLRALEDAllefpGS-VMVISHDrwfL-------DRIAthilaf 517
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVgaiefihQRLLELRDA-----GAaVLLISED---LdeilalsDRIA------ 473
|
570
....*....|.
gi 489917580 518 egdsqvVFFDG 528
Cdd:COG3845 474 ------VMYEG 478
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-221 |
2.16e-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: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPGLNIGYLPQEPELnpehtVRQSVeeg 93
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegEVLLDGKDIYDLDVDVLE-----LRRRV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 lGAVFnakQRldevyaayaePDAdFDALAAEQAELeaviaAAASSGADDIEHQMEIAADALR---LppWD-----AMVGK 165
Cdd:cd03260 84 -GMVF---QK----------PNP-FPGSIYDNVAY-----GLRLHGIKLKEELDERVEEALRkaaL--WDevkdrLHALG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF--PGTVVAVTHD 221
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
327-520 |
2.35e-17 |
|
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: 79.51 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVklgqtvklayvdqsrDSLEGNK 405
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------GMPEGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 TVFdavadgadlltvgkfeMPSRAYLGRFNFKggDQ-----NKIvgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:cd03223 66 LLF----------------LPQRPYLPLGTLR--EQliypwDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489917580 481 ETLRALEDALLEFPGSVMVISHdRWFLDRIATHILAFEGD 520
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
326-479 |
3.10e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------KLAYVDQ 396
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDIthvpaenrHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRdSLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFKGGDQNKIvGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:PRK09452 94 SY-ALFPHMTVFENVAFGLRMQKTPAAEITPRVMeaLRMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
....*
gi 489917580 475 SNDLD 479
Cdd:PRK09452 172 LSALD 176
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
337-526 |
3.56e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 84.80 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGqtvkLAYVDQ-SRDSL-------------- 401
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD----GADLSQwDREELgrhigylpqdvelf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGnkTV-----------FDAVADGADLltVGKFEMpsrayLGRFNfKGGDqnKIVGQ----LSGGERGRLHLAKTLIagG 466
Cdd:COG4618 419 DG--TIaeniarfgdadPEKVVAAAKL--AGVHEM-----ILRLP-DGYD--TRIGEggarLSGGQRQRIGLARALY--G 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 467 N--VLLLDEPSNDLDVETLRALEDALLEF---PGSVMVISHDRWFLdRIATHILAFEgDSQVVFF 526
Cdd:COG4618 485 DprLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLL-AAVDKLLVLR-DGRVQAF 547
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
337-502 |
4.44e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKlayvdQSRDSLegnktvfdavadGA 415
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-----RQRDEY------------HQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 416 DLLTVG-----KFEMPSRAYLgRFNFKGG---DQNKI----------------VGQLSGGERGRLHLAKTLIAGGNVLLL 471
Cdd:PRK13538 75 DLLYLGhqpgiKTELTALENL-RFYQRLHgpgDDEALwealaqvglagfedvpVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 489917580 472 DEPSNDLD---VETLRALEDALLEFPGSVMVISH 502
Cdd:PRK13538 154 DEPFTAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
335-503 |
5.40e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 335 AYGDRLLidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGrEQPDSGEVKLGQT-------VKLA--------------- 392
Cdd:COG4138 7 AVAGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdwsaAELArhraylsqqqsppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 -----YVDQSRDSLEGNKTVFDAVADGADLLTVGKfempsraYLGRfnfkggdqnkIVGQLSGGERGRLHLAKTLI---- 463
Cdd:COG4138 84 mpvfqYLALHQPAGASSEAVEQLLAQLAEALGLED-------KLSR----------PLTQLSGGEWQRVRLAAVLLqvwp 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489917580 464 ---AGGNVLLLDEPSNDLDVETLRALEDALLEFP---GSVMVISHD 503
Cdd:COG4138 147 tinPEGQLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
327-503 |
6.99e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVskAYGDRLLidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGReQPDSGEVKLGQT-------VKLA------- 392
Cdd:PRK03695 1 MQLNDV--AVSTRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQpleawsaAELArhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 -------------YVDQSRDSLEGNKTVFDAVADGADLLTVGKFempsrayLGRfnfkggdqnkIVGQLSGGERGRLHLA 459
Cdd:PRK03695 76 qqqtppfampvfqYLTLHQPDKTRTEAVASALNEVAEALGLDDK-------LGR----------SVNQLSGGEWQRVRLA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489917580 460 -------KTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFP---GSVMVISHD 503
Cdd:PRK03695 139 avvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-192 |
7.13e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---VDK---EIEGEAI---PMPG---LNIGYLPQEP----ELn 81
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkPDSgriFLDGEDIthlPMHKrarLGIGYLPQEAsifrKL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 82 pehtvrqSVEEGLGAV-----FNAKQRLDEVyaayaepdadfDALAAEQaeleaviaaaassgadDIEHqmeiaadaLRl 156
Cdd:COG1137 94 -------TVEDNILAVlelrkLSKKEREERL-----------EELLEEF----------------GITH--------LR- 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 157 ppwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEP 192
Cdd:COG1137 131 ---KSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-225 |
7.74e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNIGylpqepeLNPEHTVRQSVe 91
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsgrvEVNGRVSALLELGAG-------FHPELTGRENI- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 92 eglgaVFNA----------KQRLDEVyaayaepdADFdalaaeqAELEaviaaaassgaddiehqmeiaaDALRLPpwda 161
Cdd:COG1134 110 -----YLNGrllglsrkeiDEKFDEI--------VEF-------AELG----------------------DFIDQP---- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 162 mVGKLSGGEKRR----VALCRlllsKPDMLLLDEPTNHLDAE----SVEWLEQFLHKfPGTVVAVTHDRYFL 225
Cdd:COG1134 144 -VKTYSSGMRARlafaVATAV----DPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAV 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-220 |
8.33e-17 |
|
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: 78.94 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----------PMPGLNIGYLPQEPELNPEHTVRQ 88
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtplaeqrDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEeGLGAVFNAKQRldevyaayaepdADFDALAAeqaeleaviaaaasSGADDIEHqmeiaadalrLPpwdamVGKLSG 168
Cdd:TIGR01189 93 NLH-FWAAIHGGAQR------------TIEDALAA--------------VGLTGFED----------LP-----AAQLSA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQF----LHKfPGTVVAVTH 220
Cdd:TIGR01189 131 GQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLlrahLAR-GGIVLLTTH 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-238 |
9.35e-17 |
|
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: 79.37 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 8 MNRVGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE--------------AIPMPGLNIGY 73
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngqdvsdlrgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 74 LPQEPELNPEHTVRQSVEEGLGAVFNAKQRLDEVYAAyaepdadfdalAAEQAELEAVIaaaassgaddiehqmeiaada 153
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPA-----------ALELVGLSHKH--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 154 lrlppwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFlHKFPGTVVAVTHDRYFLDNAA 229
Cdd:cd03292 131 ------RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweiMNLLKKI-NKAGTTVVVATHAKELVDTTR 203
|
....*....
gi 489917580 230 EWILELDRG 238
Cdd:cd03292 204 HRVIALERG 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-474 |
9.46e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEAIPMPGLN-------------IGYLPQ------EP 78
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGA-RKIQQGRVEVLGGDmadarhrravcprIAYMPQglgknlYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 79 ELnpehtvrqSVEE---------GLGAvfnakqrldevyaayAEPDADFDALAaeqaeleaviaaaassgaddiehqmei 149
Cdd:NF033858 92 TL--------SVFEnldffgrlfGQDA---------------AERRRRIDELL--------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 150 aaDALRLPPW-DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESvewLEQF--L-----HKFPG-TVVAVTH 220
Cdd:NF033858 122 --RATGLAPFaDRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS---RRQFweLidrirAERPGmSVLVATA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 221 dryFLDNAA--EWILELDRGygipwkgnysswleqkedRLKQEEATESARQKTIKKELEwvrqnpkgrqakaKARIARFE 298
Cdd:NF033858 197 ---YMEEAErfDWLVAMDAG------------------RVLATGTPAELLARTGADTLE-------------AAFIALLP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 299 ElssyeyQKRNETQEIFIP--VGDRLGNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE 376
Cdd:NF033858 243 E------EKRRGHQPVVIPprPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 377 QPDSGEVKL-GQTV---------KLAYVDQSRdSLEGNKTVFDAVADGADLLTVGKFEMPSR--AYLGRFNFkGGDQNKI 444
Cdd:NF033858 317 PASEGEAWLfGQPVdagdiatrrRVGYMSQAF-SLYGELTVRQNLELHARLFHLPAAEIAARvaEMLERFDL-ADVADAL 394
|
490 500 510
....*....|....*....|....*....|
gi 489917580 445 VGQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:NF033858 395 PDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-221 |
1.22e-16 |
|
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: 81.69 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 24 DISLSFfPGAKIGVL-GLNGSGKSTLLKIMAGVDKEIEGE---------------AIPMPGLNIGYLPQEPELNPEHTVR 87
Cdd:COG4148 17 DVDFTL-PGRGVTALfGPSGSGKTTLLRAIAGLERPDSGRirlggevlqdsargiFLPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLGAVFNAKQRldevyaayaepdADFDALAAEqaeLEaviaaaassgaddIEHQMEiaadalRLPpwdamvGKLS 167
Cdd:COG4148 96 GNLLYGRKRAPRAERR------------ISFDEVVEL---LG-------------IGHLLD------RRP------ATLS 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDlarkAEILPYLERLRDELDIPILYVSHS 193
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-220 |
1.29e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAI--PMPGLNIGYLPQEPELNPEHTVRQSV 90
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpaagtiKLDGGDIddPDVAEACHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EeglgavFNAkqrldevyAAYAEPDADFDAlAAEQAELeaviaaaassgaDDIEHqmeiaadalrLPpwdamVGKLSGGE 170
Cdd:PRK13539 95 E------FWA--------AFLGGEELDIAA-ALEAVGL------------APLAH----------LP-----FGYLSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL--H-KFPGTVVAVTH 220
Cdd:PRK13539 133 KRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIraHlAQGGIVIAATH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
326-519 |
1.29e-16 |
|
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: 79.05 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY---GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KL 391
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQ----SRDSLEGN------KTVFDAVADGADLLTVGKF--EMPSrAYLGRFNFKGGdqnkivgQLSGGERGRLHLA 459
Cdd:cd03248 91 SLVGQepvlFARSLQDNiayglqSCSFECVKEAAQKAHAHSFisELAS-GYDTEVGEKGS-------QLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 460 KTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDRiATHILAFEG 519
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLSTVER-ADQILVLDG 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-221 |
1.32e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLNIGYLPQEPELNPehTVRQSVEEGLGAV 97
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT--TLPLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 FNAKqrldevyaayaepDAD-FDALAAEQAEleaviaaaassgaDDIEHQMEiaadalrlppwdamvgKLSGGEKRRVAL 176
Cdd:PRK09544 94 PGTK-------------KEDiLPALKRVQAG-------------HLIDAPMQ----------------KLSGGETQRVLL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGqvalYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
327-532 |
1.36e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 79.45 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG--DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVkLGQTVKLAYVDQS------- 397
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHDLALADPAwlrrqvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 ---RDSLEGNKTVFDAVADGADLLTVGKFEMPSRaYLGRFNF-----KGGDQnkIVGQ----LSGGERGRLHLAKTLIAG 465
Cdd:cd03252 80 vvlQENVLFNRSIRDNIALADPGMSMERVIEAAK-LAGAHDFiselpEGYDT--IVGEqgagLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHdRWFLDRIATHILAFEGDSQVVffDGNYQE 532
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKGRIVE--QGSHDE 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
339-519 |
1.92e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 339 RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE--QPDSGEVKLGQtvklayvdqsrDSLEGNKTVFDAVADGAD 416
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD-----------NQFGREASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 417 LLTVgkFEMPSRA-------YLGRFNfkggdqnkivgQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETL----RA 485
Cdd:COG2401 112 FKDA--VELLNAVglsdavlWLRRFK-----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAkrvaRN 178
|
170 180 190
....*....|....*....|....*....|....
gi 489917580 486 LEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:COG2401 179 LQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
330-524 |
2.00e-16 |
|
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: 79.61 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 330 NHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------------KLAYV 394
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIaamsrkelrelrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRdSLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:cd03294 108 FQSF-ALLPHRTVLENVAFGLEVQGVPRAEREERAAeaLELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 473 EPSNDLDVETLRALEDALL----EFPGSVMVISHDrwfLD---RIATHIlAFEGDSQVV 524
Cdd:cd03294 186 EAFSALDPLIRREMQDELLrlqaELQKTIVFITHD---LDealRLGDRI-AIMKDGRLV 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-221 |
2.34e-16 |
|
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: 78.63 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQEPELnpehTVRQsveEGLGAVFNA 100
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-VRLAGQDLFALDEDARA----RLRA---RHVGFVFQS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 101 KQRLD-----EVYAAYAEPDADFDALAAEQAELEaviaaaassgaddiehQMEIAAdalRLppwDAMVGKLSGGEKRRVA 175
Cdd:COG4181 99 FQLLPtltalENVMLPLELAGRRDARARARALLE----------------RVGLGH---RL---DHYPAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 176 LCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQfLHKFPG-TVVAVTHD 221
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATgeqiIDLLFE-LNRERGtTLVLVTHD 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
327-479 |
2.41e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.14 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG----DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-----KLAYVDQ 396
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVtgpgaDRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 sRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKGGDQNKIVgQLSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:COG4525 84 -KDALLPWLNVLDNVAFGLRLRGVPKAERRARAeeLLALVGLADFARRRIW-QLSGGMRQRVGIARALAADPRFLLMDEP 161
|
....*
gi 489917580 475 SNDLD 479
Cdd:COG4525 162 FGALD 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-244 |
2.63e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.60 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 28 SFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGAVFNAKQRLDEV 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-IEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 108 yaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaADALRLPP-WDAMVGKLSGGEKRRVALCrLLLSKP-D 185
Cdd:cd03237 100 -------------------------------------------AKPLQIEQiLDREVPELSGGELQRVAIA-ACLSKDaD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 186 MLLLDEPTNHLDAE----SVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDrgyGIPWK 244
Cdd:cd03237 136 IYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE---GEPSV 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
327-519 |
3.00e-16 |
|
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: 80.53 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNhVSKAYGDRLLidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------------KL 391
Cdd:COG4148 3 LEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQ------------------SRDSLEGNKTVFDAVADgadLLTVGkfempsrAYLGRFnfkggdqnkiVGQLSGGER 453
Cdd:COG4148 80 GYVFQearlfphlsvrgnllygrKRAPRAERRISFDEVVE---LLGIG-------HLLDRR----------PATLSGGER 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 454 GRLHLAKTLIAGGNVLLLDEPSNDLDVET-------LRALEDAlLEFPgsVMVISHDRWFLDRIATHILAFEG 519
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDLARkaeilpyLERLRDE-LDIP--ILYVSHSLDEVARLADHVVLLEQ 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-486 |
3.33e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.08 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 334 KAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD---SGEVKL-GQTVK-------LAYVDQSrDSLE 402
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPRKpdqfqkcVAYVRQD-DILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 GNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKG--GDQ---NKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSND 477
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdlALTrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170
....*....|....*.
gi 489917580 478 LD-------VETLRAL 486
Cdd:cd03234 174 LDsftalnlVSTLSQL 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-221 |
3.53e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.57 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPGL--NIGYLPQEPELNPEHTVRQSVee 92
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagTAPLAEAreDTRLMFQDARLLPWKKVIDNV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 GLGAVFNAKQrldevyaayaepdadfdalAAEQAeleaviaaaassgaddiehqMEIAADALRLPPWDAmvgKLSGGEKR 172
Cdd:PRK11247 103 GLGLKGQWRD-------------------AALQA--------------------LAAVGLADRANEWPA---ALSGGQKQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDA----------ESVeWLEqflHKFpgTVVAVTHD 221
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDAltriemqdliESL-WQQ---HGF--TVLLVTHD 193
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
326-532 |
3.54e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSLEG- 403
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDPKVDERLIRQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 404 ----------NKTVFDAVADGA----------------DLLtvGKFEMPSRAylgrfnfkggdqNKIVGQLSGGERGRLH 457
Cdd:PRK09493 81 mvfqqfylfpHLTALENVMFGPlrvrgaskeeaekqarELL--AKVGLAERA------------HHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEfpGSVMVI-SHDRWFLDRIATHILAFEGDSQVVffDGNYQE 532
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPelrhEVLKVMQDLAEE--GMTMVIvTHEIGFAEKVASRLIFIDKGRIAE--DGDPQV 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
326-510 |
4.03e-16 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 77.39 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLL----IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTV-KLAYVDQSRd 399
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfNGQSLsKLSSNERAK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 sLEgNKTV------------FDAVADGADLLTVGKF---EMPSRAY--LGRFNFKGgDQNKIVGQLSGGERGRLHLAKTL 462
Cdd:TIGR02211 80 -LR-NKKLgfiyqfhhllpdFTALENVAMPLLIGKKsvkEAKERAYemLEKVGLEH-RINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489917580 463 IAGGNVLLLDEPSNDLDVETLRALEDALLEFPG----SVMVISHDRWFLDRI 510
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRelntSFLVVTHDLELAKKL 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
327-479 |
4.62e-16 |
|
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: 77.15 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQtVKLAYVDQSR-------- 398
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADrpvsmlfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 -DSLEGNKTVFDAVADGAD----LLTVGKFEMpsRAYLGRFNFKGGDQnKIVGQLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:cd03298 78 eNNLFAHLTVEQNVGLGLSpglkLTAEDRQAI--EVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
....*.
gi 489917580 474 PSNDLD 479
Cdd:cd03298 155 PFAALD 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
327-502 |
4.88e-16 |
|
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: 77.65 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAYV 394
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQsrDSLEGNKTVFDAVADGADLLTVGKFEMPSRA----YLGRFNFKGGDQnkIVGQ----LSGGERGRLHLAKTLIAGG 466
Cdd:cd03254 83 LQ--DTFLFSGTIMENIRLGRPNATDEEVIEAAKEagahDFIMKLPNGYDT--VLGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 489917580 467 NVLLLDEPSNDLDVETLRALEDALLE-FPG-SVMVISH 502
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-238 |
5.22e-16 |
|
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: 77.48 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLP-------------QEPELNPEHTVRQ 88
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLPpheiarlgigrtfQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEegLGAVFNAKQRLDEVYAAYAEPDadfdalAAEQAeleaviaaaassgaddiehqMEIaADALRLPP-WDAMVGKLS 167
Cdd:cd03219 95 NVM--VAAQARTGSGLLLARARREERE------ARERA--------------------EEL-LERVGLADlADRPAGELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
326-530 |
7.74e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRD----- 399
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAagiai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 -----SLEGNKTVFDAVADGADLLTVGKF---EMPSRA--YLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIAGGNVL 469
Cdd:COG1129 84 ihqelNLVPNLSVAENIFLGREPRRGGLIdwrAMRRRAreLLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 470 LLDEPS---NDLDVETL----RALEDAllefpG-SVMVISHdrwFLD---RIATHIlafegdsqVVFFDGNY 530
Cdd:COG1129 163 ILDEPTaslTEREVERLfriiRRLKAQ-----GvAIIYISH---RLDevfEIADRV--------TVLRDGRL 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-221 |
8.91e-16 |
|
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: 79.00 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 31 PGAKI-GVLGLNGSGKSTLLKIMAGVDKEIEGEA---------------IPMPGLNIGYLPQEPELNPEHTVRQSVEEGL 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 GAVfNAKQRldevyaaYAEPDADFDALAaeqaeleaviaaaassgaddIEHQMEiaadalRLPpwdamvGKLSGGEKRRV 174
Cdd:TIGR02142 101 KRA-RPSER-------RISFERVIELLG--------------------IGHLLG------RLP------GRLSGGEKQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:TIGR02142 141 AIGRALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-221 |
9.25e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.96 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEaiPMPGL-----NIGYLPQEPELNPEHTV 86
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDptsgeiLIGGR--DVTDLppkdrNIAMVFQSYALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGLgavfnaKQRldevyaayAEPDADFDALAAEQAELEaviaaaassgadDIEHQMEiaadalRLPpwdamvGKL 166
Cdd:COG3839 93 YENIAFPL------KLR--------KVPKAEIDRRVREAAELL------------GLEDLLD------RKP------KQL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-----VEwLEQFLHKFPGTVVAVTHD 221
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLrvemrAE-IKRLHRRLGTTTIYVTHD 193
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
327-490 |
1.15e-15 |
|
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: 79.86 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKlayvDQSRDSLEG- 403
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIR----DVTQASLRAa 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 404 -----------NKTVF------------DAVADGADLltvgkfempsrAYLGRF--NFKGGDQNKiVGQ----LSGGERG 454
Cdd:COG5265 434 igivpqdtvlfNDTIAyniaygrpdaseEEVEAAARA-----------AQIHDFieSLPDGYDTR-VGErglkLSGGEKQ 501
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 455 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDAL 490
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-238 |
1.20e-15 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 77.09 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIgylpqepeLNPEH--TVRQSVeeglG 95
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGK-VTVDGLDT--------LDEENlwEIRKKV----G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVF-NakqrldevyaayaePDADFDALAAEqaeleaviaaaassgaDDI----EHQM-------EIAADALrlppwdAMV 163
Cdd:TIGR04520 81 MVFqN--------------PDNQFVGATVE----------------DDVafglENLGvpreemrKRVDEAL------KLV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 164 G----------KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQfLHKFPG-TVVAVTHDryfLDNA 228
Cdd:TIGR04520 125 GmedfrdrephLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkevLETIRK-LNKEEGiTVISITHD---MEEA 200
|
250
....*....|..
gi 489917580 229 --AEWILELDRG 238
Cdd:TIGR04520 201 vlADRVIVMNKG 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-503 |
1.20e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.21 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK--------------------LGQTVKLAYvDQS-RDS 400
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkrrkefarrigvvFGQRSQLWW-DLPaIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNKTVFDaVADG---------ADLLTVGKFEmpsraylgrfnfkggdqNKIVGQLSGGERGRLHLAKTLIAGGNVLLL 471
Cdd:COG4586 117 FRLLKAIYR-IPDAeykkrldelVELLDLGELL-----------------DTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 472 DEPSNDLDVETLRALEDALLE----FPGSVMVISHD 503
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
326-475 |
1.21e-15 |
|
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: 76.56 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK-----------LAY 393
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQSRDslegnktVFdavadgADL-----LTVGkfempsrAYLGRFNFKGGD---------------QNKIVGQLSGGER 453
Cdd:COG0410 83 VPEGRR-------IF------PSLtveenLLLG-------AYARRDRAEVRAdlervyelfprlkerRRQRAGTLSGGEQ 142
|
170 180
....*....|....*....|..
gi 489917580 454 GRLHLAKTLIAGGNVLLLDEPS 475
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPS 164
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-260 |
1.25e-15 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 76.56 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPqEPELNPehtVRQSVeeglGAVF 98
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE-ILVDGQDITGLS-EKELYE---LRRRI----GMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 99 nakQRldevyaayaepDADFDALAA---------EQAELeaviaaaassGADDIEhqmEIAADALrlppwdAMVG----- 164
Cdd:COG1127 89 ---QG-----------GALFDSLTVfenvafplrEHTDL----------SEAEIR---ELVLEKL------ELVGlpgaa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 -----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTHDRYFLDNAAEWILEL 235
Cdd:COG1127 136 dkmpsELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|....*
gi 489917580 236 DRGYgIPWKGNYSSWLEQKEDRLKQ 260
Cdd:COG1127 216 ADGK-IIAEGTPEELLASDDPWVRQ 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-221 |
1.35e-15 |
|
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: 76.35 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVeeglg 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPtsggviLEGKQITEPGPDRMVVFQNYSLLPWLTVRENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 avfnakqrldevyaAYAEPDADFDALAAEQAELeaviaaaassgaddIEHQMEI-----AADAlrlPPwdamvGKLSGGE 170
Cdd:TIGR01184 76 --------------ALAVDRVLPDLSKSERRAI--------------VEEHIALvglteAADK---RP-----GQLSGGM 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTHD 221
Cdd:TIGR01184 120 KQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEehrvTVLMVTHD 174
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-238 |
1.45e-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: 74.56 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLN-----IGYLPQEPELnpehtv 86
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRptsgrvRLDGADISQWDPNelgdhVGYLPQDDEL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 rqsveeglgavfnakqrldevyaayaepdadFDALAAeqaeleaviaaaassgaDDIehqmeiaadalrlppwdamvgkL 166
Cdd:cd03246 88 -------------------------------FSGSIA-----------------ENI----------------------L 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQF---LHKFPGTVVAVTHdRYFLDNAAEWILELDRG 238
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAH-RPETLASADRILVLEDG 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
327-502 |
1.49e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR--LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAgRE-QPDSGEVKLGQTVKLAYVDQS------ 397
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAwDPQQGEILLNGQPIADYSEAAlrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 ---------RDSLEGNKTVFDAVADGADLLTV------GKF---EMPSRAYLGrfnfKGGDqnkivgQLSGGERGRLHLA 459
Cdd:PRK11160 418 vvsqrvhlfSATLRDNLLLAAPNASDEALIEVlqqvglEKLledDKGLNAWLG----EGGR------QLSGGEQRRLGIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 460 KTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISH 502
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITH 532
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
166-479 |
1.65e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.29 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVthdryfldnaaewILELDRGYGIPwkg 245
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIP--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 246 nysswleqkedrlkqeeatESARQKTIKKELEWVRQNPKGR--QAKAKARIARFEELS------SYEYQKRNEtqeifIP 317
Cdd:PRK10938 200 -------------------DFVQFAGVLADCTLAETGEREEilQQALVAQLAHSEQLEgvqlpePDEPSARHA-----LP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 318 VGDRLgnevIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG-REQPDSGEVKL-------GQTV 389
Cdd:PRK10938 256 ANEPR----IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLfgrrrgsGETI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -----KLAYVDQS-----RDS-------LEGnktVFD------AVADGADLLTvgkfempsRAYLGRFNFKGGDQNKIVG 446
Cdd:PRK10938 332 wdikkHIGYVSSSlhldyRVStsvrnviLSG---FFDsigiyqAVSDRQQKLA--------QQWLDILGIDKRTADAPFH 400
|
330 340 350
....*....|....*....|....*....|....
gi 489917580 447 QLSGGERgRLHL-AKTLIAGGNVLLLDEPSNDLD 479
Cdd:PRK10938 401 SLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLD 433
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-231 |
1.70e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdkeiegeaipmpglnigYLPQE-------PELNPEHtvRQSVEE 92
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----------------YLPQRgrvkvmgREVNAEN--EKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 GLGAVFNAKQrlDEVYAAYAEPDADFDALAAEQAeleaviaaaassgADDIEHQMEIAADALRL------PPWdamvgKL 166
Cdd:PRK13647 80 KVGLVFQDPD--DQVFSSTVWDDVAFGPVNMGLD-------------KDEVERRVEEALKAVRMwdfrdkPPY-----HL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL---HKFPGTVVAVTHDryfLDNAAEW 231
Cdd:PRK13647 140 SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdrlHNQGKTVIVATHD---VDLAAEW 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-238 |
1.88e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 24 DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLP----------QEPELNPEHTVRQSVEEG 93
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQ-IMLDGVDLSHVPpyqrpinmmfQSYALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 LgavfnaKQ-RLdevyaayaePDADFDALAAEQAELEaviaaaassgaddieHQMEIAAdalRLPpwdamvGKLSGGEKR 172
Cdd:PRK11607 116 L------KQdKL---------PKAEIASRVNEMLGLV---------------HMQEFAK---RKP------HQLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDA--------ESVEWLEqflhKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-519 |
2.03e-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: 75.20 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR-----LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVklAYVDQS---- 397
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEpwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RDSLEGN------------KTVFDAVADGADLLtvgkfempsraylgrfNFKGGDQNkIVGQ----LSGGERGRLHLAKT 461
Cdd:cd03250 79 NGTIRENilfgkpfdeeryEKVIKACALEPDLE----------------ILPDGDLT-EIGEkginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 462 LIAGGNVLLLDEPSNDLDVETLRAL-EDAL---LEFPGSVMVISHDRWFLDRiATHILAFEG 519
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-238 |
2.16e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.48 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGL-----------NIGYLPQEPELNPEHTVRQSV 90
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHdvvreprevrrRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEgLGAVFN-----AKQRLDEVYAAYAEPDADfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwDAMVGK 165
Cdd:cd03265 95 YI-HARLYGvpgaeRRERIDELLDFVGLLEAA------------------------------------------DRLVKT 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV----EWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-223 |
2.22e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLN-----IGYLPQEPeLNPEH-T 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTpqsgtvFLGDKPISMLSSRqlarrLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGAVFNAKQRLdevyaayaepdADFDALAAEQAeleaviaaaassgaddiEHQMEIAADALRLppwdamVGK 165
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRL-----------SAEDNARVNQA-----------------MEQTRINHLADRR------LTD 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEW--LEQFLHKFPGTVVAVTHD-----RY 223
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQVELmrLMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
326-504 |
2.56e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLgQTVKLAYVD---------- 395
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPpyqrpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QSRdSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKGGDQNKiVGQLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:PRK11607 98 QSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVneMLGLVHMQEFAKRK-PHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 474 PSNDLDvETLR---ALE--DALLEFPGSVMVISHDR 504
Cdd:PRK11607 176 PMGALD-KKLRdrmQLEvvDILERVGVTCVMVTHDQ 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-238 |
2.91e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGA 96
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN-VSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VfNAKQRldeVYAAYAEPDADFDAL-AAEQAEleaviaaaassGADDIEHQMEIAA-DALRLPPwdamvgKLSGGEKRRV 174
Cdd:PRK10419 102 V-NPRKT---VREIIREPLRHLLSLdKAERLA-----------RASEMLRAVDLDDsVLDKRPP------QLSGGQLQRV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
336-384 |
3.16e-15 |
|
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: 74.88 E-value: 3.16e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489917580 336 YGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK 384
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
330-503 |
3.30e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.73 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 330 NHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV----KLGQTVKLA------------- 392
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYalseaerrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 ---YVDQS-RDSLEGnktvfdAVADGAD----LLTVGkfempSRAYlGRFNFKGG--------DQNKI---VGQLSGGER 453
Cdd:PRK11701 90 ewgFVHQHpRDGLRM------QVSAGGNigerLMAVG-----ARHY-GDIRATAGdwlerveiDAARIddlPTTFSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 454 GRLHLAKTLIAGGNVLLLDEPSNDLDV-------ETLRALedaLLEFPGSVMVISHD 503
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGL---VRELGLAVVIVTHD 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
328-485 |
3.82e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 328 EFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD---SGEVKLGQTVKLAYVDQSR------ 398
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRrigilf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 -DSLegnktVFDAVADGADLLtvgkFEMPSRayLGRFNFK------------GGDQNKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:COG4136 83 qDDL-----LFPHLSVGENLA----FALPPT--IGRAQRRarveqaleeaglAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180
....*....|....*....|
gi 489917580 466 GNVLLLDEPSNDLDVeTLRA 485
Cdd:COG4136 152 PRALLLDEPFSKLDA-ALRA 170
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-192 |
4.07e-15 |
|
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: 75.00 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAI---PMPG---LNIGYLPQEPELNPEHT 85
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRpdagkiLIDGQDIthlPMHErarLGIGYLPQEASIFRKLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEeglgAVFNAKQRLDEvyaayAEPDADFDALAAEQaeleaviaaaassgadDIEHqmeiaadaLRlppwDAMVGK 165
Cdd:TIGR04406 93 VEENIM----AVLEIRKDLDR-----AEREERLEALLEEF----------------QISH--------LR----DNKAMS 135
|
170 180
....*....|....*....|....*..
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEP 192
Cdd:TIGR04406 136 LSGGERRRVEIARALATNPKFILLDEP 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-220 |
4.19e-15 |
|
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: 74.07 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGlnigylpqepelNPEHTVRQSVEE------ 92
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGR-VLLNG------------GPLDFQRDSIARgllylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 ---GLGAVFNAKQRLdEVYAAYAEPDADFDALAaeqaeleaviaaaassgaddiehQMEIAADAlrlppwDAMVGKLSGG 169
Cdd:cd03231 80 hapGIKTTLSVLENL-RFWHADHSDEQVEEALA-----------------------RVGLNGFE------DRPVAQLSAG 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTH 220
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-238 |
4.28e-15 |
|
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: 75.46 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEaipmpglNIGYLP-------------QEPEL 80
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGR-------DITGLPphriarlgiartfQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 81 NPEHTVRQSVEegLGAVFNAKQRLDEVYAAYAEPDADFDALAAEQAELeaviaaaassgaddIEhQMEIAADAlrlppwD 160
Cdd:COG0411 91 FPELTVLENVL--VAAHARLGRGLLAALLRLPRARREEREARERAEEL--------------LE-RVGLADRA------D 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 161 AMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTHDRYFLDNAAEWILELD 236
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDergiTILLIEHDMDLVMGLADRIVVLD 227
|
..
gi 489917580 237 RG 238
Cdd:COG0411 228 FG 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-503 |
4.77e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.44 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 322 LGNEVIEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG------QTV---- 389
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSR--AYLGRFNFKG-GDQNKivGQLSGGERGRLHLAKTLIAG 465
Cdd:PRK13635 81 rQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERvdQALRQVGMEDfLNREP--HRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 466 GNVLLLDEPSNDLD-------VETLRALEDallEFPGSVMVISHD 503
Cdd:PRK13635 159 PDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-193 |
5.19e-15 |
|
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: 74.63 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAI-PMP-----GLNIGYLPQEPELNPEHTVR 87
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPprsgsiRFDGEDItGLPphriaRLGIGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEegLGAVF-----NAKQRLDEVYAAyaepdadFDALAaeqaELeaviaaaassgaddiehqmeiaadalrlppWDAM 162
Cdd:COG0410 97 ENLL--LGAYArrdraEVRADLERVYEL-------FPRLK----ER------------------------------RRQR 133
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 163 VGKLSGGEKRRVALCRLLLSKPDMLLLDEPT 193
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-238 |
5.34e-15 |
|
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: 74.43 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLNIGYL-------PQEPELNpEHT 85
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkPISQYEHKYLhskvslvGQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGAVfnakqRLDEVYAAYAEPDADfdalaaeqaeleaviaaaassgaDDI-EHQMEIAADAlrlppwDAMVG 164
Cdd:cd03248 104 LQDNIAYGLQSC-----SFECVKEAAQKAHAH-----------------------SFIsELASGYDTEV------GEKGS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHdRYFLDNAAEWILELDRG 238
Cdd:cd03248 150 QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH-RLSTVERADQILVLDGG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-235 |
5.48e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-----------DKEIEGEAIPMPGLNIGYLPQEPELNPEHTVRQS 89
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEEGLGAvfnAKQRLDevyaayaePDADFDALAAEQAeleaviaaaassgaddIEhQMEIAADAlrlppwDAMVGKLSGG 169
Cdd:PRK09536 98 VEMGRTP---HRSRFD--------TWTETDRAAVERA----------------ME-RTGVAQFA------DRPVTSLSGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDA-ESVEWLE--QFLHKFPGTVVAVTHDryfLDNAAEWILEL 235
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLElvRRLVDDGKTAVAAIHD---LDLAARYCDEL 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-229 |
5.52e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 26 SLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEIEGE---AIPMPGLNIGYLPQEPELNPEHTVRQSVeeGLGa 96
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFltpasgSLTLNGQdhtTTPPSRRPVSMLFQENNLFSHLTVAQNI--GLG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 vFNAKQRLDevyaayaepdadfdalAAEQAELEaviaaaassgadDIEHQMEIAADALRLPpwdamvGKLSGGEKRRVAL 176
Cdd:PRK10771 96 -LNPGLKLN----------------AAQREKLH------------AIARQMGIEDLLARLP------GQLSGGQRQRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDryfLDNAA 229
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEDAA 194
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
233-300 |
6.53e-15 |
|
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: 69.91 E-value: 6.53e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 233 LELDRGYGIPWKGNYSSWLEQKEDRLKQEEATESARQKTIKKELEWVRQNPKG--RQAKAKARIARFEEL 300
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKasKAKQAQSRIKALEKM 70
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
344-501 |
7.38e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTVK-------LAYVDQSRDSLEGNKTVFDAVADGA 415
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRqalqknlVAYVPQSEEVDWSFPVLVEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 416 DLLTVGKFEMPSR-------AYLGRFNFKGGDQNKIvGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET------ 482
Cdd:PRK15056 105 RYGHMGWLRRAKKrdrqivtAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTeariis 183
|
170 180
....*....|....*....|
gi 489917580 483 -LRALEDAllefpGSVMVIS 501
Cdd:PRK15056 184 lLRELRDE-----GKTMLVS 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
291-491 |
8.21e-15 |
|
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: 77.47 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 291 KARIA--RFEE--LSSYEYQKRNETQEIFIPVGDrlgnevIEFNHVSKAYG-DRLLIDDLSFKVPAGAIVGIIGPNGAGK 365
Cdd:TIGR01193 440 AARVAnnRLNEvyLVDSEFINKKKRTELNNLNGD------IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 366 STLFRMLAGREQPDSGEVKLGQTvKLAYVD-----QSRDSLEGNKTVFDAVAdgADLLTVGKFEMPSRAYLGRF------ 434
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGF-SLKDIDrhtlrQFINYLPQEPYIFSGSI--LENLLLGAKENVSQDEIWAAceiaei 590
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 435 -----NFKGGDQNKIV---GQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALL 491
Cdd:TIGR01193 591 kddieNMPLGYQTELSeegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL 655
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
332-479 |
9.43e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.84 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 332 VSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------KLAYVDQSRdSLE 402
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaerGVGMVFQSY-ALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 GNKTVFDAVADGADLLTVGKFEMPSR-----------AYLGRfnfkggdQNKivgQLSGGERGRLHLAKTLIAGGNVLLL 471
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEINQRvnqvaevlqlaHLLDR-------KPK---ALSGGQRQRVAIGRTLVAEPSVFLL 157
|
....*...
gi 489917580 472 DEPSNDLD 479
Cdd:PRK11000 158 DEPLSNLD 165
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-238 |
1.08e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 74.41 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQEpELNPehtVRQSVeeglGAVF 98
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT-VTIDGRDITAKKKK-KLKD---LRKKV----GLVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 99 nakQrldevyaaYAEpdadfDALAAEQAEleaviaaaassgaDDI-----------EHQMEIAADALRlppwdaMVG--- 164
Cdd:TIGR04521 89 ---Q--------FPE-----HQLFEETVY-------------KDIafgpknlglseEEAEERVKEALE------LVGlde 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 --------KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEQF--LHKFPG-TVVAVTHDryfLDNAAEW- 231
Cdd:TIGR04521 134 eylerspfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVILVTHS---MEDVAEYa 210
|
....*....
gi 489917580 232 --ILELDRG 238
Cdd:TIGR04521 211 drVIVMHKG 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-201 |
1.15e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.49 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNI-------GYLPQEPELNPEHTV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDInklrrkvGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGLGAVfnAKQRLDEvyaayaepdadfdalAAEQAE--LEaviaaaassgaddiehQMEIAADAlrlppwDAMVG 164
Cdd:COG1126 95 LENVTLAPIKV--KKMSKAE---------------AEERAMelLE----------------RVGLADKA------DAYPA 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV 201
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELV 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-480 |
1.21e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAI----PMPGLNIG-YL-PQEPELNPEHTVRQ 88
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarltPAKAHQLGiYLvPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEEGLGAVFNAKQRLDEVyaayaepdadfdaLAAEQAELEAviaaaassgaddiehqmeiaadalrlppwDAMVGKLSG 168
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQL-------------LAALGCQLDL-----------------------------DSSAGSLEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGT---VVAVTHDRYFLDNAAEWILELDRGYGIpwkg 245
Cdd:PRK15439 144 ADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKLPEIRQLADRISVMRDGTIA---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 246 nysswLEQKEDRLKQEEATESARQKTIKKELE-----WVRQNPKGRQAKAKARIARFEELSSyeyqkrnetqEIFIpvgd 320
Cdd:PRK15439 220 -----LSGKTADLSTDDIIQAITPAAREKSLSasqklWLELPGNRRQQAAGAPVLTVEDLTG----------EGFR---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 321 rlgneviefnhvskaygdrllidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK--------- 390
Cdd:PRK15439 281 -----------------------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLnGKEINalstaqrla 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 --LAYVDQSRDSlegNKTVFDA-VADGADLLTVGK---FEMPSR--AYLGRF----NFKGGDQNKIVGQLSGGERGRLHL 458
Cdd:PRK15439 338 rgLVYLPEDRQS---SGLYLDApLAWNVCALTHNRrgfWIKPARenAVLERYrralNIKFNHAEQAARTLSGGNQQKVLI 414
|
490 500
....*....|....*....|..
gi 489917580 459 AKTLIAGGNVLLLDEPSNDLDV 480
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDV 436
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-514 |
1.35e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 73.61 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTvKLAYVDQSRDSLEG------NKTVFDAvadga 415
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEIARLGigrkfqKPTVFEE----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 416 dlLTV-------GKFEMPSRAYLgRFNFKGGDQNKI----------------VGQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:COG4674 100 --LTVfenlelaLKGDRGVFASL-FARLTAEERDRIeevletigltdkadrlAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 473 EPSNDL-DVETLRALEdALLEFPG--SVMVISHDRWFLDRIATHI 514
Cdd:COG4674 177 EPVAGMtDAETERTAE-LLKSLAGkhSVVVVEHDMEFVRQIARKV 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-200 |
1.46e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 72.92 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGL-----------NIGYLPQEPELNPEHTVRQS 89
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-INGYsirtdrkaarqSLGYCPQFDALFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEeglgavFNAkqRLDEVYaayaepdadfdalaaeqaeleaviaaaassgADDIEHQMEIAADALRLPP-WDAMVGKLSG 168
Cdd:cd03263 96 LR------FYA--RLKGLP-------------------------------KSEIKEEVELLLRVLGLTDkANKRARTLSG 136
|
170 180 190
....*....|....*....|....*....|..
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 200
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
328-530 |
1.52e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 328 EFNHVSKAY-GDRLLiDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAyvdqsrdslegnk 405
Cdd:PRK11288 6 SFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFA------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 TVFDAVADGA-----DLLTVGKFEMPSRAYLGRFNFKGG----------------------DQNKIVGQLSGGERGRLHL 458
Cdd:PRK11288 72 STTAALAAGVaiiyqELHLVPEMTVAENLYLGQLPHKGGivnrrllnyeareqlehlgvdiDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 459 AKTLIAGGNVLLLDEPSNDL---DVETLRALEDALLEFPGSVMVISHDrwfLDRIathilaFE-GDSQVVFFDGNY 530
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSHR---MEEI------FAlCDAITVFKDGRY 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
331-479 |
2.15e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQT------------VKLAYVDQSR 398
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 dSLEGNKTVFD---AVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNkiVGQ-LSGGERGRLHLAKTLIAGGNVLLLDEP 474
Cdd:PRK10895 88 -SIFRRLSVYDnlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDS--MGQsLSGGERRRVEIARALAANPKFILLDEP 164
|
....*
gi 489917580 475 SNDLD 479
Cdd:PRK10895 165 FAGVD 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-239 |
3.04e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPG---------LNIGYLPQ-EPELNPEH 84
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEvlwqGEPIRRqrdeyhqdlLYLGHQPGiKTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRqsveeglgavFNAKQrldevyAAYAEPDADFDALAaeqaeleaviaaaassgaddiehQMEIAADAlrlppwDAMVG 164
Cdd:PRK13538 94 NLR----------FYQRL------HGPGDDEALWEALA-----------------------QVGLAGFE------DVPVR 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL--H-KFPGTVVAVTHDRYFLDNAAewILELDRGY 239
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqHaEQGGMVILTTHQDLPVASDK--VRKLRLGQ 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
333-518 |
3.23e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.99 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 333 SKAYGDRLLidDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------------KLAYVDQ- 396
Cdd:TIGR02142 6 SKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 -----------------SRDSLEGNKTVFDAVADgadLLTVGKFempsrayLGRFnfkggdqnkiVGQLSGGERGRLHLA 459
Cdd:TIGR02142 84 arlfphlsvrgnlrygmKRARPSERRISFERVIE---LLGIGHL-------LGRL----------PGRLSGGEKQRVAIG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 460 KTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFE 518
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
334-515 |
3.71e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 334 KAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAyvdqsRDS------------ 400
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLV-----RDKdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 ---------------LEGNKTVFDAVADG-ADLLTVGKFEMPSRA--YLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTL 462
Cdd:PRK10619 88 rllrtrltmvfqhfnLWSHMTVLENVMEApIQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 463 IAGGNVLLLDEPSNDLDV----ETLRALEDaLLEFPGSVMVISHDRWFLDRIATHIL 515
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-198 |
4.07e-14 |
|
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: 71.92 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 3 QYVYTMNRVGKIVP---PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE---------IEGEAiPMPGL- 69
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQP-RKPDQf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 70 --NIGYLPQEPELNPEHTVRQSVeeglgaVFNAKQRLDEvyaayaepdadfdalaaeqaeleaVIAAAASSGADDIEHQM 147
Cdd:cd03234 80 qkCVAYVRQDDILLPGLTVRETL------TYTAILRLPR------------------------KSSDAIRKKRVEDVLLR 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 148 EIAADALRlppwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 198
Cdd:cd03234 130 DLALTRIG----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-221 |
4.17e-14 |
|
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: 71.98 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQI--LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMpglniGYLPQEPElnPEHTVRqsveeg 93
Cdd:cd03267 29 RKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPWKRR--KKFLRR------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 LGAVFNAKQRL-------DEVY---AAYAEPDADFDALAAEQAELEaviaaaassgadDIEHQMeiaadalrlppwDAMV 163
Cdd:cd03267 96 IGVVFGQKTQLwwdlpviDSFYllaAIYDLPPARFKKRLDELSELL------------DLEELL------------DTPV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 164 GKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF----PGTVVAVTHD 221
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-254 |
4.45e-14 |
|
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: 75.16 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLN------------IGYLPQEPelnpeHTV 86
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE-ILLNGFSlkdidrhtlrqfINYLPQEP-----YIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGL--GAVFNAKQrlDEVYAayaepdadfdalAAEQAELEaviaaaassgaDDIE-----HQMEIAADAlrlppw 159
Cdd:TIGR01193 561 SGSILENLllGAKENVSQ--DEIWA------------ACEIAEIK-----------DDIEnmplgYQTELSEEG------ 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 160 damvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEQFLHKfpgTVVAVTHdRYFLDNAAEWILEL 235
Cdd:TIGR01193 610 ----SSISGGQKQRIALARALLTDSKVLILDESTSNLDTitekKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVL 681
|
250
....*....|....*....
gi 489917580 236 DRGyGIPWKGNYSSWLEQK 254
Cdd:TIGR01193 682 DHG-KIIEQGSHDELLDRN 699
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-220 |
6.09e-14 |
|
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: 70.98 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 24 DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLP----------QEPELNPEHTVRQSVeeG 93
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGR-VLINGVDVTAAPpadrpvsmlfQENNLFAHLTVEQNV--G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 LGAVFNAKqrldevyaayaepdadfdaLAAEQAEleaviaaaassGADDIEHQMEIAADALRLPpwdamvGKLSGGEKRR 173
Cdd:cd03298 93 LGLSPGLK-------------------LTAEDRQ-----------AIEVALARVGLAGLEKRLP------GELSGGERQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 174 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQF---LHKFPG-TVVAVTH 220
Cdd:cd03298 137 VALARVLVRDKPVLLLDEPFAALDPALRAEMLDLvldLHAETKmTVLMVTH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
6.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLNIgylpqepelnpeHTVRQSVeegl 94
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgePITKENI------------REVRKFV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 GAVFNAKQrlDEVYAAYAEPDADFDALAAEQAEleaviaaaassgaDDIEHQMEIAADALRLPPW-DAMVGKLSGGEKRR 173
Cdd:PRK13652 81 GLVFQNPD--DQIFSPTVEQDIAFGPINLGLDE-------------ETVAHRVSSALHMLGLEELrDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 174 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-227 |
6.73e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 70.03 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAipmpglnigYLPQEPELNPEHTVRQSVeeglgAVFN 99
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEKALSSLI-----SVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 100 AKQRLdevyaayaepdadFDALAAEQaeleaviaaaassgaddiehqmeiaadalrlppwdamVGK-LSGGEKRRVALCR 178
Cdd:cd03247 82 QRPYL-------------FDTTLRNN-------------------------------------LGRrFSGGERQRLALAR 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 179 LLLSKPDMLLLDEPTNHLDAES-VEWLEQFLHKFPG-TVVAVTH--------DR-YFLDN 227
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHhltgiehmDKiLFLEN 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
326-485 |
7.58e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.91 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY--GDRLLI--DDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVklgqtvklaYVD------ 395
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV---------LVDgqdlta 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 -------QSRDS---------LEGNKTVFDAVADGADLLTVGKFEMPSR--AYLgrfnfkggdqnKIVG----------Q 447
Cdd:PRK11153 72 lsekelrKARRQigmifqhfnLLSSRTVFDNVALPLELAGTPKAEIKARvtELL-----------ELVGlsdkadrypaQ 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 489917580 448 LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRA 485
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
324-503 |
7.90e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.14 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGE--------VKLGQ-TV--- 389
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAkTVwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 --KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPS-----RAYLGRFNFkggdQNKIVGQLSGGERGRLHLAKTL 462
Cdd:PRK13640 83 reKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKivrdvLADVGMLDY----IDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 463 IAGGNVLLLDEPSNDLDVE----TLRALEDALLEFPGSVMVISHD 503
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAgkeqILKLIRKLKKKNNLTVISITHD 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-221 |
8.11e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLN-------IGYLPQEPELNPEHT 85
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqPLESWSskafarkVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGAVFNAKQRldevyaayaepdadfdaLAAEQAEleaviaaaassgaddiehQMEIAADALRLPPW-DAMVG 164
Cdd:PRK10575 102 VRELVAIGRYPWHGALGR-----------------FGAADRE------------------KVEEAISLVGLKPLaHRLVD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLE--QFLHKFPG-TVVAVTHD 221
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLAlvHRLSQERGlTVIAVLHD 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
327-533 |
8.34e-14 |
|
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: 70.52 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRL--LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSLE- 402
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDISTIPLEDLRSSLTi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 --GNKTVFdavaDGADLLTVGKFEMPSRAYL-GRFNFKGGDQNkivgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:cd03369 87 ipQDPTLF----SGTIRSNLDPFDEYSDEEIyGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 480 VETlraleDALL------EFPGS-VMVISHdrwfldRIATHIlafEGDSQVVFFDGNYQEY 533
Cdd:cd03369 158 YAT-----DALIqktireEFTNStILTIAH------RLRTII---DYDKILVMDAGEVKEY 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-221 |
8.78e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 71.43 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEIEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVEE 92
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFlapssgEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 GLgavfnakqRLDEVyaayaePDADFDALAAEQAELEAViaaaassgaddiehqmeiaADALRLPPWdamvgKLSGGEKR 172
Cdd:COG4525 100 GL--------RLRGV------PKAERRARAEELLALVGL-------------------ADFARRRIW-----QLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL-------HKfpgTVVAVTHD 221
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwqrtGK---GVFLITHS 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-221 |
8.85e-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: 70.36 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI---------PMPGLNIGYLPQEPELNPEHTVR 87
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLgavfnaKQRldevyaayAEPDADFDALAAEQAELEaviaaaassgadDIEHQMEiaadalRLPpwdamvGKLS 167
Cdd:cd03301 91 DNIAFGL------KLR--------KVPKDEIDERVREVAELL------------QIEHLLD------RKP------KQLS 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:cd03301 133 GGQRQRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-220 |
9.33e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 71.03 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLN------------IGYLPQEPELnpeh 84
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGE-ILLDGVDirdlnlrwlrsqIGLVSQEPVL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 tvrqsveeglgavFNAKQRLDEVYAAYAEPDADFDAlAAEQAELEaviaaaassgaDDIEhqmeiaadalRLP-PWDAMV 163
Cdd:cd03249 89 -------------FDGTIAENIRYGKPDATDEEVEE-AAKKANIH-----------DFIM----------SLPdGYDTLV 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 164 G----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTH 220
Cdd:cd03249 134 GergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-220 |
9.36e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 68.99 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMpglnigylpqepelnpeHTVRQSVEEG 93
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKpdsgeiLVDGKEVSF-----------------ASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 LGAVfnakqrldevyaayaepdadfdalaaeqaeleaviaaaassgaddieHQmeiaadalrlppwdamvgkLSGGEKRR 173
Cdd:cd03216 77 IAMV-----------------------------------------------YQ-------------------LSVGERQM 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489917580 174 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTH 220
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
327-518 |
1.01e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSLEGNK 405
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaGHQFDFSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 ---------------TVFDAVADG-ADLLTVGKFEMPSRA-----------YLGRFNFkggdqnkivgQLSGGERGRLHL 458
Cdd:COG4161 83 kvgmvfqqynlwphlTVMENLIEApCKVLGLSKEQAREKAmkllarlrltdKADRFPL----------HLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 459 AKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHILAFE 518
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYME 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-220 |
1.15e-13 |
|
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: 70.69 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 7 TMNRVGKIVPPKRQ---ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLpQEPELNPe 83
Cdd:cd03258 3 ELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS-VLVDGTDLTLL-SGKELRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 htVRQSVeeglGAVF------NAKQRLDEVyaayaepdadfdALAAEQAELEaviaaaassgaddiehQMEIAADALRLP 157
Cdd:cd03258 80 --ARRRI----GMIFqhfnllSSRTVFENV------------ALPLEIAGVP----------------KAEIEERVLELL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 158 PW-------DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLH----KFPGTVVAVTH 220
Cdd:cd03258 126 ELvgledkaDAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRdinrELGLTIVLITH 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
327-523 |
1.31e-13 |
|
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: 69.14 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD-RLLIDDLSFKvpAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLgQTVKLAYVDQSRDslegnk 405
Cdd:cd03222 1 QLYPDCVKRYGVfFLLVELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYID------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 tvfdavadgadlltvgkfempsraylgrfnfkggdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE---- 481
Cdd:cd03222 72 ------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrln 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 482 TLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEGDSQV 523
Cdd:cd03222 110 AARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-238 |
1.60e-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: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNIGylpqepeLNPEHTVRQS 89
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgtvTVRGRVSSLLGLGGG-------FNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VeeglgaVFNA----------KQRLDEVYaayaepdaDFdalaaeqAELEaviaaaassgaddiehqmeiaaDALRLPpw 159
Cdd:cd03220 105 I------YLNGrllglsrkeiDEKIDEII--------EF-------SELG----------------------DFIDLP-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 160 damVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF---PGTVVAVTHDRYFLDNAAEWILELD 236
Cdd:cd03220 140 ---VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLE 216
|
..
gi 489917580 237 RG 238
Cdd:cd03220 217 KG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
166-231 |
2.25e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 2.25e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEQF--LHKFPGTVVAVTHDryfLDNAAEW 231
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkEILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-221 |
2.40e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQE--PELNPEHT--VRQSVEegLGA 96
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGE-VSLVGQPLHQMDEEarAKLRAKHVgfVFQSFM--LIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VFNAKQRLDEVYAAYAEPDADFDALAAEQAEleaviaaaassgaddiehQMEIAADALRLPpwdamvGKLSGGEKRRVAL 176
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGAKALLE------------------QLGLGKRLDHLP------AQLSGGEQQRVAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTHD 221
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-200 |
2.41e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPG------LNIGYLPQEPELNPEHTVRQSV 90
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EeglgavfnakqrldeVYAAYaepdadFDALAAEQAELeaviaaaassgaddIEHQMEIAadalRLP-PWDAMVGKLSGG 169
Cdd:PRK13537 102 L---------------VFGRY------FGLSAAAARAL--------------VPPLLEFA----KLEnKADAKVGELSGG 142
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAES 200
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-221 |
2.83e-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: 69.57 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------AIPMPGLNIGYLPQEPELNPEHTVRQSV 90
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEilldgkditNLPPHKRPVNTVFQNYALFPHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEGLgavfnakqRLDEVyaayaePDADFDALAAEQAELEaviaaaassgaddiehQMEIAADAlrlppwdaMVGKLSGGE 170
Cdd:cd03300 94 AFGL--------RLKKL------PKAEIKERVAEALDLV----------------QLEGYANR--------KPSQLSGGQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLeQF----LHKFPG-TVVAVTHD 221
Cdd:cd03300 136 QQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM-QLelkrLQKELGiTFVFVTHD 190
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
325-509 |
3.11e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 325 EVIEFNHvskAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK---LAYVDQ---- 396
Cdd:PRK13540 3 DVIELDF---DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlCTYQKQlcfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 -SRDSLEGNKTV-----FDAVADGADLltvGKFEMPSRAYLGRF-NFKggdqnkiVGQLSGGERGRLHLAKTLIAGGNVL 469
Cdd:PRK13540 80 gHRSGINPYLTLrenclYDIHFSPGAV---GITELCRLFSLEHLiDYP-------CGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489917580 470 LLDEPSNDLD---VETLRALEDALLEFPGSVMVISHDRWFLDR 509
Cdd:PRK13540 150 LLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-480 |
5.29e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaipmpglnIGYLPQEPELN-PehtvRQSVEEGLG 95
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS--------ILYLGKEVTFNgP----KSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQRLDEVYAAY-----AEPDADFDAlaaeqaeleaviaaaassgaddIEHQ-MEIAADAL--RLP---PWDAMVG 164
Cdd:PRK10762 83 IIHQELNLIPQLTIAEniflgREFVNRFGR----------------------IDWKkMYAEADKLlaRLNlrfSSDKLVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHL-DAESvewleQFLHKFpgtvvavthdryfldnaaewILEL-DRGYGIP 242
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-----ESLFRV--------------------IRELkSQGRGIV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 243 wkgnYSSwleqkeDRLKqeEATESARQKTIKKELEWVRQNPkgrqakakariarFEELssyeyqkrNETQEIFIPVGDRL 322
Cdd:PRK10762 196 ----YIS------HRLK--EIFEICDDVTVFRDGQFIAERE-------------VADL--------TEDSLIEMMVGRKL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 323 GNEvieFNHVSKAYGDRLL---------IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK-- 390
Cdd:PRK10762 243 EDQ---YPRLDKAPGEVRLkvdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtr 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 ---------LAYV--DQSRD------SLEGNK--TVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGG 451
Cdd:PRK10762 320 spqdglangIVYIseDRKRDglvlgmSVKENMslTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGG 399
|
490 500
....*....|....*....|....*....
gi 489917580 452 ERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
335-524 |
5.35e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 335 AYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG--QTVKLAYVDQSRD--------SLEGN 404
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDgeHIQHYASKEVARRigllaqnaTTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 KTVFDAVADGadlltvgkfEMPSRAYLGRFNFKGGD--------------QNKIVGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:PRK10253 96 ITVQELVARG---------RYPHQPLFTRWRKEDEEavtkamqatgithlADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 471 LDEPSNDLD----VETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEgDSQVV 524
Cdd:PRK10253 167 LDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALR-EGKIV 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
5.77e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 69.66 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 4 YVYTMNrvgkiVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaipmpgLNIGYLPQEPELNPE 83
Cdd:PRK13634 10 HRYQYK-----TPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIGERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 H--TVRQSVeeglGAVFN--AKQRLDEVYAA--------YAEPDADFDALAAEQAELeaviaaaassgaddiehqMEIAA 151
Cdd:PRK13634 79 KlkPLRKKV----GIVFQfpEHQLFEETVEKdicfgpmnFGVSEEDAKQKAREMIEL------------------VGLPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 152 DALRLPPWDamvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEQF--LHKFPG-TVVAVTHDryfLDN 227
Cdd:PRK13634 137 ELLARSPFE-----LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGrKEMMEMFykLHKEKGlTTVLVTHS---MED 208
|
....
gi 489917580 228 AAEW 231
Cdd:PRK13634 209 AARY 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-241 |
5.94e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.38 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 4 YVYTMNRvgkivPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGLNIGYLPQEPELNPe 83
Cdd:PRK13643 9 YTYQPNS-----PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG-KVTVGDIVVSSTSKQKEIKP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 htVRQSVeeglGAVFNAKQrlDEVYAAYAEPDADFD----ALAAEQAEleaviaaaassgaddiehqmEIAADALRLPP- 158
Cdd:PRK13643 82 --VRKKV----GVVFQFPE--SQLFEETVLKDVAFGpqnfGIPKEKAE--------------------KIAAEKLEMVGl 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 159 ----WDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEQF--LHKFPGTVVAVTHDRYFLDNAAEW 231
Cdd:PRK13643 134 adefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTHLMDDVADYADY 213
|
250
....*....|
gi 489917580 232 ILELDRGYGI 241
Cdd:PRK13643 214 VYLLEKGHII 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
327-524 |
7.33e-13 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 68.34 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR---LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LA 392
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 YVDQSRDSLEGnkTVFDAVADGADLLTVGKFEMPSR-AYLGRFNFKGGDQ-NKIVG----QLSGGERGRLHLAKTLIAGG 466
Cdd:cd03249 81 LVSQEPVLFDG--TIAENIRYGKPDATDEEVEEAAKkANIHDFIMSLPDGyDTLVGergsQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 467 NVLLLDEPSNDLDVETLRALEDALLEFPGS--VMVISHdrwfldRIAT-----HILAFeGDSQVV 524
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH------RLSTirnadLIAVL-QNGQVV 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
331-519 |
7.79e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAY---------GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-----LGQ--------- 387
Cdd:PRK10419 8 GLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKlnraqrkaf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 388 --TVKLAYVDqSRDSLEGNKTVFDAVADGA-DLLTVGKFEMPSRA--YLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTL 462
Cdd:PRK10419 88 rrDIQMVFQD-SISAVNPRKTVREIIREPLrHLLSLDKAERLARAseMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 463 IAGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-220 |
8.82e-13 |
|
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: 67.69 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI-------PMPGLNIGYLPQEPELNPEHTVRQSvee 92
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLYPKMKVIDQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 93 glgAVFNAkqRLDEVYAAYAEPDADfDALaaEQAELEAViaaaassgaddiehqmeiaadalrlppWDAMVGKLSGGEKR 172
Cdd:cd03269 91 ---LVYLA--QLKGLKKEEARRRID-EWL--ERLELSEY---------------------------ANKRVEELSKGNQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTH 220
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-197 |
8.96e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----AIPMPG------LNIGYLPQEPELNPEHTVRQSV 90
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEgLGAVFNAKQRldevyaayaEPDADFDALAaEQAELEAVIaaaassgaddiehqmeiaadalrlppwDAMVGKLSGGE 170
Cdd:PRK13536 136 LV-FGRYFGMSTR---------EIEAVIPSLL-EFARLESKA---------------------------DARVSDLSGGM 177
|
170 180
....*....|....*....|....*..
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-220 |
1.08e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.62 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKImagvdkeiegeaipmpgLNIGYLPQEPE--LN-------PEHTVRQSV 90
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL-----------------LTRAWDPQQGEilLNgqpiadySEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 eeglgAVFNakQRLDeVYAA-------YAEPDADFDALAA--EQAELEAVIaaaassgaDDIEhqmeiaadalrlpPWDA 161
Cdd:PRK11160 417 -----SVVS--QRVH-LFSAtlrdnllLAAPNASDEALIEvlQQVGLEKLL--------EDDK-------------GLNA 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 162 MVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTH 220
Cdd:PRK11160 468 WLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITH 532
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-208 |
1.13e-12 |
|
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: 67.39 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 13 KIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEG-EAIPMP---GLNIGYLPQEPELNP 82
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpdagfaTVDGfDVVKEPaeaRRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVE-----EGLgAVFNAKQRLDEVyaayaepdadFDALaaeqaeleaviaaaassgadDIEHQMeiaadalrlp 157
Cdd:cd03266 92 RLTARENLEyfaglYGL-KGDELTARLEEL----------ADRL--------------------GMEELL---------- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 158 pwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL 208
Cdd:cd03266 131 --DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-511 |
1.18e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 1 MAQYVYTMNRVGKIVPPKrQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPmpgLNIGYlpqePEL 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNINY----NKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 81 NPehtvRQSVEEGLGAVFNAKQRLDE------VYAAYAEPDADFDALAAEQAELEaviaaaassgaddIEHQMEIAADAL 154
Cdd:PRK09700 73 DH----KLAAQLGIGIIYQELSVIDEltvlenLYIGRHLTKKVCGVNIIDWREMR-------------VRAAMMLLRVGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 155 RLPPwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVThdrYFLDNAAEwILE 234
Cdd:PRK09700 136 KVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIV---YISHKLAE-IRR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 235 LDRGYGIPWKGNYsswleqkedrLKQEEATESARQKTIKKELewvrqnpkGRQAKAKariarfeelssyeYQKRNETqei 314
Cdd:PRK09700 211 ICDRYTVMKDGSS----------VCSGMVSDVSNDDIVRLMV--------GRELQNR-------------FNAMKEN--- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 315 fipVGDRLGNEVIEFNHVSKAygDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK--- 390
Cdd:PRK09700 257 ---VSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprs 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 --------LAYVDQSRD--------SLEGNKTVFDAVADGADLLTVGKFEMPSRAYLGR-----FNFKGGDQNKIVGQLS 449
Cdd:PRK09700 332 pldavkkgMAYITESRRdngffpnfSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAEnqrelLALKCHSVNQNITELS 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 450 GGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET-------LRALEDallEFPGSVMVISHDRWFL---DRIA 511
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeiykvMRQLAD---DGKVILMVSSELPEIItvcDRIA 480
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-221 |
1.21e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEAI----PMPGLNI-------GYLPQepelnpehtvrQSV 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILlngrPLSDWSAaelarhrAYLSQ-----------QQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEGLGAVFnakQRLdevyAAYAEPDADFDALAAEQAELeaviaaaassgaddiehqmeiaADALRLPP-WDAMVGKLSGG 169
Cdd:COG4138 80 PPFAMPVF---QYL----ALHQPAGASSEAVEQLLAQL----------------------AEALGLEDkLSRPLTQLSGG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 170 EKRRVALCRLLL-----SKPD--MLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTHD 221
Cdd:COG4138 131 EWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
327-492 |
1.34e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQ--PDSGEV--------------------- 383
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 384 ---KLGQTVKLAYVD--------------------QSRDSLEGNKTVFDAVADG-ADLLTVGKFEMPSRAYLGRFNFKGG 439
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDfwnlsdklrrrirkriaimlQRTFALYGDDTVLDNVLEAlEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 440 DQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE 492
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-210 |
1.40e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.50 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 6 YTMNRVGKivppKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGEaIPMPGL--------NIGYLP 75
Cdd:cd03232 11 YTVPVKGG----KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGE-ILINGRpldknfqrSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 76 QEPELNPEHTVRQSVEeglgavFNAKQRldevyaayaepdadfdALAAEQaeleaviaaaassgaddiehqmeiaadalr 155
Cdd:cd03232 86 QQDVHSPNLTVREALR------FSALLR----------------GLSVEQ------------------------------ 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 156 lppwdamvgklsggeKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHK 210
Cdd:cd03232 114 ---------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-238 |
1.48e-12 |
|
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: 67.91 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGAVfN 99
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGT-VSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAV-N 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 100 AKQRLDEVYAayaEPDADFDAL-AAEQAEleaviaaaassgadDIEHQMEI----AADALRLPPwdamvgKLSGGEKRRV 174
Cdd:TIGR02769 103 PRMTVRQIIG---EPLRHLTSLdESEQKA--------------RIAELLDMvglrSEDADKLPR------QLSGGQLQRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-544 |
1.54e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.63 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG-----REQPDSGEVKL-GQTVKLAYVDQSRD 399
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLdGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 SLE---------GNKTVFDAVADGADL--LTVGKFEMPSRAY--LGRFNFKGGDQNKI---VGQLSGGERGRLHLAKTLI 463
Cdd:PRK14247 83 RVQmvfqipnpiPNLSIFENVALGLKLnrLVKSKKELQERVRwaLEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 464 AGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDRIATHIlAFEGDSQVVfFDGNYQEYEADKKHRL 541
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYV-AFLYKGQIV-EWGPTREVFTNPRHEL 240
|
...
gi 489917580 542 GEE 544
Cdd:PRK14247 241 TEK 243
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-241 |
2.12e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaipmpgLNIGY----LPQEPELNPEHTVRQSVeeglG 95
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ------LNIAGhqfdFSQKPSEKAIRLLRQKV----G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFnakqrldEVYAAYAEpdadfdaLAAEQAELEAVIAAAASSGADDIEHQMEIAAdALRLPPW-DAMVGKLSGGEKRRV 174
Cdd:COG4161 86 MVF-------QQYNLWPH-------LTVMENLIEAPCKVLGLSKEQAREKAMKLLA-RLRLTDKaDRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 175 ALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQfLHKFPGTVVAVTHDRYFLDNAAEWILELDRGYGI 241
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDpeitAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-226 |
2.14e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.01 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK-EIEGEAIPMPGLNIgylpqePELNPEHTVRqsveegLGa 96
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVTEGEILFKGEDI------TDLPPEERAR------LG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 vfnakqrldeVYAAYAEPdadfdalaaeqaeleaviaaaassgaddiehqMEIA----ADALRlppwDAMVGkLSGGEKR 172
Cdd:cd03217 79 ----------IFLAFQYP--------------------------------PEIPgvknADFLR----YVNEG-FSGGEKK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF--PGT-VVAVTHDRYFLD 226
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLD 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
326-537 |
2.16e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG----REQPDSGEVKLGQTV----KLAY-VDQ 396
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgDKSAGSHIELLGRTVqregRLARdIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRD---------SLEGNKTVFDAVADGAdlLTVGKF----------EMPSRAY-----LGRFNFKggdqNKIVGQLSGGE 452
Cdd:PRK09984 84 SRAntgyifqqfNLVNRLSVLENVLIGA--LGSTPFwrtcfswftrEQKQRALqaltrVGMVHFA----HQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 453 RGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG----SVMVISHDRWFLDRIATHILAFEGDSqvVFFDG 528
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGH--VFYDG 235
|
....*....
gi 489917580 529 NYQEYEADK 537
Cdd:PRK09984 236 SSQQFDNER 244
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-254 |
2.39e-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: 66.87 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMA---GVDK---EIEGEAIPMPGLN-----IGYLPQEPELNPEhTV 86
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfyDVDSgriLIDGHDVRDYTLAslrrqIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVeeglgavfnakqrldevyaAYAEPDADFDAL--AAEQAELEaviaaaassgaDDIEhqmeiaadalRLPP-WDAMV 163
Cdd:cd03251 93 AENI-------------------AYGRPGATREEVeeAARAANAH-----------EFIM----------ELPEgYDTVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 164 G----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHDRYFLDNAAEwILELDR 237
Cdd:cd03251 133 GergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIENADR-IVVLED 211
|
250
....*....|....*..
gi 489917580 238 GyGIPWKGNYSSWLEQK 254
Cdd:cd03251 212 G-KIVERGTHEELLAQG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
336-518 |
2.76e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 336 YGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGqtvklayvDQSRDSLEGNK---------- 405
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR--------GQHIEGLPGHQiarmgvvrtf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 ---------TVFD--AVADGADL---LTVGKFEMPS----------RA--YLGRFNFKGGdQNKIVGQLSGGERGRLHLA 459
Cdd:PRK11300 87 qhvrlfremTVIEnlLVAQHQQLktgLFSGLLKTPAfrraesealdRAatWLERVGLLEH-ANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 460 KTLIAGGNVLLLDEPS---NDLDVETLRALEDALL-EFPGSVMVISHDRWFLDRIATHILAFE 518
Cdd:PRK11300 166 RCMVTQPEILMLDEPAaglNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
326-519 |
2.89e-12 |
|
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: 67.14 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLL---------IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQ-------- 387
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLfgakqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQdlyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 388 -------TVKLAYVDqSRDSLEGNKTVFDAVADG-ADLLTVGKFEMPSR--AYLGRFNFKGGDQNKIVGQLSGGERGRLH 457
Cdd:TIGR02769 82 qrrafrrDVQLVFQD-SPSAVNPRMTVRQIIGEPlRHLTSLDESEQKARiaELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
326-509 |
3.09e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG----------------QT 388
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlknrevpflrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 389 VKLAYVDQsrdSLEGNKTVFDAVAdgADLLTVGKFEMPSR----AYLGRFNFKGGDQNKIVgQLSGGERGRLHLAKTLIA 464
Cdd:PRK10908 81 IGMIFQDH---HLLMDRTVYDNVA--IPLIIAGASGDDIRrrvsAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDR 509
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISR 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
327-528 |
3.26e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.70 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV----------------- 389
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 --KLAYVDQSRDsLEGNKTVFDAVADGADLL---TVGKFEMPSRAYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PRK11264 84 rqHVGFVFQNFN-LFPHRTVLENIIEGPVIVkgePKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 465 GGNVLLLDEPSNDLDVE-------TLRALEDAllefpGSVMVishdrwfldrIATHILAFEGD--SQVVFFDG 528
Cdd:PRK11264 162 RPEVILFDEPTSALDPElvgevlnTIRQLAQE-----KRTMV----------IVTHEMSFARDvaDRAIFMDQ 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-514 |
3.29e-12 |
|
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: 66.62 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 346 SFK-----VPA-GAIVGIIGPNGAGKSTLFRMLAGREQPDSG----------------------------EVKLGQTVKL 391
Cdd:cd03236 14 SFKlhrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyftkllEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQSRDSLEGN----------KTVFDAVADGADLLTVGkfempsraylgrfnfkggDQNkiVGQLSGGERGRLHLAKT 461
Cdd:cd03236 94 QYVDLIPKAVKGKvgellkkkdeRGKLDELVDQLELRHVL------------------DRN--IDQLSGGELQRVAIAAA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 462 LIAGGNVLLLDEPSNDLDVE---TLRALEDALLEFPGSVMVISHDRWFLDRIATHI 514
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
342-503 |
4.05e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.95 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQ----SRDSLEGNKTVFDAVADGAD 416
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 417 L----LTVGKFEMPSRAYLGRFNFKGGdQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALL- 491
Cdd:TIGR01184 81 RvlpdLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMq 159
|
170
....*....|....*
gi 489917580 492 ---EFPGSVMVISHD 503
Cdd:TIGR01184 160 iweEHRVTVLMVTHD 174
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-479 |
4.06e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KLA 392
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 YVDQSrDSLEGNkTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:PRK10247 85 YCAQT-PTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*..
gi 489917580 473 EPSNDLD 479
Cdd:PRK10247 163 EITSALD 169
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
327-502 |
4.06e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY--GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAY 393
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLRdytlaslrnqVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQsrdslegNKTVF-DAVADGADLLTVGKFempSR---------AYLGRFnFKGGDQ--NKIVGQ----LSGGERGRLH 457
Cdd:PRK11176 422 VSQ-------NVHLFnDTIANNIAYARTEQY---SReqieeaarmAYAMDF-INKMDNglDTVIGEngvlLSGGQRQRIA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISH 502
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
337-515 |
4.28e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.24 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE--QPDSGEVKLgqtvklayvdqsrdslegnktvfdavaDG 414
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILF---------------------------KG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 415 ADLLtvgKFEMPSRAYLGRF-NFkggdQNKI---------------VGqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL 478
Cdd:cd03217 64 EDIT---DLPPEERARLGIFlAF----QYPPeipgvknadflryvnEG-FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489917580 479 DVETLRALEDA---LLEFPGSVMVISHDRWFLDRIAT---HIL 515
Cdd:cd03217 136 DIDALRLVAEVinkLREEGKSVLIITHYQRLLDYIKPdrvHVL 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
326-511 |
4.46e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 66.68 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYG---DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------KL 391
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLteenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSR-----AYLGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIAGG 466
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDFK----EREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 467 NVLLLDEPSNDLD----VETLRALEDALLEFPGSVMVISHDrwfLDRIA 511
Cdd:PRK13650 160 KIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-197 |
4.75e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKST----LLKIMAGvDKEIEGEAIPMPGLN----------IGYLPQEP--ELNPE 83
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-QGEIWFDGQPLHNLNrrqllpvrhrIQVVFQDPnsSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 HTVRQSVEEGLG---AVFNAKQRLDEVYAAYAEPDADfdalaaeqaeleaviaaaassgaddiehqmeiAADALRLPpwd 160
Cdd:PRK15134 379 LNVLQIIEEGLRvhqPTLSAAQREQQVIAVMEEVGLD--------------------------------PETRHRYP--- 423
|
170 180 190
....*....|....*....|....*....|....*..
gi 489917580 161 amvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:PRK15134 424 ---AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
338-521 |
5.00e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 338 DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQS--------RDSL---EGNKT 406
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylplgtlREALlypATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 407 VFDAVADGAdLLTVGkfeMPsrAYLGRFNfKGGDQNKIvgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL 486
Cdd:COG4178 455 FSDAELREA-LEAVG---LG--HLAERLD-EEADWDQV---LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
170 180 190
....*....|....*....|....*....|....*..
gi 489917580 487 EDALL-EFPGSVMV-ISHdRWFLDRIATHILAFEGDS 521
Cdd:COG4178 525 YQLLReELPGTTVIsVGH-RSTLAAFHDRVLELTGDG 560
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-479 |
5.45e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG-----DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV-KLAyvDQSRD 399
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdGKDVtKLP--EYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 SLEGnkTVF-DAVADGADLLTVgkFEMPSRAYL--GRFNFKGG-DQNKI---------------------VGQLSGGERG 454
Cdd:COG1101 80 KYIG--RVFqDPMMGTAPSMTI--EENLALAYRrgKRRGLRRGlTKKRRelfrellatlglglenrldtkVGLLSGGQRQ 155
|
170 180
....*....|....*....|....*
gi 489917580 455 RLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
326-503 |
6.27e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGD-RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK------------L 391
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksllevrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFKGGDqNKIVGQLSGGERGRLHLAKTLIAGGNVL 469
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKeaLKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 489917580 470 LLDEPSNDLD----VETLRALEDalLEFPGSVMVIS-HD 503
Cdd:PRK13639 160 VLDEPTSGLDpmgaSQIMKLLYD--LNKEGITIIIStHD 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
327-518 |
6.58e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.81 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-------LGQTVKLAYVDQSRD 399
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 S---------LEGNKTVFDAVADG-ADLLTVGKFEMPSRA-----------YLGRFNFkggdqnkivgQLSGGERGRLHL 458
Cdd:PRK11124 83 NvgmvfqqynLWPHLTVQQNLIEApCRVLGLSKDQALARAekllerlrlkpYADRFPL----------HLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 459 AKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPGS---VMVISHDRWFLDRIATHILAFE 518
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYME 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-541 |
6.88e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 323 GNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV------------ 389
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIpamsrsrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -KLAYVDQSrDSLEGNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKG--GDQNKIVGQLSGGERGRLHLAKTLIAGG 466
Cdd:PRK11831 84 kRMSMLFQS-GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGlrGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 467 NVLLLDEPSNDLDVETLRALEDALLEFPGSV----MVISHDRWFLDRIATH--ILAfegdSQVVFFDGNYQEYEADKKHR 540
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHayIVA----DKKIVAHGSAQALQANPDPR 238
|
.
gi 489917580 541 L 541
Cdd:PRK11831 239 V 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-238 |
7.45e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGLnigylpqepELNPEhTVRQsVEEGLGAV 97
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG-TITVGGM---------VLSEE-TVWD-VRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 FnakQRLDEVY-AAYAEPDADFdALAAEQAELEAVIAAAassgaDDIEHQMEIAADALRLPpwdamvGKLSGGEKRRVAL 176
Cdd:PRK13635 87 F---QNPDNQFvGATVQDDVAF-GLENIGVPREEMVERV-----DQALRQVGMEDFLNREP------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDryfLDNAAEW--ILELDRG 238
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD---LDEAAQAdrVIVMNKG 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
324-532 |
8.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.93 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAY-GDR-LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV-----------K 390
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklrkH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 LAYVDQSRDS-LEGNKTVFDaVADGADLLTVGKFEMPSR-----AYLGRFNFKGGDQNkivgQLSGGERGRLHLAKTLIA 464
Cdd:PRK13648 85 IGIVFQNPDNqFVGSIVKYD-VAFGLENHAVPYDEMHRRvsealKQVDMLERADYEPN----ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDAL--LEFPGSVMVIShdrwfldriATHIL--AFEGDSQVVFFDGN-YQE 532
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVrkVKSEHNITIIS---------ITHDLseAMEADHVIVMNKGTvYKE 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-238 |
9.49e-12 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 65.20 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGYLpqepelNPEHTVRQsveegLG 95
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-VDGHDLALA------DPAWLRRQ-----VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQRLDEVYAayaepdaDFDALAAEQAELEAVIAAAASSGADDIEHQMEIAadalrlppWDAMVGK----LSGGEK 171
Cdd:cd03252 80 VVLQENVLFNRSIR-------DNIALADPGMSMERVIEAAKLAGAHDFISELPEG--------YDTIVGEqgagLSGGQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 172 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHdRYFLDNAAEWILELDRG 238
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKG 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
346-542 |
1.24e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 346 SFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSL---EGN----KTVFDAVADGAD- 416
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSMlfqENNlfshLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 417 ---LLTVGKFEMPSRA-------YLGRFNfkggdqnkivGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD----VET 482
Cdd:PRK10771 99 glkLNAAQREKLHAIArqmgiedLLARLP----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 483 LRALEDALLEFPGSVMVISHDrwfLD---RIATH-ILAFEGDsqvVFFDGNYQEY---EADKKHRLG 542
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHS---LEdaaRIAPRsLVVADGR---IAWDGPTDELlsgKASASALLG 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-220 |
1.25e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 37 VLGLNGSGKSTLLKIMAG----------------VDKEiEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGAVFNA 100
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGltrpqkgrivlngrvlFDAE-KGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 101 KqrldevyaayaepdadFDALAAeqaeleaviaaaassgADDIEHQMEiaadalRLPpwdamvGKLSGGEKRRVALCRLL 180
Cdd:PRK11144 108 Q----------------FDKIVA----------------LLGIEPLLD------RYP------GSLSGGEKQRVAIGRAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 181 LSKPDMLLLDEPTNHLDA----ESVEWLEQFLHKFPGTVVAVTH 220
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-221 |
1.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYlpqepelnpeHTVRQsVEEGLG 95
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGE-IKIDGITISK----------ENLKE-IRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNakqrldevyaayaEPDADFDALAAEqaeleaviaaaassgaDDIEHQMEiaadALRLPPwDAM----------VG- 164
Cdd:PRK13632 87 IIFQ-------------NPDNQFIGATVE----------------DDIAFGLE----NKKVPP-KKMkdiiddlakkVGm 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 165 ---------KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF----PGTVVAVTHD 221
Cdd:PRK13632 133 edyldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
320-479 |
1.40e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 320 DRLGNEVIEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQ 396
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRDSL------EGNK----TVFDAVADGADLLTVGKFEMPSRAYlgrfnfkggDQNKIVG----------QLSGGERGRL 456
Cdd:PRK13632 81 IRKKIgiifqnPDNQfigaTVEDDIAFGLENKKVPPKKMKDIID---------DLAKKVGmedyldkepqNLSGGQKQRV 151
|
170 180
....*....|....*....|...
gi 489917580 457 HLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLD 174
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-528 |
1.44e-11 |
|
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: 63.22 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 323 GNEVIEFNHVSKAYGdrllIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------- 390
Cdd:cd03215 1 GEPVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTrrsprdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 LAYV--DQSRDSLEGNKTVFDAVAdgadlltvgkfempsrayLGRFnFKGGDQNKIVgqlsggergrlhLAKTLIAGGNV 468
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA------------------LSSL-LSGGNQQKVV------------LARWLARDPRV 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 469 LLLDEPSNDLDVETLRALEDALLEFP---GSVMVISHDRWFLDRIATHILafegdsqvVFFDG 528
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRIL--------VMYEG 180
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
326-538 |
1.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRL-LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV---------------KLGQTV 389
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 KLAYvdQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSR-----AYLGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PRK13636 85 GMVF--QDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRvdnalKRTGIEHLK----DKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 465 GGNVLLLDEPSNDLD----VETLRALEDALLEFPGSVMVISHDrwfLDRIATHILA-FEGDSQVVFFDGNYQEYEADKK 538
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVPLYCDNvFVMKEGRVILQGNPKEVFAEKE 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-501 |
1.63e-11 |
|
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: 63.82 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 339 RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD---SGEVKL-GQTVKLAYVDQSRDSLEGNKT-VFDAVad 413
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYnGIPYKEFAEKYPGEIIYVSEEdVHFPT-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 414 gadlLTVG---KFempsraylgRFNFKGgdqNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD-------VETL 483
Cdd:cd03233 98 ----LTVRetlDF---------ALRCKG---NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDsstaleiLKCI 161
|
170
....*....|....*...
gi 489917580 484 RALEDALlefpGSVMVIS 501
Cdd:cd03233 162 RTMADVL----KTTTFVS 175
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-221 |
1.99e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLN-----------IGYLPQEPELNPEHT 85
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqPMSKLSsaakaelrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGL--GAV--FNAKQRLDEVYAAYAepdadfdalaaeqaeleaviaaaassgaddIEHQmeiaadALRLPpwda 161
Cdd:PRK11629 104 ALENVAMPLliGKKkpAEINSRALEMLAAVG------------------------------LEHR------ANHRP---- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 162 mvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD---AESVEWLEQFLHKFPGTV-VAVTHD 221
Cdd:PRK11629 144 --SELSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-239 |
2.24e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------------AGVDKEIEGEAIPMPGL----NIGYLPQEPELNP 82
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDKAIRelrrNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVEEG----LGavfnakqrldevyaayaepdadfdaLAAEQAeleaviaaaassgaddIEHQMEIAAdALRLPP 158
Cdd:PRK11124 96 HLTVQQNLIEApcrvLG-------------------------LSKDQA----------------LARAEKLLE-RLRLKP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 159 W-DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGT---VVAVTHDRYFLDNAAEWILE 234
Cdd:PRK11124 134 YaDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVY 213
|
....*
gi 489917580 235 LDRGY 239
Cdd:PRK11124 214 MENGH 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
345-519 |
2.40e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 345 LSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAyvDQSR-----DSLEGNKTVFDAVADGADLL 418
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRG--DRSRfmaylGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 419 TVGKF---EMPSRAyLGRFNFKGGDQNkIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALE---DALLE 492
Cdd:PRK13543 108 GLHGRrakQMPGSA-LAIVGLAGYEDT-LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNrmiSAHLR 185
|
170 180
....*....|....*....|....*..
gi 489917580 493 FPGSVMVISHDRWFLDRIATHILAFEG 519
Cdd:PRK13543 186 GGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-238 |
2.62e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQE--PELNPEHtvrqsveegLGAV 97
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-YRVAGQDVATLDADalAQLRREH---------FGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 FNAKQRLDEVYAAY-AEPDADFDALAAEQAELEAVIAAAASSGADDIEHQmeiaadalrlpPwdamvGKLSGGEKRRVAL 176
Cdd:PRK10535 92 FQRYHLLSHLTAAQnVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-----------P-----SQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYfLDNAAEWILELDRG 238
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIEIRDG 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
327-530 |
2.80e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQ------TVKLAY-----VD 395
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAAqlgigII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 396 QSRDSLEGNKTVFDAVADGAdlLTVGKF---------EMPSRA--YLGRFNFKgGDQNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGR--HLTKKVcgvniidwrEMRVRAamMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 465 GGNVLLLDEPSNDL---DVETLRALEDALLEFPGSVMVISHDRWFLDRIathilafeGDSQVVFFDGNY 530
Cdd:PRK09700 163 DAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRI--------CDRYTVMKDGSS 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
324-503 |
3.14e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAY--GDRLL--IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQ-- 396
Cdd:PRK10535 2 TALLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVaGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 -----------SRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFkgGDQ-NKIVGQLSGGERGRLHLAKTL 462
Cdd:PRK10535 82 qlrrehfgfifQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAqeLLQRLGL--EDRvEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 463 IAGGNVLLLDEPSNDLDV---ETLRALEDALLEFPGSVMVISHD 503
Cdd:PRK10535 160 MNGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-221 |
3.59e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.36 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DK---EIEGEAIPMPGLN-IGYLPQEPELNPehtvRQSV 90
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIlapDSgevLWDGEPLDPEDRRrIGYLPEERGLYP----KMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEGLgaVFNAkqRLDEVYAAYAEPDAD--FDALaaeqaeleaviaaaassgadDIEHQmeiaadalrlppWDAMVGKLSG 168
Cdd:COG4152 89 GEQL--VYLA--RLKGLSKAEAKRRADewLERL--------------------GLGDR------------ANKKVEELSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL--HKFPG-TVVAVTHD 221
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIreLAAKGtTVIFSSHQ 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
326-383 |
3.69e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 3.69e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV 383
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-201 |
3.81e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGEAIPMPGLN------IGYLPQEPELnpehTV 86
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdagniiIDDEDISLLPLHararrgIGYLPQEASI----FR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGLGAVFNAKqrldevyaayaepdadfDALAAEQAEleaviaaaassgaDDIEHQM-EIAADALRlppwDAMVGK 165
Cdd:PRK10895 92 RLSVYDNLMAVLQIR-----------------DDLSAEQRE-------------DRANELMeEFHIEHLR----DSMGQS 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV 201
Cdd:PRK10895 138 LSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-514 |
3.87e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.71 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRML-----AGREQPDSGEVKL-GQTVKLAYVDQS 397
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLfGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RDSLE-----------GNKTVFDAVADGADL--LTVGKFEMPSRAYLGRFNFKGGDQ-----NKIVGQLSGGERGRLHLA 459
Cdd:PRK14267 82 EVRREvgmvfqypnpfPHLTIYDNVAIGVKLngLVKSKKELDERVEWALKKAALWDEvkdrlNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 460 KTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDRIATHI 514
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-503 |
4.16e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKS-TLLKIM----------AGVDKEIEGEAI---------PMPGLNIGYLPQEP 78
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvyPSGDIRFHGESLlhaseqtlrGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 79 --ELNPEHTVRQSVEEGLgavfnAKQRLDEVYAAYAEPDADFDALAAEQAeleaviaaaaSSGADDIEHQmeiaadalrl 156
Cdd:PRK15134 102 mvSLNPLHTLEKQLYEVL-----SLHRGMRREAARGEILNCLDRVGIRQA----------AKRLTDYPHQ---------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 157 ppwdamvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD----RYFLDNA 228
Cdd:PRK15134 157 ---------LSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNlsivRKLADRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 229 AewILELDRGygipwkgnysswLEQKEDRLKQEEATESARQKTIKKElewvrqnPKGRQ---AKAKARIARFEELSsyey 305
Cdd:PRK15134 228 A--VMQNGRC------------VEQNRAATLFSAPTHPYTQKLLNSE-------PSGDPvplPEPASPLLDVEQLQ---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 306 qkrnetqeIFIPVGDRLGNEVIEFNHVSKaygdrllidDLSFKVPAGAIVGIIGPNGAGKST----LFRMLAGReqpdsG 381
Cdd:PRK15134 283 --------VAFPIRKGILKRTVDHNVVVK---------NISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----G 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 382 EVKL-GQTV-------------KLAYVDQSRDS-LEGNKTVFDAVADGADL----LTVGKFEMPSRAYLGRFNFKGGDQN 442
Cdd:PRK15134 341 EIWFdGQPLhnlnrrqllpvrhRIQVVFQDPNSsLNPRLNVLQIIEEGLRVhqptLSAAQREQQVIAVMEEVGLDPETRH 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 443 KIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDvETLRALEDALL-----EFPGSVMVISHD 503
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALLkslqqKHQLAYLFISHD 485
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-545 |
4.52e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQP-----DSGEVKLGQTVKLAYvdqsRDSLEGNK 405
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNY----RDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 --------------TVFDAVADGA---DLLTVGKFEMPSRAYLGRFNFKGGDQNKIVG---QLSGGERGRLHLAKTLIAG 465
Cdd:PRK14271 102 rvgmlfqrpnpfpmSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVIshdrwfldrIATHILAFEG---DSQVVFFDGnyqeyeadkkhRLG 542
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVI---------IVTHNLAQAArisDRAALFFDG-----------RLV 241
|
...
gi 489917580 543 EEG 545
Cdd:PRK14271 242 EEG 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-238 |
5.11e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGLNIgylpqepelnpeHTVRQSveEGLGAV 97
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG-SIVVNGQTI------------NLVRDK--DGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 FNAKQ------RLDEVYAAYA----------EPDADFDALAAEQAELEAVIAAAASSGADDIEHQMEIAADalrlppwda 161
Cdd:PRK10619 82 ADKNQlrllrtRLTMVFQHFNlwshmtvlenVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVH--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 162 mvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK10619 153 ----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-503 |
5.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTV----------KLAYVDQSRDSLEGNKTVFDA 410
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVnaenekwvrsKVGLVFQDPDDQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 411 VADGADLLTVGKFEMPSRAylgrfnfkgGDQNKIVG----------QLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD- 479
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRV---------EEALKAVRmwdfrdkppyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDp 171
|
170 180
....*....|....*....|....*.
gi 489917580 480 --VETLRALEDALLEFPGSVMVISHD 503
Cdd:PRK13647 172 rgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-221 |
5.51e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 63.92 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG-------VDKEI--EGEAI-PMP--------GLNIGYLPQEPE-- 79
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpppgiTSGEIlfDGEDLlKLSekelrkirGREIQMIFQDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 LNPEHTVRQSVEEGLgavfNAKQRLDEvyaayaepdADFDALAAEqaeleaviaaaassgaddiehqmeiAADALRLPPW 159
Cdd:COG0444 99 LNPVMTVGDQIAEPL----RIHGGLSK---------AEARERAIE-------------------------LLERVGLPDP 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 160 DAMVGK----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:COG0444 141 ERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHD 210
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-201 |
5.70e-11 |
|
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: 62.66 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK-EIEGEAIPMPGLNIGylpqepELNPEHTVRqsveegLGa 96
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyEVTSGTILFKGQDLL------ELEPDERAR------AG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VFNAKQRLDEVYAAyaePDADF--DALAAEQAEleaviAAAASSGADDIEHQMEIAADALRLPPwdAM------VGkLSG 168
Cdd:TIGR01978 79 LFLAFQYPEEIPGV---SNLEFlrSALNARRSA-----RGEEPLDLLDFEKLLKEKLALLDMDE--EFlnrsvnEG-FSG 147
|
170 180 190
....*....|....*....|....*....|...
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV 201
Cdd:TIGR01978 148 GEKKRNEILQMALLEPKLAILDEIDSGLDIDAL 180
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
327-528 |
6.04e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.12 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVK----------LAYV 394
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdGRPLSslshsvlrqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQsrDSLEGNKTVFDAVADGAD---------LLTVGKFEMpSRAYLGRFNFKGGDQNKivgQLSGGERGRLHLAKTLIAG 465
Cdd:PRK10790 421 QQ--DPVVLADTFLANVTLGRDiseeqvwqaLETVQLAEL-ARSLPDGLYTPLGEQGN---NLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEF--PGSVMVISHdrwfldRIATHIlafEGDSQVVFFDG 528
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH------RLSTIV---EADTILVLHRG 550
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-222 |
6.64e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLP----------QEPELNPEHTVRQS 89
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR-IMLDGQDITHVPaenrhvntvfQSYALFPHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEEGLgavfnakqRLDEVYAAYAEPDAdFDALAAEQAEleaviaaaassgaddiehQMeiaadALRLPpwdamvGKLSGG 169
Cdd:PRK09452 107 VAFGL--------RMQKTPAAEITPRV-MEALRMVQLE------------------EF-----AQRKP------HQLSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAE-----SVEwLEQFLHKFPGTVVAVTHDR 222
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKlrkqmQNE-LKALQRKLGITFVFVTHDQ 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
293-479 |
7.78e-11 |
|
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: 65.35 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 293 RIARF---EELSSYEYQKRnetqeifiPVGDRLGNEVIEFNHV-SKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTL 368
Cdd:TIGR00957 609 RLRIFlshEELEPDSIERR--------TIKPGEGNSITVHNATfTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 369 FRMLAGREQPDSGEVKLGQTVklAYVDQ----SRDSLEGN------------KTVFDAVADGADLltvgkfEMpsraylg 432
Cdd:TIGR00957 681 LSALLAEMDKVEGHVHMKGSV--AYVPQqawiQNDSLRENilfgkalnekyyQQVLEACALLPDL------EI------- 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 433 rfnFKGGDQNKIvGQ----LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:TIGR00957 746 ---LPSGDRTEI-GEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-239 |
8.03e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaipmpgLNIGylpqEPELNpehTVRQSvEEGLGAVFNA 100
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIG----EKRMN---DVPPA-ERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 101 kqrldevYAAYAEPD-ADFDALAAEQAELEAViaaaassgadDIEHQMEIAADALRLppwDAMVGK----LSGGEKRRVA 175
Cdd:PRK11000 84 -------YALYPHLSvAENMSFGLKLAGAKKE----------EINQRVNQVAEVLQL---AHLLDRkpkaLSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 176 LCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEQF--LHKFPG-TVVAVTHDRYFLDNAAEWILELDRGY 239
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAAlRVQMRIEIsrLHKRLGrTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-221 |
8.55e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.41 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPGLNIGYLPQEPELNPEHTVRQSV 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 EEGLG-AVFNAKQRLDEVYAAYAEPDAdfdalaaeqaeleaviaaaassgaddiehqmeiaADALRLPPWdamvgKLSGG 169
Cdd:PRK11248 92 AFGLQlAGVEKMQRLEIAHQMLKKVGL----------------------------------EGAEKRYIW-----QLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTHD 221
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-238 |
8.74e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQE--PELNpehtvRQsveegLGA 96
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK-IWFSGHDITRLKNRevPFLR-----RQ-----IGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VFNAKQRLDE--VYAAYAEPdadfdaLAAEQAELEaviaaaassgadDIEHQMEIAADAL-RLPPWDAMVGKLSGGEKRR 173
Cdd:PRK10908 84 IFQDHHLLMDrtVYDNVAIP------LIIAGASGD------------DIRRRVSAALDKVgLLDKAKNFPIQLSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 174 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-221 |
8.74e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQI--LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMpglniGYLP--QEPELnpehtVRQsve 91
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVPfkRRKEF-----ARR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 92 egLGAVFNAKQRL--D-------EVYAA-YAEPDADFDALAAEQAELEaviaaaassgadDIEHQMEIAadalrlppwda 161
Cdd:COG4586 97 --IGVVFGQRSQLwwDlpaidsfRLLKAiYRIPDAEYKKRLDELVELL------------DLGELLDTP----------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 162 mVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTHD 221
Cdd:COG4586 152 -VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-221 |
8.87e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEaIPMPGLNIGYLPQePELnpehtvrqsveeglgavfnAKQRl 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGS-IQFAGQPLEAWSA-AEL-------------------ARHR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 105 devyaAY----AEPDAD---FDALAAEQAELeaviaaaasSGADDIEHQMEIAADALRL-PPWDAMVGKLSGGEKRRVAL 176
Cdd:PRK03695 72 -----AYlsqqQTPPFAmpvFQYLTLHQPDK---------TRTEAVASALNEVAEALGLdDKLGRSVNQLSGGEWQRVRL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 177 CRLLL-----SKPD--MLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTHD 221
Cdd:PRK03695 138 AAVVLqvwpdINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-243 |
9.69e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.24 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-----DKEIEGEAIpMPGLNIGYLP------------QEPELNP 82
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVY-LDGQDIFKMDvielrrrvqmvfQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVEEG--LGAVFNAKQRLDEVYAAyaepdadfdalAAEQAELeaviaaaassgADDIEHQMeiaadalrlppwD 160
Cdd:PRK14247 96 NLSIFENVALGlkLNRLVKSKKELQERVRW-----------ALEKAQL-----------WDEVKDRL------------D 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 161 AMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQ-FLH-KFPGTVVAVTHdryFLDNAA---EWILEL 235
Cdd:PRK14247 142 APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlFLElKKDMTIVLVTH---FPQQAArisDYVAFL 218
|
....*...
gi 489917580 236 DRGYGIPW 243
Cdd:PRK14247 219 YKGQIVEW 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-480 |
9.81e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMP--------GLNIGYlpQEPELNP 82
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQpdagsiLIDGQEMRFAsttaalaaGVAIIY--QELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVEegLGAVFNAKQRLDEvyaayaepdadfDALAAEQAEleaviaaaassgaddiehqmEIAADALRLPPwDAM 162
Cdd:PRK11288 93 EMTVAENLY--LGQLPHKGGIVNR------------RLLNYEARE--------------------QLEHLGVDIDP-DTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 163 VGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF--PGTVVA-VTHdryfldnAAEWILELDrgy 239
Cdd:PRK11288 138 LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSH-------RMEEIFALC--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 240 gipwkgnysswleqkeDRLkqeeatesarqkTIKKElewvrqnpkGRqakakaRIARFEELSSYeyqkrNETQEIFIPVG 319
Cdd:PRK11288 208 ----------------DAI------------TVFKD---------GR------YVATFDDMAQV-----DRDQLVQAMVG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 320 DRLGNevIeFNHVSKAYGD-RLLIDDL---------SFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQT 388
Cdd:PRK11288 240 REIGD--I-YGYRPRPLGEvRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 389 VKLAYV-------------DQSRDSLEGNKTVFDAVADGAD--------LLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQ 447
Cdd:PRK11288 317 IDIRSPrdairagimlcpeDRKAEGIIPVHSVADNINISARrhhlragcLINNRWEAENADRFIRSLNIKTPSREQLIMN 396
|
490 500 510
....*....|....*....|....*....|...
gi 489917580 448 LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-221 |
9.95e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkEIEGEAIPmpglNIGYLPQEPELNPEHTvrqsveeglgAVF 98
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAP----RGARVTGDVTLNGEPL----------AAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 99 NAKQ--RLDEVYAAYAEPDADFDAlaaeqAELEAVIAAAASSGADDIEHQ-MEIAADALRLPPWDAMVGK----LSGGEK 171
Cdd:PRK13547 77 DAPRlaRLRAVLPQAAQPAFAFSA-----REIVLLGRYPHARRAGALTHRdGEIAWQALALAGATALVGRdvttLSGGEL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 172 RRVALCRLL---------LSKPDMLLLDEPTNHLDAESvewleqfLHKFPGTVVAVTHD 221
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAH-------QHRLLDTVRRLARD 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
337-516 |
1.09e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.01 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE--QPDSGEV----------------KLG-----QT----- 388
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSIlldgedilelspderaRAGiflafQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 389 -VKLAY-----VDQSRDSLEGNKTVFDAVADGADLLtvgkfEMPsRAYLGRF-NfkggdqnkiVGqLSGGERGRLHLAKT 461
Cdd:COG0396 91 gVSVSNflrtaLNARRGEELSAREFLKLLKEKMKEL-----GLD-EDFLDRYvN---------EG-FSGGEKKRNEILQM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 462 LIAGGNVLLLDEPSNDLDVETLRALEDALLEF--PG-SVMVISHDRWFLDRIA---THILA 516
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDrGILIITHYQRILDYIKpdfVHVLV 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
330-510 |
1.12e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.76 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 330 NHVSKAYGD-RLLID---DLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV--------------K 390
Cdd:PRK11629 9 DNLCKRYQEgSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakaelrnqK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 391 LAYVDQSRDSLEGnktvFDAVADGADLLTVGKfEMPSRAylgrfNFKGGDQNKIVG----------QLSGGERGRLHLAK 460
Cdd:PRK11629 89 LGFIYQFHHLLPD----FTALENVAMPLLIGK-KKPAEI-----NSRALEMLAAVGlehranhrpsELSGGERQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 461 TLIAGGNVLLLDEPSNDLDVETlralEDALLEFPGSV--------MVISHDRWFLDRI 510
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELnrlqgtafLVVTHDLQLAKRM 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-480 |
1.14e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 1 MAQYVYTMNRVGKIVPPKRQiLRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEI--EGEAIPMPGLN-- 70
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKA-LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEIifEGEELQASNIRdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 71 ----IGYLPQEPELNPEHTVRQSVeeGLGAVFNAKQRLdevyaayaepdaDFDALAAEQAELEAviaaaassgaddiehQ 146
Cdd:PRK13549 80 eragIAIIHQELALVKELSVLENI--FLGNEITPGGIM------------DYDAMYLRAQKLLA---------------Q 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 147 MEIAADAlrlppwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLD 226
Cdd:PRK13549 131 LKLDINP------ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 227 NAAE---WILELDRGYGIpwkgnysswleqkedrlkqeeATESARQKTIKKELEWVrqnpKGRqakakariarfeELSS- 302
Cdd:PRK13549 205 EVKAisdTICVIRDGRHI---------------------GTRPAAGMTEDDIITMM----VGR------------ELTAl 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 303 YEYQKRNetqeifipvgdrLGNEVIEFNHVSkAYG----DRLLIDDLSFKVPAGAIVGIIGPNGAGK----STLFRMLAG 374
Cdd:PRK13549 248 YPREPHT------------IGEVILEVRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 375 REQpdsGEVKL-GQTVK-----------LAYV--DQSRDsleGNKTVFDaVADGADLLTVGKFEMPSR-----------A 429
Cdd:PRK13549 315 RWE---GEIFIdGKPVKirnpqqaiaqgIAMVpeDRKRD---GIVPVMG-VGKNITLAALDRFTGGSRiddaaelktilE 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 430 YLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:PRK13549 388 SIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-220 |
1.15e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDKEI--------EGEAIPMPGLN-------IGYLPQEPe 79
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVtitgsivyNGHNIYSPRTDtvdlrkeIGMVFQQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 lNP-EHTVRQSVEEGLG-AVFNAKQRLDEVyaayaepdadfdalaaeqaeleaviaaaassgaddIEHQMEIAA--DALR 155
Cdd:PRK14239 96 -NPfPMSIYENVVYGLRlKGIKDKQVLDEA-----------------------------------VEKSLKGASiwDEVK 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 156 LPPWDAMVGkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTH 220
Cdd:PRK14239 140 DRLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
326-494 |
1.22e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV-------------KLGQTVKL 391
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenirEVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYvdQSRDSLEGNKTV-----FDAVADGADLLTVGKFEMPSRAYLGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIAGG 466
Cdd:PRK13652 83 VF--QNPDDQIFSPTVeqdiaFGPINLGLDEETVAHRVSSALHMLGLEELR----DRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180
....*....|....*....|....*...
gi 489917580 467 NVLLLDEPSNDLDVETLRALEDALLEFP 494
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-544 |
1.26e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAY---GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSR-DSLEGNK- 405
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQiDAIKLRKe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 --------------TVFDAVA------DGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:PRK14246 92 vgmvfqqpnpfphlSIYDNIAyplkshGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 466 GNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDRIATHIlAFEGDSQVVFFdGNYQEYEADKKHRLGE 543
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV-AFLYNGELVEW-GSSNEIFTSPKNELTE 249
|
.
gi 489917580 544 E 544
Cdd:PRK14246 250 K 250
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-238 |
1.54e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.97 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLNIGYL-------PQEPELnpeht 85
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvPLVQYDHHYLhrqvalvGQEPVL----- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGavfnakqrldevYAAYAEPDADFDAlAAEQAeleaviaaaassGADDIEHQMEIAadalrlppWDAMVGK 165
Cdd:TIGR00958 567 FSGSVRENIA------------YGLTDTPDEEIMA-AAKAA------------NAHDFIMEFPNG--------YDTEVGE 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 166 ----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAEsVEWLEQFLHKFPG-TVVAVTHDRYFLDNAAEwILELDRG 238
Cdd:TIGR00958 614 kgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVERADQ-ILVLKKG 689
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-221 |
1.61e-10 |
|
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: 61.55 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 10 RVGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------AIPMPGL--NIGYLPQEP 78
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEifidgedirEQDPVELrrKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 79 ELNPEHTVRQSVeeGLgavfnakqrldeVYAAYAEPDADFDALAAEQAELEAviaaaassgaddiehqMEIAADALRLPp 158
Cdd:cd03295 85 GLFPHMTVEENI--AL------------VPKLLKWPKEKIRERADELLALVG----------------LDPAEFADRYP- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 159 wdamvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVEWLEQFLHKfpgTVVAVTHD 221
Cdd:cd03295 134 -----HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELGK---TIVFVTHD 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-238 |
2.09e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.91 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 9 NRVGKIVPPkrqiLRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaipmpglnIGYLPQEPELN----PEH 84
Cdd:COG4778 18 LQGGKRLPV----LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS--------ILVRHDGGWVDlaqaSPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEEGLGAV--F-NAKQR---LDEVyaayAEPDADfDALAAEQAEleaviaaaassgaddiehqmEIAADALR--- 155
Cdd:COG4778 86 EILALRRRTIGYVsqFlRVIPRvsaLDVV----AEPLLE-RGVDREEAR--------------------ARARELLArln 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 156 LPP--WDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKfpGT-VVAVTHDRYFLDNA 228
Cdd:COG4778 141 LPErlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTaIIGIFHDEEVREAV 218
|
250
....*....|
gi 489917580 229 AEWILELDRG 238
Cdd:COG4778 219 ADRVVDVTPF 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-228 |
2.12e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 61.51 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPmpGLN-----------IGYLPQEPELNPEH 84
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEptsgkvLIDGQDIA--AMSrkelrelrrkkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 85 TVRQSVEEGLgavfnakqrldEVYAayaEPDADFDALAAEQAELeaviaaaassgaddiehqMEIAADALRLPpwdamvG 164
Cdd:cd03294 118 TVLENVAFGL-----------EVQG---VPRAEREERAAEALEL------------------VGLEGWEHKYP------D 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDryfLDNA 228
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD---LDEA 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
339-533 |
2.18e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 339 RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVklAYVDQS----RDSLEGNKTVFDA--VA 412
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQawimNATVRGNILFFDEedAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 413 DGADLLTVGKFEmPSRAYLGrfnfkGGDQNKIvGQ----LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET-LRALE 487
Cdd:PTZ00243 751 RLADAVRVSQLE-ADLAQLG-----GGLETEI-GEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489917580 488 DALL-EFPGSVMVISHDRWFLDRIATHILAFEGDSqvVFFDGNYQEY 533
Cdd:PTZ00243 824 ECFLgALAGKTRVLATHQVHVVPRADYVVALGDGR--VEFSGSSADF 868
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
331-524 |
2.26e-10 |
|
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: 61.12 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSkaYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE--QPDSGEVKL-GQTV-KLAYVDQSRDSL----- 401
Cdd:TIGR01978 7 HVS--VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFkGQDLlELEPDERARAGLflafq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 -----------EGNKTVFDAV--ADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQ-LSGGERGRLHLAKTLIAGGN 467
Cdd:TIGR01978 85 ypeeipgvsnlEFLRSALNARrsARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 468 VLLLDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIA---THIL-----AFEGDSQVV 524
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIKpdyVHVLldgriVKSGDVELA 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
2.53e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.40 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYlPQEPELNpehtVRQSVeeglGAVFNAK 101
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR-ILFDGKPIDY-SRKGLMK----LRESV----GMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 102 QrlDEVYAAYAEPDADFDALAAEQAELEAVIAAAASSGADDIEHqmeiaadaLRLPPWDAmvgkLSGGEKRRVALCRLLL 181
Cdd:PRK13636 92 D--NQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--------LKDKPTHC----LSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 182 SKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-238 |
3.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.16 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGYLPQEPEL---------NPE-HTVRQSVE 91
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-VSGIDTGDFSKLQGIrklvgivfqNPEtQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 92 EGLgavfnakqrldevyaayaepdadfdALAAEQAELEAViaaaassgadDIEHQMEIAADALRLPPWDAMVGK-LSGGE 170
Cdd:PRK13644 97 EDL-------------------------AFGPENLCLPPI----------EIRKRVDRALAEIGLEKYRHRSPKtLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEW-LEQF--LHKFPGTVVAVTHDRYFLdNAAEWILELDRG 238
Cdd:PRK13644 142 GQCVALAGILTMEPECLIFDEVTSMLDPDSGIAvLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-238 |
3.90e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDkEIEGEAIPMPGLNIgylpqepeLNPEHTVRQSVEEGlGAVFn 99
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE-EITSGDLIVDGLKV--------NDPKVDERLIRQEA-GMVF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 100 akQRLDEVYAAYAEPDADFDAL---AAEQAELEAVIAaaassgadDIEHQMEIAADALRLPpwdamvGKLSGGEKRRVAL 176
Cdd:PRK09493 84 --QQFYLFPHLTALENVMFGPLrvrGASKEEAEKQAR--------ELLAKVGLAERAHHYP------SELSGGQQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 177 CRLLLSKPDMLLLDEPTNHLDAE---SVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-221 |
4.65e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGYlPQEPELNpehtVRQSVeeglG 95
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-IKGEPIKY-DKKSLLE----VRKTV----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQrlDEVYAAYAEPDADFDALAAEQAEleaviaaaassgaDDIEHQMEIAADALRL------PPwdamvGKLSGG 169
Cdd:PRK13639 82 IVFQNPD--DQLFAPTVEEDVAFGPLNLGLSK-------------EEVEKRVKEALKAVGMegfenkPP-----HHLSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHD 221
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-238 |
6.53e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGLN-------IGYLPQepelNPEH-----T 85
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqAITDDNfeklrkhIGIVFQ----NPDNqfvgsI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGavfNAKQRLDEVYAAYAEPDADFDALaaEQAeleaviaaaassgadDIEHQmeiaadalrlppwdamvgK 165
Cdd:PRK13648 101 VKYDVAFGLE---NHAVPYDEMHRRVSEALKQVDML--ERA---------------DYEPN------------------A 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTHDryfLDNAAE--WILELDRG 238
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD---LSEAMEadHVIVMNKG 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-222 |
7.04e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGylpqepELNPEhTVRQSVEEGLG--A 96
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL-FEGEDIS------TLKPE-IYRQQVSYCAQtpT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VFNakqrlDEVYAAYAEP------DADFDALAAEQAeleaviaaaassgaddiehQMEIAADALRLPpwdamVGKLSGGE 170
Cdd:PRK10247 92 LFG-----DTVYDNLIFPwqirnqQPDPAIFLDDLE-------------------RFALPDTILTKN-----IAELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTHDR 222
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
327-533 |
9.07e-10 |
|
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: 59.04 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGD--RLLIDDLSFKVPAGAIVGIIGPNGAGKST----LFRMLagreQPDSGEVKLG----QTVKLAYVDQ 396
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDgvdiSKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 S-----------RDSLEGNKTVFDAVADgADLLTVGKfempsRAYLGRF--NFKGGDQNKIV---GQLSGGERGRLHLAK 460
Cdd:cd03244 79 RisiipqdpvlfSGTIRSNLDPFGEYSD-EELWQALE-----RVGLKEFveSLPGGLDTVVEeggENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 461 TLIAGGNVLLLDEPSNDLDVETLRALEDAL-LEFPGS-VMVISHdrwfldRIAThILAFegDSQVVFFDGNYQEY 533
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCtVLTIAH------RLDT-IIDS--DRILVLDKGRVVEF 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-480 |
1.15e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEI--EGEAIPMPGLN------IGYLPQEPELNPEHTVR 87
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIywSGSPLKASNIRdteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVEEGLGAVFNAKQrldevyaayaepdADFDALAAEQAELEAviaaaassgaddiehQMEIAADALRLPpwdamVGKLS 167
Cdd:TIGR02633 97 ENIFLGNEITLPGGR-------------MAYNAMYLRAKNLLR---------------ELQLDADNVTRP-----VGDYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHDRYFLDNAA---EWILELDRGygipwk 244
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKavcDTICVIRDG------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 245 gnysswleqkedrlkQEEATESARQKTIKKELEWVrqnpKGRqakakariarfeELSSYeYQkrNETQEIfipvgdrlGN 324
Cdd:TIGR02633 218 ---------------QHVATKDMSTMSEDDIITMM----VGR------------EITSL-YP--HEPHEI--------GD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 325 EVIEFNHVSKAYGD---RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGR-EQPDSGEVKLGQ------------T 388
Cdd:TIGR02633 256 VILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGkpvdirnpaqaiR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 389 VKLAYVDQSRDSlEGNKTVFdAVADGADLLTVGKFEMPSR-----------AYLGRFNFKGGDQNKIVGQLSGGERGRLH 457
Cdd:TIGR02633 336 AGIAMVPEDRKR-HGIVPIL-GVGKNITLSVLKSFCFKMRidaaaelqiigSAIQRLKVKTASPFLPIGRLSGGNQQKAV 413
|
490 500
....*....|....*....|...
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDV 436
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-238 |
1.45e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV--DKEIEGEAIPMPGLNIGylpqepelnpEHTVrQSVEEGLG 95
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGITLT----------AKTV-WDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFnakQRLDEVY-AAYAEPDADFDalaaeqaeLEAVIAAAassgaddiEHQMEIAADALR----LPPWDAMVGKLSGGE 170
Cdd:PRK13640 88 IVF---QNPDNQFvGATVGDDVAFG--------LENRAVPR--------PEMIKIVRDVLAdvgmLDYIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG----TVVAVTHDryfLDNA--AEWILELDRG 238
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD---IDEAnmADQVLVLDDG 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-220 |
1.61e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 58.27 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLL------------KIMagvdkeIEGEAIPMPGLN-----IGYLPQEPELNpE 83
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfrlvelssgSIL------IDGVDISKIGLHdlrsrISIIPQDPVLF-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 HTVRqsveeglgavFNakqrLD--EVYaayaePDAD-FDALaaEQAELEAVIAAAASSGADDIEHqmeiaadalrlppwd 160
Cdd:cd03244 92 GTIR----------SN----LDpfGEY-----SDEElWQAL--ERVGLKEFVESLPGGLDTVVEE--------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 161 amVGK-LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL-HKFPG-TVVAVTH 220
Cdd:cd03244 136 --GGEnLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDcTVLTIAH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-526 |
1.76e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLaGREQPDSGEVKL-------GQTVKLAYVDQSR- 398
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVegrveffNQNIYERRVNLNRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 ---DSLEGNK------TVFDAVADGADLltVG---KFEMPSrayLGRFNFKGGD-----QNKI---VGQLSGGERGRLHL 458
Cdd:PRK14258 87 rrqVSMVHPKpnlfpmSVYDNVAYGVKI--VGwrpKLEIDD---IVESALKDADlwdeiKHKIhksALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 459 AKTLIAGGNVLLLDEPSNDLD------VETLraLEDALLEFPGSVMVISHDRWFLDRIATHILAFEGD----SQVVFF 526
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNenriGQLVEF 237
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-238 |
1.86e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---------VDKeIEGEAIPMPGL--NIGYLPQEPELnPEHTVRQSVeeg 93
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkING-IELRELDPESWrkHLSWVGQNPQL-PHGTLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 lgavfnakqrldevyaAYAEPDADFDAL--AAEQAELeaviaaaassgaDDIEHQMeiaADALRLPPWDAMVGkLSGGEK 171
Cdd:PRK11174 444 ----------------LLGNPDASDEQLqqALENAWV------------SEFLPLL---PQGLDTPIGDQAAG-LSVGQA 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 172 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHDryfLDNAAEW--ILELDRG 238
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRrqTTLMVTHQ---LEDLAQWdqIWVMQDG 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-199 |
1.93e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------AGVDKeIEGEAIPMPGL-----NIGYLPQEPELnpe 83
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRIL-IDGTDIRTVTRaslrrNIAVVFQDAGL--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 htVRQSVEEGLgavfnakqRLdevyaayAEPDADfDA---LAAEQAEleaviaaaassGADDIEHQmeiaADALrlppwD 160
Cdd:PRK13657 421 --FNRSIEDNI--------RV-------GRPDAT-DEemrAAAERAQ-----------AHDFIERK----PDGY-----D 462
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489917580 161 AMVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE 199
Cdd:PRK13657 463 TVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
337-489 |
2.12e-09 |
|
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: 57.25 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD--SGEVKL-GQTVK------LAYVDQSrDSLEGNKTV 407
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILInGRPLDknfqrsTGYVEQQ-DVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 408 FDAVADGADLltvgkfempsRAylgrfnfkggdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD-------V 480
Cdd:cd03232 97 REALRFSALL----------RG------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDsqaayniV 148
|
....*....
gi 489917580 481 ETLRALEDA 489
Cdd:cd03232 149 RFLKKLADS 157
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
326-531 |
2.24e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.15 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY--GDrLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG----------------------------- 374
Cdd:TIGR00954 451 GIKFENIPLVTpnGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGElwpvyggrltkpakgklfyvpqrpymtlg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 375 --REQ---PDSGE------------VKLGQTVKLAYVDQSrdslEGNktvFDAVADGADLltvgkfempsraylgrfnfk 437
Cdd:TIGR00954 530 tlRDQiiyPDSSEdmkrrglsdkdlEQILDNVQLTHILER----EGG---WSAVQDWMDV-------------------- 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 438 ggdqnkivgqLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPGSVMVISHdRWFLDRIATHILAF 517
Cdd:TIGR00954 583 ----------LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYM 651
|
250
....*....|....
gi 489917580 518 EGdsqvvffDGNYQ 531
Cdd:TIGR00954 652 DG-------RGGYQ 658
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-230 |
2.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMagvdkeiegEAIPMPGLNIGYLPQEPELNPEHT--VRQSVeeglGAVFn 99
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHM---------NALLIPSEGKVYVDGLDTSDEENLwdIRNKA----GMVF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 100 akQRLD-EVYAAYAEPDADF--DALAAEQAEleaviaaaassgaddIEHQMEIAADAL------RLPPwdamvGKLSGGE 170
Cdd:PRK13633 92 --QNPDnQIVATIVEEDVAFgpENLGIPPEE---------------IRERVDESLKKVgmyeyrRHAP-----HLLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489917580 171 KRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEQFLHKFPGTVVAVTHdryFLDNAAE 230
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAVE 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-238 |
2.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGYLPQEPELNPehtVRQSVeeGLG 95
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVR-VDDTLITSTSKNKDIKQ---IRKKV--GLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQRLDE-VYAAYAEPDADFdALAAEQAEleaviaaaassgaddiehqmEIAADALrlppwdAMVG---------- 164
Cdd:PRK13649 91 FQFPESQLFEEtVLKDVAFGPQNF-GVSQEEAE--------------------ALAREKL------ALVGiseslfeknp 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 -KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEQF--LHKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK13649 144 fELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGrKELMTLFkkLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
338-480 |
2.64e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 338 DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE--QPDSGEVKL-GQTV-----------KLAYVDQSR----- 398
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKdGKEVdvstvsdaidaGLAYVTEDRkgygl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 399 ---DSLEGNKTV--FDAVADGADLLTVGKFEMPSRaYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:NF040905 352 nliDDIKRNITLanLGKVSRRGVIDENEEIKVAEE-YRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
....*..
gi 489917580 474 PSNDLDV 480
Cdd:NF040905 431 PTRGIDV 437
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-254 |
2.73e-09 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 57.62 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---VDK------EIEGEAIPMPGL--NIGYLPQEPELNPEhT 85
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydPQKgqilidGIDIRDISRKSLrsMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVeeglgavfnakqrldevyaAYAEPDADFD--ALAAEQAELeaviaaaassgADDIEHqmeiaadalrLPP-WDAM 162
Cdd:cd03254 93 IMENI-------------------RLGRPNATDEevIEAAKEAGA-----------HDFIMK----------LPNgYDTV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 163 VGK----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHK-FPG-TVVAVTHDRYFLDNAAEwILELD 236
Cdd:cd03254 133 LGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAHRLSTIKNADK-ILVLD 211
|
250
....*....|....*...
gi 489917580 237 RGyGIPWKGNYSSWLEQK 254
Cdd:cd03254 212 DG-KIIEEGTHDELLAKK 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
326-542 |
2.81e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAY------GDRLLIDdLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------- 389
Cdd:PRK13643 1 MIKFEKVNYTYqpnspfASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 -----KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRAY--LGRFNFKGGDQNKIVGQLSGGERGRLHLAKTL 462
Cdd:PRK13643 80 kpvrkKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAekLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 463 IAGGNVLLLDEPSNDLD----VETLRALEdALLEFPGSVMVISHdrwFLDRIAT-----------HILAFEGDSQVvffd 527
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDpkarIEMMQLFE-SIHQSGQTVVLVTH---LMDDVADyadyvyllekgHIISCGTPSDV---- 231
|
250
....*....|....*
gi 489917580 528 gnYQEYEADKKHRLG 542
Cdd:PRK13643 232 --FQEVDFLKAHELG 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
324-475 |
3.26e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG-------QTVKL----- 391
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKImreav 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 392 AYVDQSRDSLeGNKTVFDAVADGADLLTVGKFEMPSRAYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLL 471
Cdd:PRK11614 83 AIVPEGRRVF-SRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
....
gi 489917580 472 DEPS 475
Cdd:PRK11614 162 DEPS 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-222 |
3.58e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.58 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGEAIPMPGL---NIGYLPQEPELNPEHTVRQ 88
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtegqifIDGEDVTHRSIqqrDICMVFQSYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEEGLG--AVFNA--KQRLDEvyaayaepdadfdalAAEQAELEAviaaaassgaddiehqMEiaadalrlppwDAMVG 164
Cdd:PRK11432 98 NVGYGLKmlGVPKEerKQRVKE---------------ALELVDLAG----------------FE-----------DRYVD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVEWLEQflhKFPGTVVAVTHDR 222
Cdd:PRK11432 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQ---QFNITSLYVTHDQ 197
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
145-232 |
3.86e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.85 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 145 HQMEIAADALRlppwdaMVGKLSGGEKR------RVALCRLLLSKPDMLLLDEPTNHLDAESVEW-----LEQFLHKFPG 213
Cdd:cd03240 101 HQGESNWPLLD------MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNF 174
|
90
....*....|....*....
gi 489917580 214 TVVAVTHDRYFLDNAAEWI 232
Cdd:cd03240 175 QLIVITHDEELVDAADHIY 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-197 |
4.31e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.93 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTL-LKIMAGVDKEieGEaIPMPGLNIGYLP---------------QEP--ELNPE 83
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPSE--GE-IRFDGQDLDGLSrralrplrrrmqvvfQDPfgSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 HTVRQSVEEGLGAVF---NAKQRLDEVYAAYAEPDADfdalaaeqaeleaviaaaassgaddiehqmeiAADALRLPpwd 160
Cdd:COG4172 379 MTVGQIIAEGLRVHGpglSAAERRARVAEALEEVGLD--------------------------------PAARHRYP--- 423
|
170 180 190
....*....|....*....|....*....|....*..
gi 489917580 161 amvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:COG4172 424 ---HEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
288-489 |
4.50e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.09 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 288 AKAKArIARFEELSSY----EYQKRNETQEIFipvgDRLGNEVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGA 363
Cdd:PRK11174 313 AKAQA-VGAAESLVTFletpLAHPQQGEKELA----SNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 364 GKSTLFRMLAGReQPDSGEVKL-GQTVK----------LAYVDQS----RDSLEGNKTVFDAVADGADLLTVGKfempsR 428
Cdd:PRK11174 388 GKTSLLNALLGF-LPYQGSLKInGIELReldpeswrkhLSWVGQNpqlpHGTLRDNVLLGNPDASDEQLQQALE-----N 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 429 AYLGRF--------NFKGGDQNkivGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET----LRALEDA 489
Cdd:PRK11174 462 AWVSEFlpllpqglDTPIGDQA---AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAA 531
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-221 |
5.05e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLpqepelnPEH-------TVRQ--- 88
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS-ILIDGKDVTKL-------PEYkrakyigRVFQdpm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 -------SVEE------------GLGAVFNAKQRldevyaayaepdadfDALAAEQAELEAviaaaassgadDIEHQMei 149
Cdd:COG1101 91 mgtapsmTIEEnlalayrrgkrrGLRRGLTKKRR---------------ELFRELLATLGL-----------GLENRL-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 150 aadalrlppwDAMVGKLSGGEkrRVALCrLL---LSKPDMLLLDEPTNHLD---AESVEWL-EQFLHKFPGTVVAVTHD 221
Cdd:COG1101 143 ----------DTKVGLLSGGQ--RQALS-LLmatLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHN 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-220 |
5.54e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------AGVdkEIEGEaIPMPGLNIgYlpqEPELNPEHtVRQSV 90
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGE-ILLDGEDI-Y---DPDVDVVE-LRRRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 eeglGAVFnakQRL--------DEVyaAYAEPDADFdalaAEQAELEaviaaaassgaddiehqmEIAADALR---LppW 159
Cdd:COG1117 95 ----GMVF---QKPnpfpksiyDNV--AYGLRLHGI----KSKSELD------------------EIVEESLRkaaL--W 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 160 D---------AMvgKLSGGEKRRvaLC--RLLLSKPDMLLLDEPTNHLDAESVEWLEQFLH----KFpgTVVAVTH 220
Cdd:COG1117 142 DevkdrlkksAL--GLSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELILelkkDY--TIVIVTH 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-206 |
5.96e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIPMPGLN------------IGYLPQEPEL------- 80
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlkdinlkwwrskIGVVSQDPLLfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 81 ----------NPEHTVRQSVEEGlgavFNAKQRLDEVYAAYAEPDADFDALAAEQAELEAVIAAAASSGADDIEhQMEIA 150
Cdd:PTZ00265 479 nikyslyslkDLEALSNYYNEDG----NDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSE-VVDVS 553
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 151 ADAL------RLP-PWDAMVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESvEWLEQ 206
Cdd:PTZ00265 554 KKVLihdfvsALPdKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQ 619
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
357-515 |
6.12e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.08 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 357 IIGPNGAGKSTLFR----MLAGREQPDSGEVK-----LGQTVKLAYVdqsrdslegnKTVFDaVADGADLLTVGKFEMps 427
Cdd:cd03240 27 IVGQNGAGKTTIIEalkyALTGELPPNSKGGAhdpklIREGEVRAQV----------KLAFE-NANGKKYTITRSLAI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 428 raYLGRFNFKGGDQNKI----VGQLSGGERG------RLHLAKTLIAGGNVLLLDEPSNDLDVETLR-ALEDaLLEFPGS 496
Cdd:cd03240 94 --LENVIFCHQGESNWPlldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAE-IIEERKS 170
|
170 180
....*....|....*....|....
gi 489917580 497 -----VMVISHDRWFLDRiATHIL 515
Cdd:cd03240 171 qknfqLIVITHDEELVDA-ADHIY 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
332-509 |
8.02e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.41 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 332 VSKAYGDRLLIDDLSFkvPAGAIVGIIGPNGAGKSTLfrMLAGREQpdSGEVKLGQTVKLAYvdqsrdsleGNKTVFdaV 411
Cdd:cd03238 3 VSGANVHNLQNLDVSI--PLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLISFLPKFS---------RNKLIF--I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 412 ADGADLLTVGKFEMPsrayLGRfnfkggdqnkIVGQLSGGERGRLHLAKTLIAG--GNVLLLDEPSNDLDVETLRALEDA 489
Cdd:cd03238 66 DQLQFLIDVGLGYLT----LGQ----------KLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEV 131
|
170 180
....*....|....*....|...
gi 489917580 490 ---LLEFPGSVMVISHDRWFLDR 509
Cdd:cd03238 132 ikgLIDLGNTVILIEHNLDVLSS 154
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-221 |
9.08e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.71 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 4 YVYTmnrvgKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGLNIGYLPQEPELNPe 83
Cdd:PRK13646 10 YTYQ-----KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTG-TVTVDDITITHKTKDKYIRP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 htVRQSVeeglGAVF---------------------NAKQRLDEVyAAYAepdadFDALAaeqaeleaviaaaassgadd 142
Cdd:PRK13646 83 --VRKRI----GMVFqfpesqlfedtvereiifgpkNFKMNLDEV-KNYA-----HRLLM-------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 143 iehQMEIAADALRLPPWdamvgKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAV 218
Cdd:PRK13646 131 ---DLGFSRDVMSQSPF-----QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILV 202
|
...
gi 489917580 219 THD 221
Cdd:PRK13646 203 SHD 205
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-201 |
1.06e-08 |
|
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: 55.35 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE---IEGEaIPMPGLN-----------IGYLPQEPELNP 82
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGD-IHYNGIPykefaekypgeIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVEeglgavFNAKQRLDEvyaayaepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdaM 162
Cdd:cd03233 97 TLTVRETLD------FALRCKGNE-------------------------------------------------------F 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 489917580 163 VGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV 201
Cdd:cd03233 116 VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
326-478 |
1.32e-08 |
|
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: 57.53 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGReQPD---SGEVKL-GQTVKLAYVDQSRD-- 399
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWsGSPLKASNIRDTERag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 --------SLEGNKTVFDAVADGADLLTVGKF----EMPSRAY--LGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAG 465
Cdd:TIGR02633 80 iviihqelTLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170
....*....|...
gi 489917580 466 GNVLLLDEPSNDL 478
Cdd:TIGR02633 160 ARLLILDEPSSSL 172
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
331-503 |
1.33e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 331 HVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGrEQPDSGEVKlGQTVK---------LAYVDQSRdsL 401
Cdd:PRK13547 6 HLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPR-GARVTgdvtlngepLAAIDAPR--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGNKTVFDAVADGA------DLLTVGKFEMPSRAylGRFNFKGGD--------------QNKIVGQLSGGERGRLHLAKT 461
Cdd:PRK13547 82 ARLRAVLPQAAQPAfafsarEIVLLGRYPHARRA--GALTHRDGEiawqalalagatalVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 462 L---------IAGGNVLLLDEPSNDLD-------VETLRALEDallEFPGSVMVISHD 503
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-247 |
1.39e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 14 IVPPKRQILRDiSLSF-FP-GAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-AIPMPGlNIGYLPQEPELNpEHTVRQSV 90
Cdd:TIGR00954 459 LVTPNGDVLIE-SLSFeVPsGNNLLICGPNGCGKSSLFRILGELWPVYGGRlTKPAKG-KLFYVPQRPYMT-LGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 eeglgavfnakqrldeVYaayaePDA--DFDALAAEQAELEAVIAAAassgadDIEHQMEiaadalRLPPWDAM---VGK 165
Cdd:TIGR00954 536 ----------------IY-----PDSseDMKRRGLSDKDLEQILDNV------QLTHILE------REGGWSAVqdwMDV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGTVVAVTHdRYFLDNAAEWILELDRgygipwKG 245
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDG------RG 655
|
..
gi 489917580 246 NY 247
Cdd:TIGR00954 656 GY 657
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
326-386 |
1.42e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.42e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG 386
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-238 |
1.44e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKrQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAipMPGLNIGYLPQEPE-LNPehTVRQSV----E 91
Cdd:PTZ00243 672 PK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--WAERSIAYVPQQAWiMNA--TVRGNIlffdE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 92 EglgavfNAKQRLDEVYAAYAEPDadfdaLAAEQAELEAviaaaassgaddiehqmEIAADALrlppwdamvgKLSGGEK 171
Cdd:PTZ00243 747 E------DAARLADAVRVSQLEAD-----LAQLGGGLET-----------------EIGEKGV----------NLSGGQK 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 172 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL--EQFLHKFPG-TVVAVTHDRYFLDNaAEWILELDRG 238
Cdd:PTZ00243 789 ARVSLARAVYANRDVYLLDDPLSALDAHVGERVveECFLGALAGkTRVLATHQVHVVPR-ADYVVALGDG 857
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-238 |
1.50e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLK------------IMAGvDKEIEGeAIPMPGL---------NIGYLPQE 77
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtIRVG-DITIDT-ARSLSQQkglirqlrqHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 78 PELNPEHTVRQSVEEGLGAVfnakqrldevyaaYAEPDADFDALAAEqaeleaviaaaassgaddiehqmeIAADALRLP 157
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIV-------------KGEPKEEATARARE------------------------LLAKVGLAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 158 PWDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEQF--LHKFPGTVVAVTHDRYFLDNAAEWILE 234
Cdd:PRK11264 137 KETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIF 216
|
....
gi 489917580 235 LDRG 238
Cdd:PRK11264 217 MDQG 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
326-487 |
1.87e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.56 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAgreqpdsgevKLGQTVKLAYVDQSrdSLEGNK 405
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFN----------RLNDLIPGFRVEGK--VTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 TVFDAVADGADLLT-VGK-FEMPSR---------AYLGRFNFKGGDQNKIVGQ---------------------LSGGER 453
Cdd:PRK14243 78 NLYAPDVDPVEVRRrIGMvFQKPNPfpksiydniAYGARINGYKGDMDELVERslrqaalwdevkdklkqsglsLSGGQQ 157
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 454 GRLHLAKTLIAGGNVLLLDEPSNDLD-VETLRALE 487
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDpISTLRIEE 192
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-254 |
1.99e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKST---LLKIMAGVDkeiEGEaIPMPGLNIgylpQEPEL----NPEHTVRQSVEegl 94
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDID---EGE-ILLDGHDL----RDYTLaslrNQVALVSQNVH--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 gaVFNakqrlDEVY--AAYAEPD----ADFDAlAAEQAeleaviaaaasSGADDIEhQMEiaaDALrlppwDAMVGK--- 165
Cdd:PRK11176 428 --LFN-----DTIAnnIAYARTEqysrEQIEE-AARMA-----------YAMDFIN-KMD---NGL-----DTVIGEngv 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 -LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHDRYFLDNAAEwILELDRGYgIP 242
Cdd:PRK11176 480 lLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKADE-ILVVEDGE-IV 557
|
250
....*....|..
gi 489917580 243 WKGNYSSWLEQK 254
Cdd:PRK11176 558 ERGTHAELLAQN 569
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
327-479 |
2.26e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.01 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAY-GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVklayVDQ----SRD-- 399
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV----VNElepaDRDia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 ------------SLEGN-----------KTVFDA-VADGADLLTVGKF-EMPSRaylgrfnfkggdqnkivgQLSGGERG 454
Cdd:PRK11650 80 mvfqnyalyphmSVRENmayglkirgmpKAEIEErVAEAARILELEPLlDRKPR------------------ELSGGQRQ 141
|
170 180
....*....|....*....|....*
gi 489917580 455 RLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
325-491 |
3.10e-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: 56.95 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 325 EVIEFNHVSKAYG--DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSLe 402
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM- 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 403 GNKTVFDAVadgADLLTvGKFEMPSRAYLGRFNFKGGDQ---------------NKIVGQLSGGERGRLHLAKTLIAGGN 467
Cdd:TIGR01257 2015 GYCPQFDAI---DDLLT-GREHLYLYARLRGVPAEEIEKvanwsiqslglslyaDRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180
....*....|....*....|....
gi 489917580 468 VLLLDEPSNDLDVETLRALEDALL 491
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
337-503 |
3.43e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.81 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLG---------------QTVKLAYVDQSRdSL 401
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevRRKKIAMVFQSF-AL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 402 EGNKTVFDAVADGADLLTVGKFEMPSRAY-----LGRFNFKGGDQNkivgQLSGGERGRLHLAKTLIAGGNVLLLDEPSN 476
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERREKALdalrqVGLENYAHSYPD----ELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 477 DLDVETLRALEDALLEFPG----SVMVISHD 503
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-198 |
3.70e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMA-----GVDKE----IEGEAIPMPGLNI--GYLPQEPELNPEHT 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKGSgsvlLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRqsveEGLgaVFNAKQRLDEVYAAyaepdadfdalaaeqaeleaviaAAASSGADDIEHQMEI--AADALRLPPWDamV 163
Cdd:TIGR00955 116 VR----EHL--MFQAHLRMPRRVTK-----------------------KEKRERVDEVLQALGLrkCANTRIGVPGR--V 164
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 164 GKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 198
Cdd:TIGR00955 165 KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
327-543 |
3.72e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG-----DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV----------- 389
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 ---KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA--YLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PRK13641 83 lrkKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKAlkWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDALLEFPG---SVMVISHDRWFLDRIATHILAFE-------GDSQVVFFDGNYQeye 534
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEhgklikhASPKEIFSDKEWL--- 239
|
....*....
gi 489917580 535 adKKHRLGE 543
Cdd:PRK13641 240 --KKHYLDE 246
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-238 |
4.39e-08 |
|
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: 53.57 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTL-LKIMAGVDKE-----IEGEAIPMPGL-----NIGYLPQEPELNpEHTVRQ 88
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEAEegkieIDGIDISTIPLedlrsSLTIIPQDPTLF-SGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEeglgaVFNaKQRLDEVYAAyaepdadfdalaaeqaeleaviaaaassgaddiehqMEIAADALrlppwdamvgKLSG 168
Cdd:cd03369 101 NLD-----PFD-EYSDEEIYGA------------------------------------LRVSEGGL----------NLSQ 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHK-FPG-TVVAVTHD-RYFLDNAAewILELDRG 238
Cdd:cd03369 129 GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFTNsTILTIAHRlRTIIDYDK--ILVMDAG 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-482 |
5.07e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTVKLAYVDQSRDS----------LEGNKTVFDA 410
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAgigiihqelnLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 411 VADGADLltVGKF------EMPSRA--YLGRFNFKGGDQnKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL-DVE 481
Cdd:PRK10762 100 IFLGREF--VNRFgridwkKMYAEAdkLLARLNLRFSSD-KLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
.
gi 489917580 482 T 482
Cdd:PRK10762 177 T 177
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
341-486 |
5.32e-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: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 341 LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPD---SGEVKLG--------QTVKLAYVDQSrDSLEGNKTVFD 409
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNgmpidakeMRAISAYVQQD-DLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 410 avadgaDLLTVGKFEMPSRAY-----------LGRFNFKGGdQNKIVGQ------LSGGERGRLHLAKTLIAGGNVLLLD 472
Cdd:TIGR00955 119 ------HLMFQAHLRMPRRVTkkekrervdevLQALGLRKC-ANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180
....*....|....*....|.
gi 489917580 473 EPSNDLD-------VETLRAL 486
Cdd:TIGR00955 192 EPTSGLDsfmaysvVQVLKGL 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-198 |
5.53e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 15 VPPKR-QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGEaIPMPGLN---------IGYLPQEPELNP 82
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGD-IRISGFPkkqetfariSGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 83 EHTVRQSVeeglgavfnakqrldeVYAAyaepdadFDALAAEQAELEaviaaaASSGADDIEHQMEIaaDALRlppwDAM 162
Cdd:PLN03140 967 QVTVRESL----------------IYSA-------FLRLPKEVSKEE------KMMFVDEVMELVEL--DNLK----DAI 1011
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489917580 163 VG-----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 198
Cdd:PLN03140 1012 VGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-238 |
6.70e-08 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 55.11 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEAIPMPGLNIGYLPQEPELNPEHTVRQSVeeglgAVF 98
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF-YEPDSGQILLDGHDLADYTLASLRRQVALVSQDV-----VLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 99 NakqrlDEVYA--AYAEPDAdfdalaAEQAELEAVIAaaassgaddiehqmeiAADAL----RLPP-WDAMVG----KLS 167
Cdd:TIGR02203 419 N-----DTIANniAYGRTEQ------ADRAEIERALA----------------AAYAQdfvdKLPLgLDTPIGengvLLS 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL-HKFPG-TVVAVTHDRYFLDNAAEwILELDRG 238
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALeRLMQGrTTLVIAHRLSTIEKADR-IVVMDDG 543
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-226 |
7.01e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.53 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK-EI-EGEAIpMPGLNIGylpqepELNPEHTVR-------Q- 88
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyEVtSGSIL-LDGEDIL------ELSPDERARagiflafQy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 -------SVEEGLGAVFNAkQRLDEVYAayaepdADFDALAAEQAELeaviaaaassgaddiehqMEIAADAL-RlppwD 160
Cdd:COG0396 86 pveipgvSVSNFLRTALNA-RRGEELSA------REFLKLLKEKMKE------------------LGLDEDFLdR----Y 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 161 AMVGkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVEWleqfLHKFPGTVVAVTHDRYFLD 226
Cdd:COG0396 137 VNEG-FSGGEKKRNEILQMLLLEPKLAILDETDSGLDidalrivAEGVNK----LRSPDRGILIITHYQRILD 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-242 |
7.08e-08 |
|
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: 53.91 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 31 PGAKIGVLGLNGSGKSTLLKIMAGvdkeiegEAIPmpglNIGYLPQEPELnpehtvRQSVEEGLGA---VFNAKQRLDEV 107
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-------KLKP----NLGKFDDPPDW------DEILDEFRGSelqNYFTKLLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 108 YAAYAEPDADFDALAAEQAELEAVIAAAASSGADDIEHQMEIAadalrlPPWDAMVGKLSGGEKRRVALCRLLLSKPDML 187
Cdd:cd03236 88 KVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELR------HVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 188 LLDEPTNHLDAE---SVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWILELdrgYGIP 242
Cdd:cd03236 162 FFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL---YGEP 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-229 |
7.45e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGlnigylpqePELNPEHTvrQSVEEGLGAVFNAK 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDG---------ELLTAENV--WNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 102 QrlDEVYAAYAEPDADFDAlaaeqaELEAVIAAAASSGADDIEHQMEIAADALRLPpwdamvGKLSGGEKRRVALCRLLL 181
Cdd:PRK13642 91 D--NQFVGATVEDDVAFGM------ENQGIPREEMIKRVDEALLAVNMLDFKTREP------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489917580 182 SKPDMLLLDEPTNHLDAESVEWLEQFLH----KFPGTVVAVTHDryfLDNAA 229
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHeikeKYQLTVLSITHD---LDEAA 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
324-512 |
8.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 324 NEVIEFNHVSKAY---GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTV---------- 389
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA-----YLGRFNFKggdqNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVdeallAVNMLDFK----TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489917580 465 GGNVLLLDEPSNDLD----VETLRALEDALLEFPGSVMVISHDrwfLDRIAT 512
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-220 |
8.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.90 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIgylpQEPELNPEHtVRQSVeeglG 95
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGK-IIIDGVDI----TDKKVKLSD-IRKKV----G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQrldevYAAYAEPDADFDALAAEQAELEAviaaaassgaDDIEHQMEIAADALRLPpWDAMVGK----LSGGEK 171
Cdd:PRK13637 87 LVFQYPE-----YQLFEETIEKDIAFGPINLGLSE----------EEIENRVKRAMNIVGLD-YEDYKDKspfeLSGGQK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489917580 172 RRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEQF--LHK-FPGTVVAVTH 220
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRdEILNKIkeLHKeYNMTIILVSH 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-211 |
8.78e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkeiegeAIPMPGLNIgylpqepELNPEHTVRQSVEEGLGAVFnak 101
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG--------ALPRTSGYV-------TLDGHEVVTRSPQDGLANGI--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 102 qrldevyaAYAEPDADFDAL-----AAEQAELEAVIAAAASSGAddIEHQMEIAA--DALRL-----PPWDAMVGKLSGG 169
Cdd:PRK10762 330 --------VYISEDRKRDGLvlgmsVKENMSLTALRYFSRAGGS--LKHADEQQAvsDFIRLfniktPSMEQAIGLLSGG 399
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF 211
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF 441
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
327-510 |
9.43e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDR-LLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRDSLEgn 404
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYRKLFS-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 405 kTVFDAVADGADLLTVGKFEMPS---RAYLGRFNFKGG---DQNKIVG-QLSGGERGRLHLAKTLIAGGNVLLLDEPSND 477
Cdd:PRK10522 401 -AVFTDFHLFDQLLGPEGKPANPalvEKWLERLKMAHKlelEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489917580 478 LDVETLRALEDALL----EFPGSVMVISH-DRWFL--DRI 510
Cdd:PRK10522 480 QDPHFRREFYQVLLpllqEMGKTIFAISHdDHYFIhaDRL 519
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-208 |
9.87e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE--------IEGEAIPMPGLN-IGYLPQEPELNPEHTVRQ 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnftgtilANNRKPTKQILKrTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVeeglgaVFNAKQRLDEVYAAyaepdaDFDALAAEQ--AELEAVIAAAASSGaddiehqmeiaadalrlppwDAMVGKL 166
Cdd:PLN03211 160 TL------VFCSLLRLPKSLTK------QEKILVAESviSELGLTKCENTIIG--------------------NSFIRGI 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL 208
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-222 |
1.03e-07 |
|
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: 55.30 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDKEIEGEAIPMPGLNI-------GYLPQEPELnpehtvrq 88
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGEIQIDGVSWNSVTLqtwrkafGVIPQKVFI-------- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 sveegLGAVFnaKQRLDEvYAAYAepDADFDALAAEQAeleaviaaaassgaddIEHQMEIAADALRLPPWDAMVgKLSG 168
Cdd:TIGR01271 1304 -----FSGTF--RKNLDP-YEQWS--DEEIWKVAEEVG----------------LKSVIEQFPDKLDFVLVDGGY-VLSN 1356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 169 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL-HKFPGTVVAVTHDR 222
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-238 |
1.04e-07 |
|
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: 52.72 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA------IPMPGL---------NIGYLPQEPELnpehtV 86
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknESEPSFeatrsrnrySVAYAAQKPWL-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGL--GAVFNaKQRLDEVYAAYA-EPDADFDALAaeqaeleaviaaaassgaddieHQMEIAADALrlppwdamv 163
Cdd:cd03290 92 NATVEENItfGSPFN-KQRYKAVTDACSlQPDIDLLPFG----------------------DQTEIGERGI--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 164 gKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQ-----FLHKFPGTVVAVTHDRYFLDNaAEWILELDRG 238
Cdd:cd03290 140 -NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-221 |
1.06e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDKEIE--------GEAIPMPGLNIGYLPQE-------PEL 80
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKClnrMNELESEVRvegrveffNQNIYERRVNLNRLRRQvsmvhpkPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 81 NPeHTVRQSVEEGLGAV-FNAKQRLDEVYAAyaepdadfdalAAEQAELeaviaaaassgADDIEHQMEIAADalrlppw 159
Cdd:PRK14258 100 FP-MSVYDNVAYGVKIVgWRPKLEIDDIVES-----------ALKDADL-----------WDEIKHKIHKSAL------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 160 damvgKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFP----GTVVAVTHD 221
Cdd:PRK14258 150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-492 |
1.16e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLF----RMLAgrEQPD---SGEVKL-GQTVklaYvDQS 397
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMND--LIPGarvEGEILLdGEDI---Y-DPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RDSLE-----G------N---KTVFDAVADGADLltvgkFEMPSRAYLgrfnfkggdqNKIV------------------ 445
Cdd:COG1117 85 VDVVElrrrvGmvfqkpNpfpKSIYDNVAYGLRL-----HGIKSKSEL----------DEIVeeslrkaalwdevkdrlk 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 446 ---GQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD-VETLRaLEDALLE 492
Cdd:COG1117 150 ksaLGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILE 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-221 |
1.44e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.78 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIG------------YLPQEPELNPEHTVR 87
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGE-VLVDGLDVAttpsrelakrlaILRQENHINSRLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVeeGLGAVFNAKQRLDevyaayAEpdadfDALAAEQA----ELEaviaaaassgadDIEHQmeiaadalrlppwdaMV 163
Cdd:COG4604 94 ELV--AFGRFPYSKGRLT------AE-----DREIIDEAiaylDLE------------DLADR---------------YL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 164 GKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEQF------LHKfpgTVVAVTHD 221
Cdd:COG4604 134 DELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMKLLrrladeLGK---TVVIVLHD 195
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-237 |
1.46e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.08 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVL-GLNGSGKSTLLKIMA----GVDKEIEGeaIPMPGLNIgylpQEPELNPEHTV-------RQS 89
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIAlalsGLLSRLDD--VKFRKLLI----RNGEFGDSAKLilyygtsRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VEEGLGAVFNAKQRLDEVYAAYAE---PDADFDALAaeqAELEAVIAAAASSGADDIEHQMEIAADALR--LPPWDAM-- 162
Cdd:COG3950 88 LDGPLKKLERLKEEYFSRLDGYDSlldEDSNLREFL---EWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDIri 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 163 ------------------VGKLSGGEKRRVALC-----RLLLSKPDM---------LLLDEPTNHLdaeSVEWLEQFLHK 210
Cdd:COG3950 165 drdpgrlvildkngeelpLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPD 241
|
250 260 270
....*....|....*....|....*....|...
gi 489917580 211 ----FPGT-VVAVTHDRYFLDNA-AEWILELDR 237
Cdd:COG3950 242 lrkiFPNIqFIVTTHSPLILSSLeDEEVIVLER 274
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-228 |
1.47e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIG-----------YLPQEPELNPEHTVRQS 89
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-ILFERQSIKkdlctyqkqlcFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 90 VeeglgavfnakqrldeVYaayaepDADFDALAAEQAELEAVIAaaassgaddIEHQMeiaadalrlppwDAMVGKLSGG 169
Cdd:PRK13540 95 C----------------LY------DIHFSPGAVGITELCRLFS---------LEHLI------------DYPCGLLSSG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 170 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLE---QFLHKFPGTVVAVTHDRYFLDNA 228
Cdd:PRK13540 132 QKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIItkiQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
327-479 |
1.47e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYG-----DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV------------ 389
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 390 ---KLAYVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA------------YLGRFNFkggdqnkivgQLSGGERG 454
Cdd:PRK13634 83 lrkKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAremielvglpeeLLARSPF----------ELSGGQMR 152
|
170 180
....*....|....*....|....*
gi 489917580 455 RLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-220 |
1.70e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.54 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 20 QILRDISLSFFPGAKIGVLGLNGSGKSTLLK-----IMAGVDKEIEGEaIPMPGLNIgylpQEPELNPEHtVRQSVeegl 94
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGE-VRLFGRNI----YSPDVDPIE-VRREV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 GAVFNakqrldevyaaYAEPdadFDALAAEQAELEAVIAAAASSGADDIEHQMEIAADALRLppWDAM-------VGKLS 167
Cdd:PRK14267 88 GMVFQ-----------YPNP---FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAL--WDEVkdrlndyPSNLS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTH 220
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
341-482 |
1.73e-07 |
|
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: 54.53 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 341 LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKlgQTVKLAYVDQSRDSLEGnkTVFDAVADGadlLTV 420
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQTSWIMPG--TIKDNIIFG---LSY 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 421 GKFEMPS-------RAYLGRFNFKggdQNKIVGQ----LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 482
Cdd:TIGR01271 514 DEYRYTSvikacqlEEDIALFPEK---DKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-479 |
1.86e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 336 YGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVkLGQTVKLAYVDQSRDSLEGN-KTVF------ 408
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLLALRQQvATVFqdpeqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 409 ----DAVADGA---DLLTVGKFEMPSRA--YLGRFNFKGGDQNKIvGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:PRK13638 90 ifytDIDSDIAfslRNLGVPEAEITRRVdeALTLVDAQHFRHQPI-QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-193 |
1.99e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPG------LNIGYLPqepE------LNPE 83
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPadsgeiRLDGKPVRIRSprdairAGIAYVP---EdrkgegLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 HTVRQ-----SVEEGLGAVFNAKQRLDEVYAAYAEpdadfdalaaeqaeleaviaaaassgaddiehQMEIaadalRLPP 158
Cdd:COG1129 345 LSIREnitlaSLDRLSRGGLLDRRRERALAEEYIK--------------------------------RLRI-----KTPS 387
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 159 WDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPT 193
Cdd:COG1129 388 PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
342-503 |
2.16e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.04 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKLAYVDQSRD--------------SLEGNKT 406
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEAQKLlrqkiqivfqnpygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 407 VFDAVADGADLLT-VGKFEMPSR--AYLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV--- 480
Cdd:PRK11308 111 VGQILEEPLLINTsLSAAERREKalAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVsvq 190
|
170 180
....*....|....*....|....
gi 489917580 481 -ETLRALEDALLEFPGSVMVISHD 503
Cdd:PRK11308 191 aQVLNLMMDLQQELGLSYVFISHD 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-247 |
2.17e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKimagvdkEIEGEAIPMPGLNIGYLPQEPeLNPEHTVrqsveeglgav 97
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR-------LLAGALKGTPVAGCVDVPDNQ-FGREASL----------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 fnakqrLDEVYaayaePDADFDAlAAEqaeleaviaaaassgaddIEHQMEIAADALRLPPWDAmvgkLSGGEKRRVALC 177
Cdd:COG2401 103 ------IDAIG-----RKGDFKD-AVE------------------LLNAVGLSDAVLWLRRFKE----LSTGQKFRFRLA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 178 RLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF----PGTVVAVTHdRYFLDNAaewiLELDR----GYGIPWKGNY 247
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLVVATH-HYDVIDD----LQPDLlifvGYGGVPEEKR 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
326-503 |
2.25e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGD---RLLI-DDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKlAYVDQSRDS 400
Cdd:PRK10584 6 IVEVHHLKKSVGQgehELSIlTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLH-QMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNKT--VFDAVADGADLLTVGKFEMP--------------SRAYLGRFNFkGGDQNKIVGQLSGGERGRLHLAKTLIA 464
Cdd:PRK10584 85 LRAKHVgfVFQSFMLIPTLNALENVELPallrgessrqsrngAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489917580 465 GGNVLLLDEPSNDLDVETLRALEDALL----EFPGSVMVISHD 503
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFslnrEHGTTLILVTHD 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-243 |
2.37e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 2 AQYVYTMNRVGKIVPPKrQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEAIPMPGlNIGYLPQEPELN 81
Cdd:PRK14246 7 AEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL-IEIYDSKIKVDG-KVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 82 PEHTVRQSVeeglGAVFNAKQRLDE--VYAAYAEPdadfdaLAAEQAELEAVIAAAASSGADDIEHQMEIAaDALRLPpw 159
Cdd:PRK14246 84 DAIKLRKEV----GMVFQQPNPFPHlsIYDNIAYP------LKSHGIKEKREIKKIVEECLRKVGLWKEVY-DRLNSP-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 160 damVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHDRYFLDNAAEWILELDR 237
Cdd:PRK14246 151 ---ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYN 227
|
....*.
gi 489917580 238 GYGIPW 243
Cdd:PRK14246 228 GELVEW 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-221 |
2.63e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA----IPMPGLNI-------------GYLPQEPELN 81
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdVLLGGRSIfnyrdvlefrrrvGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 82 PeHTVRQSVEEGlgavfnakqrldeVYAAYAEPDADFDALAaeQAELEAVIAaaassgaddiehqMEIAADALRLPPWda 161
Cdd:PRK14271 114 P-MSIMDNVLAG-------------VRAHKLVPRKEFRGVA--QARLTEVGL-------------WDAVKDRLSDSPF-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 162 mvgKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHD 221
Cdd:PRK14271 163 ---RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-480 |
2.66e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaipmpglnIGYLPQEPELnpeHTVRQSVEEGLGA 96
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS--------ILFQGKEIDF---KSSKEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 97 VFN----AKQR--LDEVYAA--------------YAEPDADFDALaaeqaeleaviaaaassgadDIEhqmeiaadalrL 156
Cdd:PRK10982 78 VHQelnlVLQRsvMDNMWLGryptkgmfvdqdkmYRDTKAIFDEL--------------------DID-----------I 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 157 PPWDAmVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPgtvvavthdryfldnaaewilelD 236
Cdd:PRK10982 127 DPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-----------------------E 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 237 RGYGIPWKGNysswleqkedrlKQEEATESARQKTIKKELEWVRQNP-KGRQAKAKARIARFEELSSYEYQKRNETQEIF 315
Cdd:PRK10982 183 RGCGIVYISH------------KMEEIFQLCDEITILRDGQWIATQPlAGLTMDKIIAMMVGRSLTQRFPDKENKPGEVI 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 316 IPVgdrlgNEVIEFNHVSkaygdrllIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVKlayv 394
Cdd:PRK10982 251 LEV-----RNLTSLRQPS--------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKIN---- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 dqsrdslegNKTVFDAVADGADLLT-----VGKFEMPS----------RAYLGRF-------------------NFKGGD 440
Cdd:PRK10982 314 ---------NHNANEAINHGFALVTeerrsTGIYAYLDigfnslisniRNYKNKVglldnsrmksdtqwvidsmRVKTPG 384
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 489917580 441 QNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 480
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
342-479 |
2.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 52.36 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL------GQTVKLAY-------VDQSRDSLEGNKTVF 408
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDirkkvglVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 409 DAVADGADLLTVGKFEMPSRAYLGrFNFKGGDQNKIVGQ----LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 479
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-MNIVGLDYEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-221 |
2.98e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAgvdkeieGEAIPMPGlNIGYLPQEPELNPEHT------------- 85
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALS-------ARLAPDAG-EVHYRMRDGQLRDLYAlseaerrrllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 ---VRQSVEEGL------GAvfNAKQRLdevYAAYAEPDADFDALAAEQAEleaviaaaassgaddiehQMEIAADALrl 156
Cdd:PRK11701 91 wgfVHQHPRDGLrmqvsaGG--NIGERL---MAVGARHYGDIRATAGDWLE------------------RVEIDAARI-- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 157 ppwDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK11701 146 ---DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
344-510 |
3.15e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKvpAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKL-GQTVklayvdqSRDSLEGNKTVFDAV-ADG---ADLL 418
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdGQPV-------TADNREAYRQLFSAVfSDFhlfDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 419 TVGKFEMPSRA--YLGRFNFKggDQNKIVG------QLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE--------- 481
Cdd:COG4615 423 GLDGEADPARAreLLERLELD--HKVSVEDgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfytel 500
|
170 180 190
....*....|....*....|....*....|....*
gi 489917580 482 --TLRALedallefpG-SVMVISHD-RWF--LDRI 510
Cdd:COG4615 501 lpELKAR--------GkTVIAISHDdRYFdlADRV 527
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
337-547 |
4.93e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDS-GEVKLGQTVklAYVDQSrdSLEGNKTVFDAVADGA 415
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTV--AYVPQV--SWIFNATVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 416 DlltvgkFEMPsraylgRFN--------------FKGGDQNKIvGQ----LSGGERGRLHLAKTLIAGGNVLLLDEPSND 477
Cdd:PLN03130 704 P------FDPE------RYEraidvtalqhdldlLPGGDLTEI-GErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 478 LDVETLRALEDALL--EFPGSVMV-ISHDRWFLDRIATHILAFEGdsqVVFFDGNYQEYEADKK--HRLGEEGAK 547
Cdd:PLN03130 771 LDAHVGRQVFDKCIkdELRGKTRVlVTNQLHFLSQVDRIILVHEG---MIKEEGTYEELSNNGPlfQKLMENAGK 842
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-199 |
5.18e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.73 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 9 NRVGKIVP-PKRQI--LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGYLPqEPELNpehT 85
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-VDGQDLTALS-EKELR---K 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVeeglGAVF------NAKQRLDEVyaAYA-----EPDADFDALAAEQAELeaviaaaassgaddiehqMEIAADAL 154
Cdd:PRK11153 80 ARRQI----GMIFqhfnllSSRTVFDNV--ALPlelagTPKAEIKARVTELLEL------------------VGLSDKAD 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 155 RLPpwdamvGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE 199
Cdd:PRK11153 136 RYP------AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
5.28e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.77 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLPQEPELNPEHTVRQ-----SVEEGLG 95
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGT-IQVGDIYIGDKKNNHELITNPYSKKiknfkELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQRldEVYAAYAEPDADFDALAAEQAELEAVIAAAASSGaddiehQMEIAADALRLPPWDamvgkLSGGEKRRVA 175
Cdd:PRK13631 120 MVFQFPEY--QLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLN------KMGLDDSYLERSPFG-----LSGGQKRRVA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 176 LCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL---HKFPGTVVAVTHDRYFLDNAAEWILELDRG 238
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-253 |
6.06e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG----VDKEIEGEAIPMPGLNI-------GYLPQEPELNPEhTVR 87
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhfdvSEGDIRFHDIPLTKLQLdswrsrlAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 88 QSVeeglgavfnakqrldevyaAYAEPDAdfdalaaeqaeleaviaaaassGADDIEHQMEIAA---DALRLPP-WDAMV 163
Cdd:PRK10789 407 NNI-------------------ALGRPDA----------------------TQQEIEHVARLASvhdDILRLPQgYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 164 GK----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVewlEQFLHKFPG-----TVVAVTHDRYFLDNAAEwILE 234
Cdd:PRK10789 446 GErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE---HQILHNLRQwgegrTVIISAHRLSALTEASE-ILV 521
|
250
....*....|....*....
gi 489917580 235 LDRGyGIPWKGNYSSWLEQ 253
Cdd:PRK10789 522 MQHG-HIAQRGNHDQLAQQ 539
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-241 |
6.30e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.37 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIgylpqEPELNPEHTVRQSVEEGLG 95
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT-ITIAGYHI-----TPETGNKNLKKLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVFNAKQRLDEVY---AAYAEPDADFDALAAEQAELEAVIaaaassgaddiehQMEIAADALRLPPWDamvgkLSGGEKR 172
Cdd:PRK13641 91 FQFPEAQLFENTVlkdVEFGPKNFGFSEDEAKEKALKWLK-------------KVGLSEDLISKSPFE-----LSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 173 RVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEQFL--HKFPGTVVAVTHDryfLDNAAEW---ILELDRGYGI 241
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKdyQKAGHTVILVTHN---MDDVAEYaddVLVLEHGKLI 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
344-480 |
6.58e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKV----PAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------------KLAYVDQ-SR----D 399
Cdd:PRK11144 12 DLCLTVnltlPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQdARlfphY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 400 SLEGN---------KTVFDAVadgADLLTVGKFempsrayLGRFNfkggdqnkivGQLSGGERGRLHLAKTLIAGGNVLL 470
Cdd:PRK11144 92 KVRGNlrygmaksmVAQFDKI---VALLGIEPL-------LDRYP----------GSLSGGEKQRVAIGRALLTAPELLL 151
|
170
....*....|
gi 489917580 471 LDEPSNDLDV 480
Cdd:PRK11144 152 MDEPLASLDL 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-200 |
7.07e-07 |
|
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: 52.26 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIG------------YLPQEPELnpehtvrq 88
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGE-IIIDGLNIAkiglhdlrfkitIIPQDPVL-------- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 sveeglgavFNAKQRLD-EVYAAYAEPDAdfdALAAEQAELEaviaAAASSGADDIEHQMEIAADalrlppwdamvgKLS 167
Cdd:TIGR00957 1372 ---------FSGSLRMNlDPFSQYSDEEV---WWALELAHLK----TFVSALPDKLDHECAEGGE------------NLS 1423
|
170 180 190
....*....|....*....|....*....|...
gi 489917580 168 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 200
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
352-525 |
7.71e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 352 GAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKlgqtvklayvdqsrdslegnktvfdaVADGADLLTVGKFEMpsrayl 431
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI--------------------------YIDGEDILEEVLDQL------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 432 grfnfKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET---------LRALEDALLEFPGSVMVISH 502
Cdd:smart00382 50 -----LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|...
gi 489917580 503 DRWFLDRiatHILAFEGDSQVVF 525
Cdd:smart00382 125 DEKDLGP---ALLRRRFDRRIVL 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
159-220 |
7.87e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 7.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 159 WDAMVG----KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTH 220
Cdd:PTZ00265 1348 YDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-226 |
7.92e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGEaIPMPGLNIGYLpqEPEL-----------NPEHT 85
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGD-ILFKGESILDL--EPEErahlgiflafqYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 86 VRQSVEEGLGAVFNAKQRldevyaAYAEPDADfdalaaeqaELEAviaaaassgaddiehqMEIAADALRLPPWDAM--- 162
Cdd:CHL00131 97 PGVSNADFLRLAYNSKRK------FQGLPELD---------PLEF----------------LEIINEKLKLVGMDPSfls 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 163 --VGK-LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPGT---VVAVTHDRYFLD 226
Cdd:CHL00131 146 rnVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSensIILITHYQRLLD 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-503 |
8.19e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.61 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKS-TLLKIM-------AGVDKEI--EGE---AIPMPGLN------IGYLPQEP- 78
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpdpaAHPSGSIlfDGQdllGLSERELRrirgnrIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 79 -ELNPEHTV-RQSVE-----EGLGAVfNAKQR----LDEV--------YAAYaePdadfdalaaeqaeleaviaaaassg 139
Cdd:COG4172 103 tSLNPLHTIgKQIAEvlrlhRGLSGA-AARARalelLERVgipdperrLDAY--P------------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 140 addieHQmeiaadalrlppwdamvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTV 215
Cdd:COG4172 155 -----HQ-------------------LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMAL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 216 VAVTHDryfldnaaewiLELDRGYGipwkgnysswleqkeDR---LKQEEATESArqktikkELEWVRQNPKgrqakaka 292
Cdd:COG4172 211 LLITHD-----------LGVVRRFA---------------DRvavMRQGEIVEQG-------PTAELFAAPQ-------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 293 riarfeelssYEYqkrneTQEIF--IPVGDRL-----GNEVIEFNHVSKAYGDR--LL---------IDDLSFKVPAGAI 354
Cdd:COG4172 250 ----------HPY-----TRKLLaaEPRGDPRpvppdAPPLLEARDLKVWFPIKrgLFrrtvghvkaVDGVSLTLRRGET 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 355 VGIIGPNGAGKSTLFRMLAgREQPDSGEVKL-GQTvkLAYVDQS------RD----------SLEGNKTVFDAVADGADL 417
Cdd:COG4172 315 LGLVGESGSGKSTLGLALL-RLIPSEGEIRFdGQD--LDGLSRRalrplrRRmqvvfqdpfgSLSPRMTVGQIIAEGLRV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 418 LTVGkfemPSRA--------YLGRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV-------ET 482
Cdd:COG4172 392 HGPG----LSAAerrarvaeALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaqilDL 467
|
570 580
....*....|....*....|.
gi 489917580 483 LRALEDallEFPGSVMVISHD 503
Cdd:COG4172 468 LRDLQR---EHGLAYLFISHD 485
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
342-383 |
8.61e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 8.61e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV 383
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-507 |
1.21e-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: 49.64 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTVK---------------LAYVDQSRDSLEG--- 403
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLNAtve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 404 ---------NKTVFDAVADGADLltvgkfeMPSRAYLgrfnfKGGDQNKIvGQ----LSGGERGRLHLAKTLIAGGNVLL 470
Cdd:cd03290 97 enitfgspfNKQRYKAVTDACSL-------QPDIDLL-----PFGDQTEI-GErginLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489917580 471 LDEPSNDLDVE-TLRALEDALLEF----PGSVMVISHDRWFL 507
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFlqddKRTLVLVTHKLQYL 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
337-504 |
1.27e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAgREQPDSGEVKLG---------QTVKLAY--VDQS-------- 397
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDgvswnsvtlQTWRKAFgvIPQKvfifsgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 RDSLEGNKTVFDA----VADGADLLTVGKfEMPsraylGRFNFKGGDQNKIvgqLSGGERGRLHLAKTLIAGGNVLLLDE 473
Cdd:TIGR01271 1309 RKNLDPYEQWSDEeiwkVAEEVGLKSVIE-QFP-----DKLDFVLVDGGYV---LSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190
....*....|....*....|....*....|..
gi 489917580 474 PSNDLDVETLRALEDALLE-FPGSVMVISHDR 504
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
344-503 |
1.32e-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: 48.51 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFkvPAGAIVGIIGPNGAGKSTLFR---MLAGREQPD---SGEVKLGQTVklAYVdqsrdSLEgnktvfdavadgadl 417
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILDaigLALGGAQSAtrrRSGVKAGCIV--AAV-----SAE--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 418 ltvgkfempsraylgrFNFkggdqnkIVGQLSGGERGRLHLAKTL----IAGGNVLLLDEPSNDLDVETLRALEDALLEF 493
Cdd:cd03227 71 ----------------LIF-------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEH 127
|
170
....*....|...
gi 489917580 494 PGS---VMVISHD 503
Cdd:cd03227 128 LVKgaqVIVITHL 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-197 |
1.38e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGlNIGYLPQEPELNPeHTVRQSVEEGLG----- 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-IKHSG-RISFSPQTSWIMP-GTIKDNIIFGLSydeyr 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 --AVFNAKQrLDEVYAAYAEPDadfdalaaeqaeleaviaaaassgaddiehqmeiaadalRLPPWDAMVgKLSGGEKRR 173
Cdd:TIGR01271 518 ytSVIKACQ-LEEDIALFPEKD---------------------------------------KTVLGEGGI-TLSGGQRAR 556
|
170 180
....*....|....*....|....
gi 489917580 174 VALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-524 |
1.54e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 17 PKRQILRDISLSFFPGAKIGVLGLNGSGKS-TLLKIM-----AGVDKEIEG--------EAIPMP-----------GLNI 71
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKmllrrrsrQVIELSeqsaaqmrhvrGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 72 GYLPQEP--ELNPEHTVRQSVEEGLgavfnakqRLDEvyaayaepdadfdALAAEQAELEAVIAAaassgaddiehqmei 149
Cdd:PRK10261 107 AMIFQEPmtSLNPVFTVGEQIAESI--------RLHQ-------------GASREEAMVEAKRML--------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 150 aaDALRLPPWDAMVGK----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK10261 151 --DQVRIPEAQTILSRyphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 222 RYFLDNAAEWILELDRGYGIpwkgnysswleqkeDRLKQEEATESARQKTIKKELEWVrqnPKGRQAKAKARIARFEELS 301
Cdd:PRK10261 229 MGVVAEIADRVLVMYQGEAV--------------ETGSVEQIFHAPQHPYTRALLAAV---PQLGAMKGLDYPRRFPLIS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 302 SYEYQKRN-ETQEIFIPVGD---RLGNEVIEF-------NHVSKaygDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFR 370
Cdd:PRK10261 292 LEHPAKQEpPIEQDTVVDGEpilQVRNLVTRFplrsgllNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 371 MLAGREQPDSGEVKL-GQTVKL--AYVDQS--RD----------SLEGNKTVFDAVADGADLLTVGKFEMPSRA---YLG 432
Cdd:PRK10261 369 ALLRLVESQGGEIIFnGQRIDTlsPGKLQAlrRDiqfifqdpyaSLDPRQTVGDSIMEPLRVHGLLPGKAAAARvawLLE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 433 RFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVeTLRA-----LEDALLEFPGSVMVISHDRWFL 507
Cdd:PRK10261 449 RVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiinlLLDLQRDFGIAYLFISHDMAVV 527
|
570
....*....|....*..
gi 489917580 508 DRIaTHILAFEGDSQVV 524
Cdd:PRK10261 528 ERI-SHRVAVMYLGQIV 543
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-200 |
1.87e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 1 MAQYVYTMNRVGKIVPPKRQILRDISLSFfPGAKIGVL-GLNGSGKSTLLKIMAGVDKEIEGEaipmpglnIGYLPQepe 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGK--------ISILGQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 lnpehTVRQSVEEGLGAVFNAKQRLDEVYAAYAEpDADFDALAAEQAELEAVIaaaassgaddiEHQMEIAADAL-RLPP 158
Cdd:PRK15056 70 -----PTRQALQKNLVAYVPQSEEVDWSFPVLVE-DVVMMGRYGHMGWLRRAK-----------KRDRQIVTAALaRVDM 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 159 WD---AMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 200
Cdd:PRK15056 133 VEfrhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
344-500 |
2.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKLGQTV---------------KLAYVDQSRDSLEGNKTVF 408
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 409 DAVADGADLLTVGKFEMPSRAyLGRFNFKGGDQN---KIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRA 485
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALA-REKLALVGISESlfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170
....*....|....*
gi 489917580 486 LEDALLEFPGSVMVI 500
Cdd:PRK13649 184 LMTLFKKLHQSGMTI 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-221 |
2.53e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIgylpqePELNPEH--TVRQ--SVEEGL 94
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGE-ILFDGENI------PAMSRSRlyTVRKrmSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 95 GAVFNAKQRLDEVyaayAEPDADFDALAAEqaeleaviaaaassgaddIEHQ---MEIAADALRLPPwDAMVGKLSGGEK 171
Cdd:PRK11831 93 GALFTDMNVFDNV----AYPLREHTQLPAP------------------LLHStvmMKLEAVGLRGAA-KLMPSELSGGMA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489917580 172 RRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITmgvlVKLISELNSALGVTCVVVSHD 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-193 |
2.79e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.72 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeAIPMPGLNIGYLP------QEPELNPEHT---VRQ 88
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSG-RIVFDGKDITDWQtakimrEAVAIVPEGRrvfSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 SVEEGL--GAVFNAK----QRLDEVYAAyaepdadFDALAAEQAEleaviaaaassgaddiehqmeiaadalrlppwdaM 162
Cdd:PRK11614 96 TVEENLamGGFFAERdqfqERIKWVYEL-------FPRLHERRIQ----------------------------------R 134
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 163 VGKLSGGEKRRVALCRLLLSKPDMLLLDEPT 193
Cdd:PRK11614 135 AGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-482 |
3.01e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.08 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 341 LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVKlgQTVKLAYVDQSRDSLEGN---------------- 404
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQFSWIMPGTikeniifgvsydeyry 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 405 KTVFDAVADGADLLtvgKFEMPSRAYLGrfnfKGGDqnkivgQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 482
Cdd:cd03291 130 KSVVKACQLEEDIT---KFPEKDNTVLG----EGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
342-532 |
3.69e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQP-DSGEVKLGQTVklAYVDQSrdSLEGNKTVFDAVADGADlltv 420
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSV--AYVPQV--SWIFNATVRENILFGSD---- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 421 gkFEmPSRaYLGRFN----------FKGGDQNKIvGQ----LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL 486
Cdd:PLN03232 705 --FE-SER-YWRAIDvtalqhdldlLPGRDLTEI-GErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489917580 487 EDALL--EFPGSVMV-ISHDRWFLDRIATHILAFEGdsqVVFFDGNYQE 532
Cdd:PLN03232 780 FDSCMkdELKGKTRVlVTNQLHFLPLMDRIILVSEG---MIKEEGTFAE 825
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
342-539 |
4.36e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.93 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTVKLAYVDQSRDSLEGNKTVF-DAVADGADLLT 419
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAVRSDIQMIFqDPLASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 420 VGK-FEMPSRAY---LGRFNFKGGDQNKI--VGQL-----------SGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV-- 480
Cdd:PRK15079 117 IGEiIAEPLRTYhpkLSRQEVKDRVKAMMlkVGLLpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVsi 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489917580 481 --ETLRALEDALLEFPGSVMVISHDRwfldRIATHIlafeGDSQVVFFDGN------YQEYEADKKH 539
Cdd:PRK15079 197 qaQVVNLLQQLQREMGLSLIFIAHDL----AVVKHI----SDRVLVMYLGHavelgtYDEVYHNPLH 255
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
166-199 |
6.46e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.54 E-value: 6.46e-06
10 20 30
....*....|....*....|....*....|....
gi 489917580 166 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE 199
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-239 |
7.04e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 7 TMNRVGKIVPP--KRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DK------EIEGEAIPMPG------- 68
Cdd:PRK09984 3 TIIRVEKLAKTfnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKsagshiELLGRTVQREGrlardir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 69 ---LNIGYLPQEPELNPEHTVRQSVEEG-LGAV---------FNAKQRLDEVYAAYAEPDADFdalaaeqaeleaviaaa 135
Cdd:PRK09984 83 ksrANTGYIFQQFNLVNRLSVLENVLIGaLGSTpfwrtcfswFTREQKQRALQALTRVGMVHF----------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 136 assgaddiEHQMeiaadalrlppwdamVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG-- 213
Cdd:PRK09984 146 --------AHQR---------------VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnd 202
|
250 260
....*....|....*....|....*...
gi 489917580 214 --TVVAVTHDRYFLDNAAEWILELDRGY 239
Cdd:PRK09984 203 giTVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
332-502 |
7.11e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 332 VSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK-LGQTVKLAyvdQSRDSLEGNKTVFDa 410
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIDFK---SSKEALENGISMVH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 411 vadgADLLTVGKFEMPSRAYLGRFNFKGG--DQNKI--------------------VGQLSGGERGRLHLAKTLIAGGNV 468
Cdd:PRK10982 80 ----QELNLVLQRSVMDNMWLGRYPTKGMfvDQDKMyrdtkaifdeldididprakVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 489917580 469 LLLDEPSNDL---DVETLRALEDALLEFPGSVMVISH 502
Cdd:PRK10982 156 VIMDEPTSSLtekEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
342-383 |
1.09e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 1.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489917580 342 IDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV 383
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-502 |
1.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.39 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 323 GNEVIEFNHVSKAYGD------RLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVklgqtvklaYVDQ 396
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------YVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 397 SRDSLEGN---------------------KTVFDAVADGADLLTVGKFEMPSRA-----YLGRFNFKGGDQNkivgQLSG 450
Cdd:PRK13633 72 LDTSDEENlwdirnkagmvfqnpdnqivaTIVEEDVAFGPENLGIPPEEIRERVdeslkKVGMYEYRRHAPH----LLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 451 GERGRLHLAKTLIAGGNVLLLDEPSNDLD----VETLRALEDALLEFPGSVMVISH 502
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-229 |
1.21e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 142 DIEHQMEIAADALRLPPWDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES---------VEWLEQFLHKFP 212
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKN 116
|
90
....*....|....*..
gi 489917580 213 GTVVAVTHDRYFLDNAA 229
Cdd:smart00382 117 LTVILTTNDEKDLGPAL 133
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-198 |
1.25e-05 |
|
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: 48.40 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 16 PPKrqiLRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGlNIGYLPQEPELNPEhTVRQSVEEGlg 95
Cdd:TIGR00957 651 PPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH-VHMKG-SVAYVPQQAWIQND-SLRENILFG-- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 avfnaKQRLDEVYAAYAEPdadfdalAAEQAELEAVIAAAassgaddiehQMEIAADALrlppwdamvgKLSGGEKRRVA 175
Cdd:TIGR00957 723 -----KALNEKYYQQVLEA-------CALLPDLEILPSGD----------RTEIGEKGV----------NLSGGQKQRVS 770
|
170 180
....*....|....*....|...
gi 489917580 176 LCRLLLSKPDMLLLDEPTNHLDA 198
Cdd:TIGR00957 771 LARAVYSNADIYLFDDPLSAVDA 793
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
166-241 |
1.25e-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: 45.78 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 LSGGEKRRVALCRLLLS--KPDMLLLDEPTNHLDAESvewLEQFLHKFPG------TVVAVTHDRYFLDnAAEWILELDR 237
Cdd:cd03238 88 LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLS-SADWIIDFGP 163
|
....
gi 489917580 238 GYGI 241
Cdd:cd03238 164 GSGK 167
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
160-208 |
1.35e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489917580 160 DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL 208
Cdd:PRK13543 132 DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
159-221 |
1.52e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.70 E-value: 1.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 159 WDAMVGKL-------SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKFPG--TVVAVTHD 221
Cdd:PRK14243 138 WDEVKDKLkqsglslSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-197 |
1.53e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.51 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 14 IVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-DKEIEGEaIPMPG--LNIGYLPQEPE----LNPEHTV 86
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGN-VFINGkpVDIRNPAQAIRagiaMVPEDRK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGLGAVFNAKQRLDEVYAAYAEPDAdfdalAAEQAELEAVIaaaassgaddieHQMEIAADALRLPpwdamVGKL 166
Cdd:TIGR02633 347 RHGIVPILGVGKNITLSVLKSFCFKMRIDA-----AAELQIIGSAI------------QRLKVKTASPFLP-----IGRL 404
|
170 180 190
....*....|....*....|....*....|.
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-221 |
1.82e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAIpMPGLNIGYLPqepelnpEHTVRQSVEEGLGAVFNAK 101
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL-IDGVDIAKIS-------DAELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 102 QRLDEVYAAyaepdaDFDALAAEQAELEAviaaaassgaddiEHQMEIAADALRLPPWDAMV----GKLSGGEKRRVALC 177
Cdd:PRK10070 116 ALMPHMTVL------DNTAFGMELAGINA-------------EERREKALDALRQVGLENYAhsypDELSGGMRQRVGLA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489917580 178 RLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK10070 177 RALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-221 |
2.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.54 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 13 KIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAI----PMPGlNIGYLPQEPELNPEhtvrq 88
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyAIPA-NLKKIKEVKRLRKE----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 89 sveegLGAVFNAKQRldEVYAAYAEPDADFDA--LAAEQAELeaviaaaaSSGADDIEHQMEIAADALRLPPWDamvgkL 166
Cdd:PRK13645 92 -----IGLVFQFPEY--QLFQETIEKDIAFGPvnLGENKQEA--------YKKVPELLKLVQLPEDYVKRSPFE-----L 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 167 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVE----WLEQFLHKFPGTVVAVTHD 221
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHN 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-200 |
2.24e-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: 47.70 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 31 PGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA----------IPMPGLNIGYLPQEPELNPEHTVRQSVEeglgavfna 100
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAtvagksiltnISDVHQNMGYCPQFDAIDDLLTGREHLY--------- 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 101 kqrldeVYAAyaepdadFDALAAEQaeleaviaaaassgaddIEHQMEIAADALRLPPW-DAMVGKLSGGEKRRVALCRL 179
Cdd:TIGR01257 2035 ------LYAR-------LRGVPAEE-----------------IEKVANWSIQSLGLSLYaDRLAGTYSGGNKRKLSTAIA 2084
|
170 180
....*....|....*....|.
gi 489917580 180 LLSKPDMLLLDEPTNHLDAES 200
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQA 2105
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-221 |
2.45e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 11 VGKIVPPKRQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNIGYLpqEPE----------- 79
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGGRVVNEL--EPAdrdiamvfqny 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 -LNPEHTVRQSVEEGLgavfnaKQRldevyaayaepdadfdalaaeqaeleaviaaaaSSGADDIEHQMEIAADALRLPP 158
Cdd:PRK11650 86 aLYPHMSVRENMAYGL------KIR---------------------------------GMPKAEIEERVAEAARILELEP 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 159 W-DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-----SVEWLEqfLHKFPGTV-VAVTHD 221
Cdd:PRK11650 127 LlDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrvqmRLEIQR--LHRRLKTTsLYVTHD 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-110 |
2.86e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKST-LLKIMAGVdkEIEGEAIPMPGLNIG------------YLPQEPELNpEHTVR 87
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTlLLTFMRMV--EVCGGEIRVNGREIGayglrelrrqfsMIPQDPVLF-DGTVR 1401
|
90 100
....*....|....*....|...
gi 489917580 88 QSVEEGLGAvfnakqRLDEVYAA 110
Cdd:PTZ00243 1402 QNVDPFLEA------SSAEVWAA 1418
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-222 |
3.03e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 21 ILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEaIPMPGLNIGYLPQEPELNPEHTVRQSVEEGLGAVfna 100
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGD-IQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 101 KQRLDEvYAAYAEPDAdfdALAAEQAELEAVIAAAAssgaDDIEHQMEIAADALrlppwdamvgklSGGEKRRVALCRLL 180
Cdd:cd03289 94 RKNLDP-YGKWSDEEI---WKVAEEVGLKSVIEQFP----GQLDFVLVDGGCVL------------SHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489917580 181 LSKPDMLLLDEPTNHLDAESVEWLEQFL-HKFPGTVVAVTHDR 222
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
165-229 |
3.37e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.88 E-value: 3.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 165 KLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAVTHDryfLDNAA 229
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
334-503 |
3.80e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 334 KAYGDRLLIDdlsFkvpAGAIVGIIGPNGAGKSTLFR----MLAG-------------REQPDSGEVKL----------- 385
Cdd:COG0419 11 RSYRDTETID---F---DDGLNLIVGPNGAGKSTILEairyALYGkarsrsklrsdliNVGSEEASVELefehggkryri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 386 ----GQTVKLAYVDQS--RDSLEG--NKTVFDAVADGADLL---------TVGKFEMPSRAYLGRFNFKGGdqnkiVGQL 448
Cdd:COG0419 85 errqGEFAEFLEAKPSerKEALKRllGLEIYEELKERLKELeealesaleELAELQKLKQEILAQLSGLDP-----IETL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 449 SGGERGRLHLAKTLiaggnVLLLDEPSndLDVETLRALEDALLEfpgsVMVISHD 503
Cdd:COG0419 160 SGGERLRLALADLL-----SLILDFGS--LDEERLERLLDALEE----LAIITHV 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
320-384 |
4.55e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 4.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 320 DRLGNEVIEFNHVSKAYGdrllIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEVK 384
Cdd:PRK13546 22 ERMKDALIPKHKNKTFFA----LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
344-502 |
4.75e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV--KLGQTVKLA-----YVDQSRdSLEGNKTVFDAVADGAD 416
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyyKNCNINNIAkpyctYIGHNL-GLKLEMTVFENLKFWSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 417 LltvgkFEMPSRAYLGRFNFKGGD-QNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETlRALEDALLEFP- 494
Cdd:PRK13541 97 I-----YNSAETLYAAIHYFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-RDLLNNLIVMKa 170
|
170
....*....|.
gi 489917580 495 ---GSVMVISH 502
Cdd:PRK13541 171 nsgGIVLLSSH 181
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
326-486 |
5.59e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.98 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 326 VIEFNHVSKAYGDRL-LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV-----------KLGQTVKL-A 392
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 393 YVDQSRDSLEGNKTVFDAVADGADLLTVGKFEMPSRA-------YLGRFNFKGGDqnkivgQLSGGERGRLHLAKTLIAG 465
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVdralaeiGLEKYRHRSPK------TLSGGQGQCVALAGILTME 154
|
170 180
....*....|....*....|.
gi 489917580 466 GNVLLLDEPSNDLDVETLRAL 486
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAV 175
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-232 |
5.71e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 32 GAKIGVLGLNGSGKSTLLKIMAGVDKEiEGEAIPMPGLNIGYLPQEPelnpehtvrqsveeglgavfnakqrldevyaay 111
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIP-NGDNDEWDGITPVYKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 112 aepdadfdalaaeqaeleaviaaaassgaddiehqmeiaadalrlppwdamvgKLSGGEKRRVALCRLLLSKPDMLLLDE 191
Cdd:cd03222 71 -----------------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDE 97
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489917580 192 PTNHLDAE----SVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWI 232
Cdd:cd03222 98 PSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
338-510 |
6.34e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 338 DRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGRE--QPDSGEVKLGQTVKLAYVDQSRdsleGNKTVFDAVADGA 415
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDR----AGEGIFMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 416 DLLTVG-KFEMPS-----RAY-----LGRFNFKGGDQNKI---------------VGqLSGGERGRLHLAKTLIAGGNVL 469
Cdd:PRK09580 89 EIPGVSnQFFLQTalnavRSYrgqepLDRFDFQDLMEEKIallkmpedlltrsvnVG-FSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489917580 470 LLDEPSNDLDVETLRALE---DALLEFPGSVMVISHDRWFLDRI 510
Cdd:PRK09580 168 ILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-202 |
7.91e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 43.57 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAIPMPglnigylpqepelnpehTVRQSVEEGLG 95
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpasgeiTLDGKPVTRR-----------------SPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 96 AVfnAKQRLDEvyaayaepdadfdALAAEQaeleaviaaaassgadDIEHQMEIAADalrlppwdamvgkLSGGEKRRVA 175
Cdd:cd03215 79 YV--PEDRKRE-------------GLVLDL----------------SVAENIALSSL-------------LSGGNQQKVV 114
|
170 180
....*....|....*....|....*..
gi 489917580 176 LCRLLLSKPDMLLLDEPTNHLDAESVE 202
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKA 141
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
325-538 |
8.70e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.38 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 325 EVIEFNHVSKAYGDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLaGREQPDSGEVKLGQTVKL----AYVDQSrDS 400
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghnIYSPRT-DT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 401 LEGNK--------------TVFDAVADGADLLTVGKFEMPSRAYlgRFNFKGG---DQNK------IVGqLSGGERGRLH 457
Cdd:PRK14239 82 VDLRKeigmvfqqpnpfpmSIYENVVYGLRLKGIKDKQVLDEAV--EKSLKGAsiwDEVKdrlhdsALG-LSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 458 LAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDRIAthilafegDSQVVFFDGNYQEYEA 535
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRIS--------DRTGFFLDGDLIEYND 230
|
...
gi 489917580 536 DKK 538
Cdd:PRK14239 231 TKQ 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-221 |
1.07e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 24 DISLSFFPGAKIGVLGLNGSGKS-TLLKIMAGVDK--EIEGEAI---------PMPGLN------IGYLPQEP--ELNPe 83
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATfngreilnlPEKELNklraeqISMIFQDPmtSLNP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 htvRQSVEEGLGAVFNAKQRLDEVyAAYAEPDADFDALaaeqaeleaviaaaassgaddiehQMEIAADALRLPPWDamv 163
Cdd:PRK09473 113 ---YMRVGEQLMEVLMLHKGMSKA-EAFEESVRMLDAV------------------------KMPEARKRMKMYPHE--- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 164 gkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK09473 162 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
160-197 |
1.30e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 1.30e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489917580 160 DAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-254 |
1.39e-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: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAipmpglnigYLPQEPELNPEHTV-RQSVeeglgav 97
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDGRPLSSLSHSVlRQGV------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 98 fnAKQRLDEVYAAyaepDADFDALAAEQaeleaviaaaassgadDI-EHQMEIAADALRLPPW--------DAMVGK--- 165
Cdd:PRK10790 418 --AMVQQDPVVLA----DTFLANVTLGR----------------DIsEEQVWQALETVQLAELarslpdglYTPLGEqgn 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 166 -LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFLHKF--PGTVVAVTHdRYFLDNAAEWILELDRGYGIP 242
Cdd:PRK10790 476 nLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH-RLSTIVEADTILVLHRGQAVE 554
|
250
....*....|..
gi 489917580 243 wKGNYSSWLEQK 254
Cdd:PRK10790 555 -QGTHQQLLAAQ 565
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
344-515 |
1.70e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 344 DLSFKVPAGAIVGIIGPNGAGKS-----TLFRMLAG---REQPDSGEVK----LGQTVKLAYVDQS-------------- 397
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSslindTLYPALARrlhLKKEQPGNHDriegLEHIDKVIVIDQSpigrtprsnpatyt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 398 --------------------RDSLE---GNKTVFDAVAdgadlLTVGK----FEMPSR--AYLGRFNFKGGDQNKIvGQ- 447
Cdd:cd03271 93 gvfdeirelfcevckgkrynRETLEvryKGKSIADVLD-----MTVEEalefFENIPKiaRKLQTLCDVGLGYIKL-GQp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 448 ---LSGGERGRLHLAKTL--IAGGNVL-LLDEPSNDL---DVETLRALEDALLEFPGSVMVISHDrwfLD--RIATHIL 515
Cdd:cd03271 167 attLSGGEAQRIKLAKELskRSTGKTLyILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDviKCADWII 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-221 |
1.71e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.44 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 18 KRQILRDISLSFFPGAKIGVLGLNGSGKSTLL----KIMAGVDKEI--EGEAIPM-----PGLNIGYLPQEPELNPEHTV 86
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLrtlsRLMTPAHGHVwlDGEHIQHyaskeVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 87 RQSVEEGL---GAVFNAKQRLDEVYAAYAEPDADFDALAAEQaeleaviaaaassgaddiehqmeiaadalrlppwdamV 163
Cdd:PRK10253 99 QELVARGRyphQPLFTRWRKEDEEAVTKAMQATGITHLADQS-------------------------------------V 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 164 GKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEQF--LHKFPG-TVVAVTHD 221
Cdd:PRK10253 142 DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLELLseLNREKGyTLAAVLHD 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
327-535 |
2.62e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRL--LIDDLSFKVPAGAIVGIIGPNGAGKST----LFRMLA---GREQPDSGEV-KLGQT---VKLAY 393
Cdd:PLN03232 1235 IKFEDVHLRYRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVElekGRIMIDDCDVaKFGLTdlrRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 394 VDQSRDSLEGN-KTVFDAVADGADlltVGKFEMPSRAYLG---RFNFKGGDQNKIVG--QLSGGERGRLHLAKTLIAGGN 467
Cdd:PLN03232 1315 IPQSPVLFSGTvRFNIDPFSEHND---ADLWEALERAHIKdviDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 468 VLLLDEPSNDLDVETlraleDALL------EFPGSVM-VISHdrwfldRIATHIlafEGDSQVVFFDGNYQEYEA 535
Cdd:PLN03232 1392 ILVLDEATASVDVRT-----DSLIqrtireEFKSCTMlVIAH------RLNTII---DCDKILVLSSGQVLEYDS 1452
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-200 |
3.25e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaIPMPGLNI--------GYLPQEPELNPEHTvrqsVEEG 93
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGN-IYYKNCNInniakpycTYIGHNLGLKLEMT----VFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 LgaVFNAK--QRLDEVYAAYaepdadfdalaaeqaeleaviaaaassgaddieHQMEIaADALrlppwDAMVGKLSGGEK 171
Cdd:PRK13541 91 L--KFWSEiyNSAETLYAAI---------------------------------HYFKL-HDLL-----DEKCYSLSSGMQ 129
|
170 180
....*....|....*....|....*....
gi 489917580 172 RRVALCRLLLSKPDMLLLDEPTNHLDAES 200
Cdd:PRK13541 130 KIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
165-226 |
3.49e-04 |
|
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: 42.76 E-value: 3.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 165 KLSGGEKR---RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL---HKFPGTVVAVTHDRYFLD 226
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTTHSPLLLD 303
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-197 |
3.58e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.03 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 6 YTMNRvGKIVPPKR-QILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE--------AIPMPGL------N 70
Cdd:PRK11308 15 YPVKR-GLFKPERLvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdlLKADPEAqkllrqK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 71 IGYLPQEP--ELNPEHTVRQSVEEGL--GAVFNAKQRLDEVYAAYAEPdadfdALAAEQAEleaviaaaassgaddiehq 146
Cdd:PRK11308 94 IQIVFQNPygSLNPRKKVGQILEEPLliNTSLSAAERREKALAMMAKV-----GLRPEHYD------------------- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489917580 147 meiaadalRLPpwdAMvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 197
Cdd:PRK11308 150 --------RYP---HM---FSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
343-374 |
3.74e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 3.74e-04
10 20 30
....*....|....*....|....*....|..
gi 489917580 343 DDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG 374
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
337-374 |
3.87e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 3.87e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAG 374
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
166-228 |
4.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917580 166 LSGGEkrRVAL---CRLLLS-----KPDMLLLDEPTNHLDAES----VEWLEQFLHKFPgTVVAVTHDRYFLDNA 228
Cdd:PRK03918 789 LSGGE--RIALglaFRLALSlylagNIPLLILDEPTPFLDEERrrklVDIMERYLRKIP-QVIIVSHDEELKDAA 860
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
327-551 |
7.25e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 327 IEFNHVSKAYGDRL-----LIDDLSFKVPAGAIVGIIGPNGAGKSTLFRMLAGREQPDSGEV-------KLGQTVKLAYV 394
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 395 DQSRDSLEGNK----------------------------TVFDAVADGADLLTVGKFEMPSRA------------YLGRF 434
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAakyielvgldesYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 435 NFkggdqnkivgQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD---VETLRALEDALLEFPGSVMVISHDrwfLDRI- 510
Cdd:PRK13651 163 PF----------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVl 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489917580 511 --ATHILAFEgDSQVVfFDGNYQEYEADKKHrLGEEGAKPKRL 551
Cdd:PRK13651 230 ewTKRTIFFK-DGKII-KDGDTYDILSDNKF-LIENNMEPPKL 269
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-238 |
7.99e-04 |
|
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: 42.09 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdkeiegeaipmpglnigYLPQEPELN------PEHTV---RQ--Sveeg 93
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL-----------------YRPESGEILldgqpvTADNReayRQlfS---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 94 lgAVFnAKQRL-DEVYAAYAEPDadfDALAAEQ-AELEaviaaaassgaddIEHQMEIAADAL-RLppwdamvgKLSGGE 170
Cdd:COG4615 410 --AVF-SDFHLfDRLLGLDGEAD---PARARELlERLE-------------LDHKVSVEDGRFsTT--------DLSQGQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 171 KRRVALCRLLLSKPDMLLLDE------PtnhldaesvewleQFLHKF-----P-----G-TVVAVTHD-RYFldNAAEWI 232
Cdd:COG4615 463 RKRLALLVALLEDRPILVFDEwaadqdP-------------EFRRVFytellPelkarGkTVIAISHDdRYF--DLADRV 527
|
....*.
gi 489917580 233 LELDRG 238
Cdd:COG4615 528 LKMDYG 533
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
166-235 |
1.07e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 166 LSGGEKRRVALCRLLLSK---PDMLLLDEPTNHLDAESVEWLEQFLHKFPG---TVVAVTHDryfLD--NAAEWILEL 235
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkgnTVVVIEHN---LDviKTADYIIDL 904
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-62 |
1.12e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE 62
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
166-235 |
1.14e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 166 LSGGEKRRVALCRLLlSKPD----MLLLDEPTNHLDAESVEWLEQFLHKFP---GTVVAVTHDryfLD--NAAEWILEL 235
Cdd:cd03271 170 LSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVdkgNTVVVIEHN---LDviKCADWIIDL 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
337-511 |
1.30e-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: 41.59 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 337 GDRLLIDDLSFKVPAGAIVGIIGPNGAGKS----TLFRMLAGREQPDSGEVKLGQTVKLAYVDQSRDSLEGNK------- 405
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRiamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 406 ---------TVFDAVA---------DGA-------DLLT-VGKFEMPSRayLGRFNFkggdqnkivgQLSGGERGRLHLA 459
Cdd:COG4172 101 pmtslnplhTIGKQIAevlrlhrglSGAaararalELLErVGIPDPERR--LDAYPH----------QLSGGQRQRVMIA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 460 KTLIAGGNVLLLDEPSNDLDVeTLRA--LEdaLL-----EFPGSVMVISHD----RWFLDRIA 511
Cdd:COG4172 169 MALANEPDLLIADEPTTALDV-TVQAqiLD--LLkdlqrELGMALLLITHDlgvvRRFADRVA 228
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
354-543 |
1.96e-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: 40.45 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 354 IVGIIGPNGAGKSTLFRML--AGREQPDSGEVKLGQTVKLAYVDQSRDSLEGNKtvfdavaDGADLLTVGKFEMPSRAYL 431
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALrfLADFDALVIGLTDERSRNGGIGGIPSLLNGIDP-------KEPIEFEISEFLEDGVRYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 432 GRFNFKGGDQNKIVGQLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFPG--SVMVISHDRWFLDR 509
Cdd:pfam13304 74 YGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDliSGLLLLSIISPLSF 153
|
170 180 190
....*....|....*....|....*....|....
gi 489917580 510 IATHILAFEGDSQVVFFDGNYQEYEADKKHRLGE 543
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
447-511 |
2.56e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 2.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 447 QLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFPGSVMVISHD----RWFLDRIA 511
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNlsivRKLADRVA 228
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-61 |
2.81e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 2.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489917580 22 LRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEG 61
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
164-439 |
3.07e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 164 GKLSGGEKRRVALCRLLLSKPD--MLLLDEPTNHLDAESVEWLEQF---LHKFPGTVVAVTHDRYFLdNAAEWILELDRG 238
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTlkrLRDLGNTLIVVEHDEDTI-RAADYVIDIGPG 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 239 YGIpwkgnysswleqkedrlkqeEATESARQKTikkeLEWVRQNPKgrqakakariarfeelsSYEYQKRNETQEIFIPV 318
Cdd:TIGR00630 566 AGE--------------------HGGEVVASGT----PEEILANPD-----------------SLTGQYLSGRKKIEVPA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 319 GDRLGN-EVIEfnhVSKAYGDRLliDDLSFKVPAGAIVGIIGPNGAGKSTLF----------RMLAGREQPDSGE--VKL 385
Cdd:TIGR00630 605 ERRPGNgKFLT---LKGARENNL--KNITVSIPLGLFTCITGVSGSGKSTLIndtlypalanRLNGAKTVPGRYTsiEGL 679
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489917580 386 GQTVKLAYVDQS---RDSLEGNKT---VFDAVADgadlLTVGKFEMPSRAY-LGRFNF--KGG 439
Cdd:TIGR00630 680 EHLDKVIHIDQSpigRTPRSNPATytgVFDEIRE----LFAETPEAKVRGYtPGRFSFnvKGG 738
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-202 |
3.98e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 19 RQILRDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-DKEIEGEAIPMPGLNIgylpqePELNPEHTVRQSV------- 90
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGReDYEVTGGTVEFKGKDL------LELSPEDRAGEGIfmafqyp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 91 --EEGLGAVFNAKQRLDEVYAAYAEPDAD-FDalaaeqaeleaviaaaassGADDIEHQMEIaadaLRLPPwDAM----- 162
Cdd:PRK09580 88 veIPGVSNQFFLQTALNAVRSYRGQEPLDrFD-------------------FQDLMEEKIAL----LKMPE-DLLtrsvn 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489917580 163 VGkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVE 202
Cdd:PRK09580 144 VG-FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALK 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
442-503 |
4.21e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489917580 442 NKIVGQLSGGERGRLHLAKTLIAG--GNVLLLDEPS-------NDLDVETLRALEDalleFPGSVMVISHD 503
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSiglhqrdNRRLINTLKRLRD----LGNTLIVVEHD 549
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
446-512 |
4.81e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489917580 446 GQ----LSGGERGRLHLAKTL--IAGGNVL-LLDEPSNDL---DVETL-RALeDALLEFPGSVMVISHDrwfLDRIAT 512
Cdd:COG0178 821 GQpattLSGGEAQRVKLASELskRSTGKTLyILDEPTTGLhfhDIRKLlEVL-HRLVDKGNTVVVIEHN---LDVIKT 894
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-221 |
6.31e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.53 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 15 VPPKRQILRDISLSFFPGAKIGVLGLNGSGKS----TLLKIM-AGVDKE-----IEGEAI---PMPGLNIGYLPQEPE-- 79
Cdd:PRK10418 12 LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTagrvlLDGKPVapcALRGRKIATIMQNPRsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 80 LNPEHTVRQSVEEGLGAVfnAKQRLDEVYAAyaepdadfdalAAEQAELEAviaaaassgaddiehqmeiAADALRLPPW 159
Cdd:PRK10418 92 FNPLHTMHTHARETCLAL--GKPADDATLTA-----------ALEAVGLEN-------------------AARVLKLYPF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489917580 160 DamvgkLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEQFLHKFPGTVVAVTHD 221
Cdd:PRK10418 140 E-----MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHD 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
164-221 |
6.64e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 38.43 E-value: 6.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917580 164 GKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEQFL----HKFPGTVVAVTHD 221
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHD 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-233 |
6.87e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.95 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 25 ISLSFFPGAKIGVLGLNGSGKS-TLLKIMAGVD------------------KEIEGEAIPMPGLNIGYLPQEP--ELNPE 83
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvmaeklefngqdlqRISEKERRNLVGAEVAMIFQDPmtSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917580 84 HTVRQSVEEGL-----GAVFNAKQRldevyaayaepdadfdALaaeqaeleaviaaaassgadDIEHQMEIAADALRLpp 158
Cdd:PRK11022 106 YTVGFQIMEAIkvhqgGNKKTRRQR----------------AI--------------------DLLNQVGIPDPASRL-- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489917580 159 wDAMVGKLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEQFLHKFPGTVVAVTHDRYFLDNAAEWIL 233
Cdd:PRK11022 148 -DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| |
